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  • 1
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    Design and function of superfast muscles : new insights into the physiology of skeletal muscle (2005)
    Annual Reviews
    Details
    Publication Date: 2022-05-25
    Description: First published online as a Review in Advance on October 24, 2005. (Some corrections may occur before final publication online and in print)
    Description: Author Posting. © Annual Reviews, 2005. This article is posted here by permission of Annual Reviews for personal use, not for redistribution. The definitive version was published in Annual Review of Physiology 68 (2006): 22.1-22.29, doi:10.1146/annurev.physiol.68.040104.105418.
    Description: Superfast muscles of vertebrates power sound production. The fastest, the swimbladder muscle of toadfish, generates mechanical power at frequencies in excess of 200 Hz. To operate at these frequencies, the speed of relaxation has had to increase approximately 50-fold. This increase is accomplished by modifications of three kinetic traits: (a) a fast calcium transient due to extremely high concentration of sarcoplasmic reticulum (SR)-Ca2+ pumps and parvalbumin, (b) fast off-rate of Ca2+ from troponin C due to an alteration in troponin, and (c) fast cross-bridge detachment rate constant (g, 50 times faster than that in rabbit fast-twitch muscle) due to an alteration in myosin. Although these three modifications permit swimbladder muscle to generate mechanical work at high frequencies (where locomotor muscles cannot), it comes with a cost: The high g causes a large reduction in attached force-generating cross-bridges, making the swimbladder incapable of powering low-frequency locomotory movements. Hence the locomotory and sound-producing muscles have mutually exclusive designs.
    Description: This work was made possible by support from NIH grants AR38404 and AR46125 as well as the University of Pennsylvania Research Foundation.
    Keywords: Parvalbumin ; Ca2+ release ; Ca2+ uptake ; Cross-bridges ; Adaptation ; Sound production ; Whitman Center
    Repository Name: Woods Hole Open Access Server
    Type: Article
    Format: 567086 bytes
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  • 2
    Electronic Resource
    Electronic Resource
    Excitation-contraction coupling in a pre-vertebrate twitch muscle: The myotomes of Branchiostoma lanceolatum (1992)
    Springer
    The journal of membrane biology 129 (1992), S. 237-252 
    Details
    ISSN: 1432-1424
    Keywords: muscle ; excitation-contraction coupling ; ryanodine receptor ; Ca2+ current ; dihydropyridine receptor ; Ca2+ release
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The segmented trunk muscle (myotome muscle) of the lancelet (Branchiostoma lanceolatum), a pre-vertebrate chordate, was studied in order to gain information regarding the evolution of excitation-contraction (EC) coupling. Myotome membrane vesicles could be separated on isopycnic sucrose gradients into two main fractions, probably comprising solitary microsomes and diads of plasma membrane and sarcoplasmic reticulum, respectively. Both fractions bound the dihydropyridine PN 200/110 and the phenylalkylamine (−)D888 (devapamil) while specific ryanodine binding was observed in the diad preparation only. Pharmacological effects on Ca2+ currents measured under voltage-clamp conditions in single myotome fibers included a weak block by the dihydropyridine nifedipine and a shift of the voltage dependences of inactivation and restoration to more negative potentials by (−)D888. After blocking the Ca2+ current by cadmium in voltage-clamped single fibers, the contractile response persisted and a rapid intramembrane charge movement could be demonstrated. Both responses exhibited a voltage sensitivity very similar to the one of the voltage-activated Ca2+ channels. Our biochemical and electrophysiological results indicate that the EC coupling mechanism of the protochordate myotome cell is similar to that of the vertebrate skeletal muscle fiber: Intracellular Ca2+ release, presumably taking place via the ryanodine receptor complex, is under control of the cell membrane potential. The sarcolemmal Ca2+ channels might serve as voltage sensors for this process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00232906
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  • 3
    Electronic Resource
    Electronic Resource
    Mechanism of calcium release from skeletal sarcoplasmic reticulum (1982)
    Springer
    The journal of membrane biology 66 (1982), S. 193-201 
    Details
    ISSN: 1432-1424
    Keywords: sarcoplasmic reticulum ; Ca2+ release ; excitation-contraction coupling ; muscular contraction ; valinomycin ; ruthenium red
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Ca2+-induced Ca2+ release at the terminal cisternae of skeletal sarcoplasmic reticulum was demonstrated using heavy sarcoplasmic reticulum vesicles. Ca2+ release was observed at 10 μm Ca2+ in the presence of 1.25mm free Mg2+ and was sensitive to low concentrations of ruthenium red and was partially inhibited by valinomycin. These results suggest that the Ca2+-induced Ca2+ release is electrogenic and that an inside negative membrane potential created by the Ca2+ flux opens a second channel that releases Ca2+. Results in support of this formulation were obtained by applying a Cl− gradient or K+ gradient to sarcoplasmic reticulum vesicles to initiate Ca2+ release. Based on experiments the following hypothesis for the excitation-contraction coupling of skeletal muscle was formulated. On excitation, small amounts of Ca2+ enter from the transverse tubule and interact with a Ca2+ receptor at the terminal cisternae and cause Ca2+ release (Ca2+-induced Ca2+ release). This Ca2+ flux generates an inside negative membrane potential which opens voltage-gated Ca2+ channels (membrane potential-dependent Ca2+ release) in amounts sufficient for contraction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868494
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  • 4
    Electronic Resource
    Electronic Resource
    Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories (1992)
    Springer
    Journal of molecular evolution 34 (1992), S. 416-448 
    Details
    ISSN: 1432-1432
    Keywords: EF-hand ; Calcium binding protein ; Gene duplication ; Congruence ; Domain transposition ; Calmodulin ; Troponin C ; Light chains of myosin ; Parvalbumin ; S100 ; Calpain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In the first report in this series we described the relationships and evolution of 152 individual proteins of the EF-hand subfamilies. Here we add 66 additional proteins and define eight (CDC, TPNV, CLNB, LPS, DGK, 1 F8, VIS, TCBP) new subfamilies and seven (CAL, SQUD, CDPK, EFH5, TPP, LAV, CRGP) new unique proteins, which we assume represent new subfamilies. The main focus of this study is the classification of individual EF-hand domains. Five subfamilies—calmodulin, troponin C, essential light chain, regulatory light chain, CDC31/caltractin-and three uniques—call, squidulin, and calcium-dependent protein kinase-are congruent in that all evolved from a common four-domain precursor. In contrast calpain and sarcoplasmic calcium-binding protein (SARC) each evolved from its own one-domain precursor. The remaining 19 subfamilies and uniques appear to have evolved by translocation and splicing of genes encoding the EF-hand domains that were precursors to the congruent eight and to calpain and to SARC. The rates of evolution of the EF-hand domains are slower following formation of the subfamilies and establishment of their functions. Subfamilies are not readily classified by patterns of calcium coordination, interdomain linker stability, and glycine and proline distribution. There are many homoplasies indicating that similar variants of the EF-hand evolved by independent pathways.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00162998
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  • 5
    Electronic Resource
    Electronic Resource
    Endogenous, Ca2+-dependent cysteine-protease cleaves specifically the ryanodine receptor/Ca2+ release channel in skeletal muscle (1994)
    Springer
    The journal of membrane biology 142 (1994), S. 281-288 
    Details
    ISSN: 1432-1424
    Keywords: Ryanodine receptor ; Ca2+ release channel ; Calpain ; Junctional sarcoplasmic reticulum ; Ca2+ release
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The association of an endogenous, Ca2+-dependent cysteine-protease with the junctional sarcoplasmic reticulum (SR) is demonstrated. The activity of this protease is strongly stimulated by dithiothreitol (DTT), cysteine and β-mercaptoethanol, and is inhibited by iodoacetamide, mercuric chloride and leupeptin, but not by PMSF. The activity of this thiol-protease is dependent on Ca2+ with half-maximal activity obtained at 0.1 μm and maximal activity at 10 μm. Mg2+ is also an activator of this enzyme (CI50=22 μm). These observations, together with the neutral pH optima and inhibition by the calpain I inhibitor, suggest that this enzyme is of calpain I type. This protease specifically cleaves the ryanodine receptor monomer (510 kD) at one site to produce two fragments with apparent molecular masses of 375 and 150 kD. The proteolytic fragments remain associated as shown by purification of the cleaved ryanodine receptor. The calpain binding site is identified as a PEST (proline, glutamic acid, serine, threonine-rich) region in the amino acid sequence GTPGGTPQPGVE, at positions 1356–1367 of the RyR and the cleavage site, the calmodulin binding site, at residues 1383–1400. The RyR cleavage by the Ca2+-dependent thiol-protease is prevented in the presence of ATP (1–5 mm) and by high NaCl concentrations. This cleavage of the RyR has no effect on ryanodine binding activity but stimulates Ca2+ efflux. A possible involvement of this specific cleavage of the RyR/Ca2+ release channel in the control of calpain activity is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00233435
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  • 6
    Electronic Resource
    Electronic Resource
    Ca2+ Modulation of sarcoplasmic reticulum Ca2+ release in rat skeletal muscle fibers (1995)
    Springer
    The journal of membrane biology 146 (1995), S. 91-99 
    Details
    ISSN: 1432-1424
    Keywords: Ca2+ transients ; Excitation contraction coupling ; Mammalian skeletal muscle ; Mag-Fura-2 ; Fura-2 ; Ca2+ release
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Ca2+ transients and the rate of Ca2+ release (dCaREL/dt) from the sarcoplasmic reticulum (SR) in voltage-clamped, fast-twitch skeletal muscle fibers from the rat were studied with the double Vaseline gap technique and using mag-fura-2 and fura-2 as Ca2+ indicators. Single pulse experiments with different returning potentials showed that Ca2+ removal from the myoplasm is voltage independent. Thus, the myoplasmic Ca2+ removal (dCaREM/dt) was studied by fitting the decaying phase of the Ca2+ transient (Melzer, Ríos & Schneider, 1986) and dCaREL/dt was calculated as the difference between dCa/dt and dCaREM/dt. The fast Ca2+ release decayed as a consequence of Ca2+ inactivation of Ca2+ release. Double pulse experiments showed inactivation of the fast Ca2+ release depending on the prepulse duration. At constant interpulse interval, long prepulses (200 msec) induced greater inactivation of the fast Ca2+ release than shorter depolarizations (20 msec). The correlation (r) between the myoplasmic [Ca2+]i and the inhibited amount of Ca2+ release was 0.98. The [Ca2+]i for 50% inactivation of dCaREL/dt was 0.25 μm, and the minimum number of sites occupied by Ca2+ to inactivate the Ca2+ release channel was 3.0. These data support Ca2+ binding and inactivation of SR Ca2+ release.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00232683
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  • 7
    Electronic Resource
    Electronic Resource
    Activation of Ca2+ release in isolated sarcoplasmic reticulum (1988)
    Springer
    The journal of membrane biology 103 (1988), S. 67-77 
    Details
    ISSN: 1432-1424
    Keywords: sarcoplasmic reticulum ; Ca2+ release ; surface charge ; tetraphenylboron ; ANS fluorescence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The relationship between Ca2+ release from sarcoplasmic reticulum, induced by elevated pH, tetraphenylboron (TPB−) or chemical modification, and the change in the surface charge of the membranes as measured by the fluorescence intensity of anilinonaphthalene sulfonate (ANS) is examined. The stimulated Ca2+ release is inhibited by dicyclohexylcarbodiimide and external Ca2+. TPB−, but not tetraphenylarsonium (TPA+), causes a decrease in ANS− fluorescence, with 50% decrease occurring at about 5 μm TPB−. The decrease in ANS− fluorescence as well as the inhibition of Ca2+ accumulation induced by TPB− are prevented by TPA+. A linear relationship between the decrease in membrane surface potential and the extent of the Ca2+ released by TPB− is obtained. Similar levels of [3H]TPB− bound to sarcoplasmic reticulum membranes were obtained regardless of whether or not the vesicles have taken up Ca2+. The inhibition of Ca2+ accumulation and the [3H]TPB− incorporation into the membranes were correlated. Ca2+ release from sarcoplasmic reticulum, by pH elevation, chemical modification or by addition of NaSCN (0.2 to 0.5m) or the Ca2+ ionophore ionomycin, is also accompanied by a decrease in ANS− fluorescence intensity. However, chemical modification and elevated pH affects the surface potential much less than SCN− or TPB− do. These results suggest that the enhancement of Ca2+ release by these treatments is not due to a general effect on the membrane surface potential, but rather through the modification of a specific protein. They also suggest that membrane surface charges might play an important role in the control mechanism of Ca2+ release.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871933
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  • 8
    Electronic Resource
    Electronic Resource
    Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences (1990)
    Springer
    Journal of molecular evolution 30 (1990), S. 522-562 
    Details
    ISSN: 1432-1432
    Keywords: Calcium-modulated protein ; EF-hand ; Maximum parsimony ; Calmodulin ; Troponin C ; Light chains of myosin ; Parvalbumin ; S100 ; Calpain ; Calbindin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The relationships among 153 EF-hand (calcium-modulated) proteins of known amino acid sequence were determined using the method of maximum parsimony. These proteins can be ordered into 12 distinct subfamilies-calmodulin, troponin C, essential light chain of myosin, regulatory light chain, sarcoplasmic calcium binding protein, calpain, aequorin,Strongylocentrotus purpuratus ectodermal protein, calbindin 28 kd, parvalbumin, α-actinin, and S100/intestinal calcium-binding protein. Eight individual proteins-calcineurin B fromBos, troponin C fromAstacus, calcium vector protein fromBranchiostoma, caltractin fromChlamydomonas, cell-division-cycle 31 gene product fromSaccharomyces, 10-kd calcium-binding protein fromTetrahymena, LPS1 eight-domain protein fromLytechinus, and calcium-binding protein fromStreptomyces—are tentatively identified as unique; that is, each may be the sole representative of another subfamily. We present dendrograms showing the relationships among the subfamilies and uniques as well as dendrograms showing relationships within each subfamily. The EF-hand proteins have been characterized from a broad range of organismal sources, and they have an enormous range of function. This is reflected in the complexity of the dendrograms. At this time we urge caution in assigning a simple scheme of gene duplications to account for the evolution of the 600 EF-hand domains of known sequence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02101108
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  • 9
    Electronic Resource
    Electronic Resource
    Osmotic changes of sarcoplasmic reticulum vesicles during Ca2+ uptake (1983)
    Springer
    The journal of membrane biology 76 (1983), S. 165-171 
    Details
    ISSN: 1432-1424
    Keywords: sarcoplasmic reticulum ; Ca2+-ATPase ; Ca2+ transport ; Ca2+ release ; osmotic swelling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The ATP-dependent accumulation of Ca2+ by sarcoplasmic reticulum vesicles at 37° C reaches a peak after approximately 100 sec. The Ca2+-loading level then declines until a steady-state level is reached which is 20% less than the peak value. This spontaneous release of Ca2+ is enhanced by inclusion of maleate in the Ca2+ uptake medium. Increasing the extravesicular osmolarity by the addition of sucrose to the Ca2+ uptake medium prevents spontaneous Ca2+ release and increases the steady-state Ca2+-loading capacity of sarcoplasmic reticulum vesicles. Swelling of sarcoplasmic reticulum vesicles during Ca2+ uptake in medium containing sucrose is indicated by changes in the light-scattering intensity. These experiments indicate that the capacity of sarcoplasmic reticulum vesicles to accumulate Ca2+ is limited by the osmotic gradient generated by the increase in intravesicular Ca2+. Swelling of sarcoplasmic reticulum vesicles during Ca2+ uptake causes spontaneous Ca2+ release.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02000616
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  • 10
    Electronic Resource
    Electronic Resource
    Measurement of facilitated calcium diffusion by a soluble calcium-binding protein
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 773 (1984), S. 91-98 
    Details
    ISSN: 0005-2736
    Keywords: Ca^2^+ diffusion ; Ca^2^+-binding protein ; Diffusion coefficient ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(84)90553-4
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  • 11
    Electronic Resource
    Electronic Resource
    Structure and expression of genes encoding the three-domain Ca^2^+-binding proteins parvalbumin and oncomodulin
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression 1009 (1989), S. 201-215 
    Details
    ISSN: 0167-4781
    Keywords: Calcium binding protein ; Gene organization ; Gene regulation ; Oncomodulin ; Parvalbumin ; Tissue-specific gene expression
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0167-4781(89)90104-8
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  • 12
    Electronic Resource
    Electronic Resource
    Electron transfer from excited tryptophan to cytochrome c: mechanism of phosphorescence quenching?
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 1100 (1992), S. 33-39 
    Details
    ISSN: 0005-2728
    Keywords: Alcohol dehydrogenase ; Aldolase ; Cytochrome c reduction ; Parvalbumin ; Phosphorescence ; Tryptophan triplet state
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0005-2728(92)90123-J
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  • 13
    Electronic Resource
    Electronic Resource
    The purification of a unique calcium-binding protein from Morris hepatoma 5123 tc
    Amsterdam : Elsevier
    BBA - Protein Structure 621 (1980), S. 296-304 
    Details
    ISSN: 0005-2795
    Keywords: (Morris hepatoma) ; Ca^2^+-binding protein ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2795(80)90181-6
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  • 14
    Electronic Resource
    Electronic Resource
    Binding shift assay of parvalbumin, calmodulin and carbonic anhydrase by high-performance capillary electrophoresis
    Amsterdam : Elsevier
    Journal of Biochemical and Biophysical Methods 22 (1991), S. 263-268 
    Details
    ISSN: 0165-022X
    Keywords: CE ; Calmodulin ; Capillary electrophoresis ; Carbonic anhydrase ; High-performance capillary electrophoresis, HPCE ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0165-022X(91)90032-R
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  • 15
    Electronic Resource
    Electronic Resource
    Fluorescence quenching of the buried tryphtophan residue of cod parvalbumin
    Amsterdam : Elsevier
    Biophysical Chemistry 22 (1985), S. 173-180 
    Details
    ISSN: 0301-4622
    Keywords: (Cod) ; Fluorescence quenching ; Parvalbumin ; Tryptophan
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0301-4622(85)80040-5
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  • 16
    Electronic Resource
    Electronic Resource
    Viscosity dependence of the solute quenching of the tryptophanyl fluorescence of proteins
    Amsterdam : Elsevier
    Biophysical Chemistry 25 (1986), S. 277-282 
    Details
    ISSN: 0301-4622
    Keywords: Fluorescence quenching ; Parvalbumin ; Ribonuclease T"1 ; Tryptophan ; Viscosity dependence
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0301-4622(86)80019-9
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  • 17
    Electronic Resource
    Electronic Resource
    Pressure dependence of fluorescence quenching reactions in proteins
    Amsterdam : Elsevier
    Biophysical Chemistry 32 (1988), S. 121-130 
    Details
    ISSN: 0301-4622
    Keywords: Activation volume ; Fluorescence quenching ; Melittin ; N-Acetyl-l-tryptopha ; Parvalbumin ; Pressure dependence ; Ribonuclease T"1 ; Volume change
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0301-4622(88)85040-3
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  • 18
    Electronic Resource
    Electronic Resource
    Stopped-flow kinetic studies of Ca(II) and Mg(II) dissociation in cod parvalbumin and bovine α-lactalbumin
    Amsterdam : Elsevier
    Biophysical Chemistry 28 (1987), S. 225-233 
    Details
    ISSN: 0301-4622
    Keywords: Ca^2^+ ; Dissociation kinetics ; Mg^2^+ ; Parvalbumin ; α-Lactalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0301-4622(87)80093-5
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  • 19
    Electronic Resource
    Electronic Resource
    Interaction of acrylamide with proteins in the concentration range used for fluorescence quenching studies
    Amsterdam : Elsevier
    Biophysical Chemistry 47 (1993), S. 9-19 
    Details
    ISSN: 0301-4622
    Keywords: Acrylamide binding ; Equilibrium dialysis ; Human serum albumin ; Ovalbumin ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0301-4622(93)80028-H
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  • 20
    Electronic Resource
    Electronic Resource
    Interaction of cupric ion with parvalbumin
    Amsterdam : Elsevier
    Biophysical Chemistry 42 (1992), S. 189-194 
    Details
    ISSN: 0301-4622
    Keywords: Calcium ion binding ; Cupric ion binding ; Fluorescence spectroscopy ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0301-4622(92)85008-R
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  • 21
    Electronic Resource
    Electronic Resource
    Sensitive immunoassay for rat parvalbumin: tissue distribution and developmental changes
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 1075 (1991), S. 68-74 
    Details
    ISSN: 0304-4165
    Keywords: Immunoassay ; Muscle ; Nervous tissue ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0304-4165(91)90076-S
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  • 22
    Electronic Resource
    Electronic Resource
    The binding of arsenazo III to cell components
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 629 (1980), S. 317-327 
    Details
    ISSN: 0304-4165
    Keywords: (Rabbit skeletal muscle) ; Arsenazo III binding ; Ca^2^+ binding ; Calcium assay ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0304-4165(80)90104-X
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  • 23
    Electronic Resource
    Electronic Resource
    Sodium and potassium binding to parvalbumins measured by means of intrinsic protein fluorescence
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 749 (1983), S. 185-191 
    Details
    ISSN: 0167-4838
    Keywords: (Fish) ; Fluorescence change ; Ion binding ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90251-0
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  • 24
    Electronic Resource
    Electronic Resource
    Noncovalent complex between domain AB and domains CD^*EF of parvalbumin
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 1076 (1991), S. 67-70 
    Details
    ISSN: 0167-4838
    Keywords: Calcium binding ; EF-hand ; Fluorescence ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0167-4838(91)90220-T
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  • 25
    Electronic Resource
    Electronic Resource
    Europium(III) ion luminescence as a structural probe of parvalbumin isotypes
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 1040 (1990), S. 229-236 
    Details
    ISSN: 0167-4838
    Keywords: Calcium-binding site ; Europium ; Lanthanide ion ; Luminescence ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-4838(90)90081-P
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    Correspondence of homologies in amino acid sequence and tertiary structure of protein molecules
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 701 (1982), S. 242-252 
    Details
    ISSN: 0167-4838
    Keywords: Interferon ; Parvalbumin ; Sequence homology, Primary structure ; Tertiary structure
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-4838(82)90120-0
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    Electron transfer from excited tryptophan to cytochrome c: mechanism of phosphorescence quenching?
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 1100 (1992), S. 33-39 
    Details
    ISSN: 0167-4838
    Keywords: Alcohol dehydrogenase ; Aldolase ; Cytochrome c reduction ; Parvalbumin ; Phosphorescence ; Tryptophan triplet state
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0167-4838(92)90533-J
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  • 28
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    Protein sequence determination by ESI-MS and LSI-MS tandem mass spectrometry: parvalbumin primary structures from cat, gerbil and monkey skeletal muscle
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 1160 (1992), S. 1-7 
    Details
    ISSN: 0167-4838
    Keywords: Calcium ; Electrospray ; Parvalbumin ; Tandem mass spectrometry
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-4838(92)90032-9
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    Lanthanide-binding properties of rat oncomodulin
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 872 (1986), S. 16-23 
    Details
    ISSN: 0167-4838
    Keywords: (Rat) ; Ca^2^+-binding protein ; Europium ; Lanthanide ; Oncomodulin ; Parvalbumin ; Terbium
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-4838(86)90142-1
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    Interaction of parvalbumin of pike II with calcium and terbium ions
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 952 (1988), S. 67-76 
    Details
    ISSN: 0167-4838
    Keywords: (Circular dichroism) ; (Pike) ; Calcium ion ; Energy transfer ; Intramolecular distance ; Metal binding ; Parvalbumin ; Terbium ion
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-4838(88)90102-1
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    Identification and quantification in single muscle fibers of four isoforms of parvalbumin in the iliofibularis muscle of Xenopus laevis
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 998 (1989), S. 137-144 
    Details
    ISSN: 0167-4838
    Keywords: (X. laevis) ; Parvalbumin ; Single muscle fiber
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0167-4838(89)90265-3
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    Near-infrared Yb^3^+ vibronic sideband spectroscopy: application to Ca^2^+-binding proteins
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 1101 (1992), S. 121-124 
    Details
    ISSN: 0167-4838
    Keywords: Calcium binding protein ; Near-infrared vibronic sideband spectroscopy ; Parvalbumin ; Tryptophan fluorescence ; Vibrational spectroscopy ; Ytterbium
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0167-4838(92)90475-S
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  • 33
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    Oligomerization of an avian thymic parvalbumin Chemical evidence for a Ca^2^+-specific conformation
    Amsterdam : Elsevier
    FEBS Letters 349 (1994), S. 295-300 
    Details
    ISSN: 0014-5793
    Keywords: Ca^2^+-binding protein ; Disulfide bond ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(94)00691-1
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    Rapid reduction in parvalbumin concentration during chronic stimulation of rabbit fast twitch muscle
    Amsterdam : Elsevier
    FEBS Letters 152 (1983), S. 180-182 
    Details
    ISSN: 0014-5793
    Keywords: Ca^2^+ ; Chronic stimulation ; Fast and slow twitch muscle ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(83)80374-3
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  • 35
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    Central helix role in the contraction-relaxation switching mechanisms of permeabilized skeletal and smooth muscles with genetic manipulation of calmodulin
    Amsterdam : Elsevier
    FEBS Letters 263 (1990), S. 340-344 
    Details
    ISSN: 0014-5793
    Keywords: Calcium ; Oncomodulin ; Parvalbumin ; Troponin C
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(90)81409-H
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    Parvalbumin in rat kidney - Purification and localization
    Amsterdam : Elsevier
    FEBS Letters 201 (1986), S. 51-56 
    Details
    ISSN: 0014-5793
    Keywords: (Kidney) ; Ca^2^+ binding protein ; Calbindin-28 "K ; Parvalbumin ; Vitamin D
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(86)80569-5
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    Specific increase of genetic expression of parvalbumin in fast skeletal muscles of mdx mice
    Amsterdam : Elsevier
    FEBS Letters 326 (1993), S. 272-274 
    Details
    ISSN: 0014-5793
    Keywords: Calcium homeostasis ; Duchenne muscular dystrophy ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)81806-B
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    Evidence that deprotonation of Serine-55 is responsible for the pH-dependence of the parvalbumin Eu^3^+ ^7F"0-〉^5D"0 Spectrum
    Amsterdam : Elsevier
    FEBS Letters 314 (1992), S. 130-134 
    Details
    ISSN: 0014-5793
    Keywords: Ca^2^+-binding protein ; Europium ; Lanthanide ; Oncomodulin ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(92)80958-J
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    The complete amino acid sequence of bullfrog (Rana catesbeiana) parvalbumin pI4.97
    Amsterdam : Elsevier
    FEBS Letters 268 (1990), S. 249-251 
    Details
    ISSN: 0014-5793
    Keywords: Amino acid sequence ; Calcium binding protein ; Frog phylogeny ; Molecular evolution ; Muscle protein ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(90)81020-O
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    A calorimetric study of Ca^2^+ binding to two major isotypes of bullfrog parvalbumin
    Amsterdam : Elsevier
    FEBS Letters 185 (1985), S. 165-169 
    Details
    ISSN: 0014-5793
    Keywords: Ca^2^+ binding ; Enthalpy titration ; Mg^2^+ binding ; Microcalorimetry ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(85)80763-8
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    Crystal structure study of Opsanus tau parvalbumin by multiwavelength anomalous diffraction
    Amsterdam : Elsevier
    FEBS Letters 179 (1985), S. 133-137 
    Details
    ISSN: 0014-5793
    Keywords: Anomalous scattering ; Electronic area detector ; Multiwavelength anomalous diffraction ; Parvalbumin ; Protein crystallography ; Synchrotron radiation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(85)80207-6
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    Characterization of the Ca^2^+-switch in skeletal and cardiac muscles
    Amsterdam : Elsevier
    FEBS Letters 251 (1989), S. 177-182 
    Details
    ISSN: 0014-5793
    Keywords: Calmodulin ; Oncomodulin ; Parvalbumin ; Troponin C
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(89)81450-4
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    Calcium-binding proteins in rat skin
    Amsterdam : Elsevier
    FEBS Letters 214 (1987), S. 21-27 
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    ISSN: 0014-5793
    Keywords: (Skin, Epidermis) ; Ca^2^+-binding protein ; Parvalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(87)80006-6
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    Modulation of Ca2+ mobilization by protein kinase C in the submandibular duct cell line A253 (1999)
    Springer
    Molecular and cellular biochemistry 198 (1999), S. 39-46 
    Details
    ISSN: 1573-4919
    Keywords: IP3 formation ; Ca2+ release ; Ca2+ influx ; protein kinase C
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The expression of protein kinase C (PKC) isoforms and the modulation of Ca2+ mobilization by PKC were investigated in the human submandibular duct cell line A253. Three new PKC (nPKC) isoforms (δ, ε, and θ) and one atypical PKC (aPKC) isoform (λ) are expressed in this cell line. No classical PKC (cPKC) isoforms were present. The effects of the PKC activator phorbol 12-myristate-13-acetate (PMA) and of the PKC inhibitors calphostin C (CC) and bisindolymaleimide I (BSM) on inositol 1,4,5-trisphosphate (IP3) and Ca2+ responses to ATP and to thapsigargin (TG) were investigated. Pre-exposure to PMA inhibited IP3 formation, Ca2+ release and Ca2+ influx in response to ATP. Pre-exposure to CC or BSM slightly enhanced IP3 formation but inhibited the Ca2+ release and the Ca2+ influx induced by ATP. In contrast, pre-exposure to PMA did not modify the Ca2+ release induced by TG, but reduced the influx of Ca2+ seen in the presence of this Ca2+-ATPase inhibitor. These results suggest that PKC modulates elements of the IP3/Ca2+ signal transduction pathway in A253 cells by (1) inhibiting phosphatidylinositol turnover and altering the sensitivity of the Ca2+ channels to IP3, (2) altering the activity, the sensitivity to inhibitors, or the distribution of the TG-sensitive Ca2+ ATPase, and (3) modulating Ca2+ entry pathways.
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    Immunological cross-reactions among cyprinidae parvalbumins
    Amsterdam : Elsevier
    Biochemical Systematics and Ecology 2 (1974), S. 103-107 
    Details
    ISSN: 0305-1978
    Keywords: Ca^2^+ binding protein ; Cyprinidae ; Ostariophysi ; Parvalbumin ; Teleost Fishes ; immunological cross-reactions ; white muscle
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
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    URL: http://linkinghub.elsevier.com/retrieve/pii/0305-1978(74)90012-X
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    The unraveling architecture of the junctional sarcoplasmic reticulum (1989)
    Springer
    Journal of bioenergetics and biomembranes 21 (1989), S. 215-225 
    Details
    ISSN: 1573-6881
    Keywords: Skeletal muscle ; sarcoplasmic reticulum ; membrane proteins ; calsequestrin ; Ca2+ release ; Ca2+ channel
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The sarcoplasmic reticulum (SR) of skeletal muscle controls the contraction-relaxation cycle by raising and lowering the myoplasmic free-Ca2+ concentration. The coupling between excitation, i.e., depolarization of sarcolemma and transvers tubule (TT) and Ca2+ release from the terminal cisternae (TC) of SR takes place at the triad. The triad junction is formed by a specialized region of the TC, the junctional SR, and the TT. The molecular architecture and protein composition of the junctional SR are under active investigation. Since the junctional SR plays a central role in excitation-contraction coupling and Ca2+ release, some of its protein constituents are directly involved in these processes. The biochemical evidence supporting this contention is reviewed in this article.
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    Extensive Ca2+ release from energized mitochondria induced by disulfiram (1989)
    Springer
    Journal of bioenergetics and biomembranes 21 (1989), S. 335-345 
    Details
    ISSN: 1573-6881
    Keywords: Disulfiram ; antabuse ; Ca2+ release ; mitochondria ; kidney
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The effect of the alcohol-deterrent drug, disulfiram, on mitochondrial Ca2+ content was studied. Addition of this drug (20 µM) to mitochondria induces a complete loss of accumulated Ca2+. The calcium release is accompanied by a collapse of the transmembrane potential, mitochondrial swelling, and a diminution of the NAD(P)H/NAD(P) radio. These effects of disulfiram depend on Ca2+ accumulation; thus, ruthenium red reestablished the membrane δψ and prevents the oxidation of pyridine nucleotides. The binding of disulfiram to the membrane sulfhydryls appeared to depend on the metabolic state of mitochondria, as well as on the mitochondrial configuration. In addition, it is shown that modification of 9 nmol -SH groups per mg protein suffices to induce the release of accumulated Ca2+.
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    Pharmacology of calcium release from sarcoplasmic reticulum (1989)
    Springer
    Journal of bioenergetics and biomembranes 21 (1989), S. 295-320 
    Details
    ISSN: 1573-6881
    Keywords: Ca2+ release ; drug actions ; excitation-contraction coupling ; pharmacology ; sarcoplasmic reticulum ; skeletal muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Calcium release from sarcoplasmic reticulum (SR) has been elicited in response to additions of many different agents. Activators of Ca2+ release are here tentatively classified as activators of a Ca2+-induced Ca2+ release channel preferentially localized in SR terminal or as likely activators of other Ca2+ efflux pathways. Some of these pathways may be associated with several different mechanisms for SR Ca2+ release that have been postulated previously. Studies of various inhibitors of excitation-contraction coupling and of certain forms of SR Ca2+ release are summarized. The sensitivity of isolated SR to certain agents is unusually affected by experimental conditions. These effects can seriously undermine attempts to anticipate effects of the same pharmacological agentsin situ. Finally, mention is made of a new preparation (“sarcoballs”) designed to make the pharmacological study of SR Ca2+ release more accessible to electrophysiologists, and some concluding speculations on the future of SR pharmacology are offered.
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    Lead-207 NMR: a novel probe for the study of calcium-binding proteins (1996)
    Springer
    JBIC 1 (1996), S. 39-48 
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    ISSN: 1432-1327
    Keywords: Key words207Pb NMR ; Calmodulin ; Parvalbumin ; Helix-loop-helix
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The high-affinity Ca2+–binding sites of carp (pI 4.25) and pike (pI 5.0) parvalbumins, as well as those of mammalian calmodulin (CaM) and its C-terminal tryptic half-molecule (TR2C), were analyzed by 207Pb NMR spectroscopy. For the parvalbumins, two 207Pb signals were observed ranging in chemical shift from ≈750 to ≈1260 ppm downfield of aqueous Pb(NO3)2, corresponding to 207Pb2+ bound to the two high-affinity helix-loop-helix Ca2+–binding sites in each of these proteins. Four 207Pb signals, which fall in the same chemical shift window, could be discerned for CaM. Experiments on TR2C permitted the assignment of each signal as due to 207Pb2+ occupying a helix-loop-helix site in either the N- or the C-lobe of the intact protein. 207Pb and 1H NMR titration studies on CaM provided evidence that Pb2+ binding to all four sites occurs simultaneously, in contrast to the behavior of this protein in the presence of Ca2+. Titrations of the 207Pb2+–forms of CaM and TR2C with the antipsychotic drug trifluoperazine demonstrated that drug binding to the exposed hydrophobic surfaces in CaM causes substantial conformational changes and proceeds in a sequential manner – first the C-lobe and subsequently the N-lobe. Finally, the field dependence of CaM-bound 207Pb signals was examined. The 207Pb signal linewidths exhibited a sharp dependence on the square of the external magnetic field, a trend characteristic of relaxation via chemical shift anisotropy. Relaxation studies on TR2C demonstrated that chemical exchange also contributes to the observed linewidths. The large chemical shift dispersion observed for the 207Pb signals of the three proteins studied here illustrates the remarkable sensitivity of this parameter to subtle differences in the chemical environment of the protein-bound 207Pb nucleus. To our knowledge, the data presented in this article comprise the first ever published example of the application of 207Pb NMR spectroscopy to metalloproteins.
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    Sulfhydryl oxidation induces calcium release from fragmented sarcoplasmic reticulum even in the presence of glutathione (1993)
    Springer
    Cellular and molecular life sciences 49 (1993), S. 282-284 
    Details
    ISSN: 1420-9071
    Keywords: Sarcoplasmic reticulum ; Ca2+ release ; sulfhydryl oxidation ; alcian blue ; plumbagin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Alcian blue and plumbagin induced transient Ca2+ release from fragmented sarcoplasmic reticulum. Dithiothreitol (DTT) and glutathione (GSH) partially blocked Ca2+ release induced by these oxidizing compounds. Pretreatment of alcian blue and plumbagin with DTT or GSH for more than 1 min was required to abolish the ability of the oxidizing compounds to release Ca2+. Mg2+ and ruthenium red completely blocked alcian blue-and plumbagin-induced Ca2+ release. These results suggest that oxidation of sulfhydryls on Ca2+ release channels induces Ca2+ release even in the presence of GSH in situ.
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    Parvalbumin, and intracellular calcium-binding protein; distribution, properties and possible roles in mammalian cells (1984)
    Springer
    Cellular and molecular life sciences 40 (1984), S. 910-921 
    Details
    ISSN: 1420-9071
    Keywords: Parvalbumin ; calcium-binding protein ; muscle ; mammalian
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01946439
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    Interaction of Sr2+ with Ca2+-induced Ca2+ release in mitochondria (1988)
    Springer
    Journal of bioenergetics and biomembranes 20 (1988), S. 749-757 
    Details
    ISSN: 1573-6881
    Keywords: Ca2+ release ; Ca2+ cycling ; mitochondria ; phospholipase A2 ; Sr2+ ; swelling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Respiring rat liver mitochondria are known to spontaneously release the Ca2+ taken up when they have accumulated Ca2+ over a certain threshold, while Sr2+ and Mn2+ are well tolerated and retained. We have studied the interaction of Sr2+ with Ca2+ release. When Sr2+ was added to respiring mitochondria simultaneously with or soon after the addition of Ca2+, the release was potently inhibited or reversed. On the other hand, when Sr2+ was added before Ca2+, the release was stimulated. Ca2+-induced mitochondrial damage and release of accumulated Ca2+ is generally believed to be due to activation of mitochondrial phospholipase A (EC 3.1.1.4.) by Ca2+. However, isolated mitochondrial phospholipase A activity was little if at all inhibited by Sr2+. The Ca2+ -release may thus be triggered by some Ca2+ -dependent function other than phospholipase.
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    Phenylalanine fluorescence and phosphorescence used as a probe of conformation for cod parvalbumin (1993)
    Springer
    Journal of fluorescence 3 (1993), S. 57-64 
    Details
    ISSN: 1573-4994
    Keywords: Parvalbumin ; phenylalanine ; fluorescence ; phosphorescence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The fluorescence emission and triplet absorption properties of phenylalanine in cod fish parvalbumin type II, a protein that contains no Trp or Tyr, was examined in the time scale ranging from nanoseconds to microseconds at 25°C in aqueous buffer (pH 7.0). In the presence of Ca(II), the decay of fluorescence gave two lifetimes (5.9 and 53 ns) and the triplet lifetime was 425 μs. Upon removal of Ca, the fluorescence intensity decreased to values approaching that for free Phe, while the longest fluorescence decay component was 17 ns. At the same time, the decay of triplet showed complex nonexponential kinetics with decay rates faster than in the presence of Ca. Quenching and denaturation analyses suggest that the Phe's are present in a hydrophobic environment in the Ca-bound protein but that the Ca-free protein is relatively unstructured. It is concluded that Phe luminescence in proteins is sensitive to conformation and that the long lifetime of Phe excited states needs to be considered when studying its photochemistry in proteins.
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    Spectroscopic determination of sarcoplasmic reticulum Ca2+ uptake and Ca2+ release (1997)
    Springer
    Molecular and cellular biochemistry 172 (1997), S. 159-170 
    Details
    ISSN: 1573-4919
    Keywords: ryanodine receptor ; sarcoplasmic reticulum ; Ca2+ release ; Calcium Green-2 ; antipyrylazo III
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract In this report we describe the application of spectroscopic methods to the study of Ca2+ release by isolated native sarcoplasmic reticulum (SR) membranes from rabbit skeletal muscle. To date, dual-wavelength spectroscopy of arsenazo III and antipyrylazo III difference absorbance have been the most common spectroscopic methods for the assay of SR Ca2+ transport. The utility of these methods is the ability to manipulate intraluminal Ca2+ loading of SR vesicles. These methods have also been useful for studying the effect of both agonists and antagonists upon SR Ca2+ release and Ca2+ uptake. In this study, we have developed the application of Calcium Green-2, a long-wavelength excitable fluorescent indicator, for the study of SR Ca2+ uptake and release. With this method we demonstrate how ryanodine receptor Ca2+ channel opening and closing is regulated in a complex manner by the relative distribution of Ca2+ between extraluminal and intraluminal Ca2+ compartments. Intraluminal Ca2+ is shown to be a key regulator of Ca2+ channel opening. However, these methods also reveal that the intraluminal Ca2+ threshold for Ca2+-induced Ca2+ release varies as a function of extraluminal Ca2+ concentration. The ability to study how the relative distribution of a finite pool of Ca2+ across the SR membrane influences Ca2+ uptake and Ca2+ release may be useful for understanding how the ryanodine receptor is regulated, in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006879926286
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    Comparison of properties of Ca2+ release channels between rabbit and frog skeletal muscles (1999)
    Springer
    Molecular and cellular biochemistry 190 (1999), S. 191-201 
    Details
    ISSN: 1573-4919
    Keywords: Ca2+ release ; frog ; rabbit ; ryanodine receptor ; skeletal muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Biochemical investigation of Ca2+ release channel proteins has been carried out mainly with rabbit skeletal muscles, while frog skeletal muscles have been preferentially used for physiological investigation of Ca2+ release. In this review, we compared the properties of ryanodine receptors (RyR), Ca2+ release channel protein, in skeletal muscles between rabbit and frog. While the Ryr1 isoform is the main RyR of rabbit skeletal muscles, two isoforms, α- and β-RyR which are homologous to Ryr1 and Ryr3 isoforms in mammals, respectively, coexist as a homotetramer in a similar amount in frog skeletal muscles. The two isoforms in an isotonic medium show very similar property in [3H]ryanodine binding activity which is parallel to Ca2+-induced Ca2+ release (CICR) activity, and make independent contributions to the activities of the sarcoplasmic reticulum. CICR and [3H]ryanodine binding activities of rabbit and frog are qualitatively similar in stimulation by Ca2+, adenine nucleotide and caffeine, however, they showed the following quantitative differences. First, rabbit RyR showed higher Ca2+ affinity than the frog. Second, rabbit RyR showed higher activity in the presence of Ca2+ alone with less stimulation by adenine nucleotide than the frog. Third, rabbit RyR displayed less enhancement of [3H]ryanodine binding by caffeine in spite of having a similar magnitude of Ca2+ sensitization than the frog, which may explain the occasional difficulty by researchers to demonstrate caffeine contracture with mammalian skeletal muscles. Finally, but not least, rabbit RyR still showed marked inhibition of [3H]ryanodine binding in the presence of high Ca2+ concentrations in the 1 M NaCl medium, while frog RyR showed disinhibition. Other matters relevant to Ca2+ release were also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006903401123
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    Evidence that quantal Ca2+ release in HSG cells is not due to ‘all-or-none’ release from discrete Ca2+ stores with differing sensitivities to IP3 (1979)
    Springer
    Molecular and cellular biochemistry 158 (1979), S. 53-56 
    Details
    ISSN: 1573-4919
    Keywords: Ca2+ release ; quantal Ca2+ release ; stimulus secretion coupling ; IP3 receptor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract We demonstrate that the application of the muscarinic agonist carbachol to the human salivary epithelial cell line HSG elicits the now well-known phenomenon of ‘quantal’ Ca2+-release; namely, that the application of a submaximal concentration of agonist results in the release of only a portion of the agonist-sensitive intracellular Ca2+ pool. One explanation that has been proposed to account for this effect is that there are multiple intracellular Ca2+ stores, each with a different agonist sensitivity, which release Ca2+ in an ‘all-or-none’ fashion. We test this hypothesis in intact HSG cells with an experimental protocol designed to preferentially load less-agonist-sensitive stores with 45Ca2+ and more-agonist-sensitive stores with 45Ca2+. However, contrary to the expectations of the above explanation, these cells do not preferentially release 45Ca2+ in response to low concentrations of agonist. Thus our data suggest that quantal Ca2+ release must arise from some other property of the stores or their Ca2+ release channels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00225882
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    Sulfhydryl oxidation and Ca2+ release from sarcoplasmic reticulum (1988)
    Springer
    Molecular and cellular biochemistry 82 (1988), S. 81-84 
    Details
    ISSN: 1573-4919
    Keywords: sarcoplasmic reticulum ; Ca2+ release ; oxidation-reduction ; sulfhydryl groups
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Our interest in the role of sulfhydryl groups (SH) in regulating or altering transport across biological membranes has focused on the significance of a critical SH group associated with the Ca2+-release protein from skeletal muscle sarcoplasmic reticulum (SR). We have shown that binding of heavy metals to this group or oxidation of this sulfhydryl to a disulfide induces rapid Ca2+ release from SR vesicles [1, 2] and induces contraction in skinned muscle fibers [3]. Several models are described in which oxidation and reduction might control the state of the Ca2+-release channel from SR.
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    URL: http://dx.doi.org/10.1007/BF00242520
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    Calcium-binding proteins in the retina of a calbindin-null mutant mouse (1998)
    Springer
    Cell & tissue research 292 (1998), S. 211-218 
    Details
    ISSN: 1432-0878
    Keywords: Key words Calbindin ; Parvalbumin ; Calretinin ; Neurofilament protein ; Calmodulin-like protein ; Mouse [calbindin null mutant ( ; / ; )]
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Calcium-binding proteins are abundantly expressed in many neurons of mammalian retinae. Their physiological roles are, however, largely unknown. This is particularly true for calcium-modulating proteins (“calcium buffers”) such as calbindin D28k. Here, we have studied retinae of wildtype (+/+) and calbindin-null mutant (–/–) mice by using immunocytochemical methods. Although calbindin immunoreactivity was completely absent in the calbindin (–/–) retinae, those cells that express the protein in wildtype retinae, such as horizontal cells, were still present and appeared normal. This was verified by immunostaining horizontal cells for various neurofilament proteins. In order to assess whether other calcium-binding proteins are upregulated in the mutant mouse and may thus compensate for the loss of calbindin, mouse retinae were also immunolabeled for parvalbumin, calretinin, and a calmodulin-like protein (CALP). In no instance could a change in the expression pattern of these proteins be detected by immunocytochemical methods. Thus, our results show that calbindin is not required for the maintenance of the light-microscopic structure of the differentiated retina and suggest roles for this protein in retinal function.
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    URL: http://dx.doi.org/10.1007/s004410051052
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    Changes in Intestinal Mucosal Permeability Caused by Nonprotein Thiol Loss in Rats (1986)
    Springer
    Pharmaceutical research 3 (1986), S. 345-351 
    Details
    ISSN: 1573-904X
    Keywords: mucosal membrane permeability ; intestine ; nonprotein thiol ; Ca2+ release ; hydrophilic compounds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The barrier selectivity of the intestinal mucosal membrane permeability may be impaired in certain disease conditions. Membrane permeability was previously shown to be correlated with changes in nonprotein thiol in rat intestinal tissue by the everted sac method. In the present study, the mucosal effects of alloxan-induced diabetes and chronic alcohol administration to intact rats, as well as pre-treatment with diethyl maleate, ethanol, and salicylate, were investigated. In each case, a drop of mucosal nonprotein thiol was associated with an increased absorption of cefoxitin, cefmetazole, and phenol red, hydrophilic compounds that are poorly absorbed through intact membrane, and with a decreased absorption of L-phenylalanine. The effect of nonprotein thiol loss on rectal absorption of cefoxitin, cefmetazole, and phenol red was greater than that on the small intestinal absorption. The increase in phenol red absorption by diethyl maleate in the in vitro everted sac method correlated with Ca2+ release from the intestinal mucosa, which was induced by nonprotein thiol loss. Resistance to the effect of nonprotein thiol loss on Ca2+ homeostasis was greater in rat ileum than in rat colon (including rectum). The administration of cysteamine as an exogenous nonprotein thiol restored non-protein thiol levels in the mucosa along with the barrier function of the intestinal mucosa to the absorption of cefoxitin, cefmetazole, and phenol red. In contrast, the transport of L-phenylalanine in the small intestinal mucosa was not restored by cysteamine treatment.
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    URL: http://dx.doi.org/10.1023/A:1016384007304
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    Calcium-binding proteins: selective markers of nerve cells (1993)
    Springer
    Cell & tissue research 271 (1993), S. 181-208 
    Details
    ISSN: 1432-0878
    Keywords: Parvalbumin ; Calbindin D-28k ; Calretinin ; Central nervous system ; Development ; Neuroanatomy ; Neurodegenerative diseases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318606
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    Cellular distribution of parvalbumin immunoreactivity in the peripheral vestibular system of three rodents (1993)
    Springer
    Cell & tissue research 274 (1993), S. 487-492 
    Details
    ISSN: 1432-0878
    Keywords: Parvalbumin ; Peripheral vestibular system ; Crista ampullaris ; Utricle ; Immunocytochemistry ; Mouse (CBA/C57) ; Rat (Wistar) ; Guinea pig (BFA)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The cellular distribution of parvalbumin immunoreactivity in the vestibular peripheral system of mouse, rat, and guinea pig was investigated by light and electron microscopy. Parvalbumin was found in all neurons of the vestibular ganglia of these species but in the sensory epithelia immunoreactivity was restricted to type I hair cells localized exclusively in the central areas. The very intense staining pattern was similar in the cristae ampullares and utricles of all three species but a faint immunoreaction was also detectable in sensory cells of peripheral areas of rat cristae. The parvalbumin-immunoreactive type I sensory cells are connected by nerve fibres of the calyx unit type which are known selectively to contain calretinin.
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    URL: http://dx.doi.org/10.1007/BF00314545
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    Cellular localization of the Ca2+-binding protein parvalbumin in the developing avian cerebellum (1986)
    Springer
    Cell & tissue research 243 (1986), S. 69-78 
    Details
    ISSN: 1432-0878
    Keywords: Ca-binding protein ; Parvalbumin ; Cerebellum ; Development ; Birds ; Zebra finch, Poephila guttata
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The appearance and distribution of the calciumbinding protein parvalbumin was investigated immunocytochemically at different postnatal developmental stages of the zebra finch cerebellum. Purkinje, basket and stellate, but not granule neurons or glial cells were labeled by an antiserum against chicken parvalbumin. At all developmental stages investigated immunostained Purkinje cells were found in clusters separated by spaces containing unstained large cells, probably Purkinje and Golgi type-II cells, and unstained smaller cells resembling granule neurons. Perisomatic processes, dendrites and spines of Purkinje cells were heavily immunoreactive. Axons of Purkinje cells were observed to be parvalbumin-positive throughout their entire length until developmental stage D 24, i.e., 10 days after hatching. Their immunoreactivity gradually decreased up to adulthood, when only their proximal portions, in addition to a few punctate structures in the internal granular layer and in the deep cerebellar nuclei presumably representing the synaptic terminals, remained immunoreactive. This decrease in immunoreactivity might be related to progressive maturation and/or degree of myelination. The developmental expression of parvalbumin immunoreactivity and its ultrastructural localization in spines, postsynaptic densities and on microtubular elements leads to several suggestions concerning the possible function of parvalbumin in neurons. In outgrowing dendrites and axons the protein might be involved in the regulation of the synthesis of membrane components, their intracellular transport and fusion of new membrane components into the plasmalemma, events that are Ca- and/or Mg-dependent. In spines and postsynaptic densities parvalbumin might be involved in the development and regulation of synaptic activities in Ca-spiking elements such as the inhibitory Purkinje cells, and possibly also in stellate and basket cells. Furthermore, in developing and adult neurons parvalbumin might be involved in the Ca-/Mg-regulation of a variety of enzymatic activities and hence influence the alteration of the intracellular metabolic potential in response to extracellular signals.
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    URL: http://dx.doi.org/10.1007/BF00221854
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    Immunocytochemical and biochemical localization of parvalbumin in the retina (1986)
    Springer
    Cell & tissue research 243 (1986), S. 213-217 
    Details
    ISSN: 1432-0878
    Keywords: Ca2+-binding protein ; Parvalbumin ; Retina ; Immunohistochemistry ; Radioimmunoassay ; Mammals
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The cellular distribution of parvalbumin-like immunoreactivity (PA-LI) in normal retina of rat, monkey, and human was investigated by immunohistochemical peroxidase antiperoxidase methods, and the levels of PA-LI in normal rat retina and brain were measured by radioimmunoassay. The antibody, raised in rabbits using rat skeletal muscle parvalbumin, did not cross-react with other Ca2+-binding proteins such as calmodulin or S-100 proteins. In rat retina, PA-LI-containing cells are located in the proximal inner nuclear layer and send processes to the external half of the internal plexiform layer, suggesting that they are amacrine cells. In monkey and human retina, PA-LI positive cells exist in the outermost sublayer of inner nuclear layer, and PA-LI-containing fibers that extend horizontally are found in the internal zone of outer plexiform layer. The radioimmunoassay revealed that the rat retina contained 1710±91 ng PA-LI/mg protein, the levels of which were higher than that of brain (881±165 ng PA-LI/mg protein). These results show an additional location for PA-LI outside skeletal muscle and brain, and also provide information on the function of interneurons of retina, which are still poorly understood.
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    URL: http://dx.doi.org/10.1007/BF00221870
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    Distribution of parvalbumin, cytochrome oxidase activity and 14C-2-deoxyglucose uptake in the brain of the zebra finch (1985)
    Springer
    Cell & tissue research 240 (1985), S. 117-127 
    Details
    ISSN: 1432-0878
    Keywords: Visual system, avian ; Parvalbumin ; Cytochrome oxidase ; 2-Deoxyglucose ; Zebra finch
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The visual system of adult zebra finches was investigated 1) immunocytochemically for the distribution of the Ca2+-binding protein parvalbumin, 2) for the activity of the respiratory enzyme cytochrome oxidase, and 3) for the uptake of 2-deoxyglucose. In the visual system, only nuclei of the tecto-fugal pathway and related nuclei were labeled by the parvalbumin antiserum (ectostriatum, nucleus rotundus, tectum opticum, nucleus postero-ventralis, nucleus praetectalis, nucleus subpraetectalis, nucleus isthmipars parvocellularis and-magnocellularis, nucleus isthmoopticus). Additionally, parvalbumin-positive nuclei such as area entorhinalis, area “a” in the hyperstriatum accessorium, nucleus septalis medialis and nucleus habenularis are described. With few exceptions there was a striking correlation of parvalbumin-positive and cytochrome oxidase-positive nuclei of the visual system. Most of the areas with high levels of parvalbumin and cytochrome oxidase were labeled with 2-deoxyglucose as well. Nucleus posteroventralis showed labeling below background intensity. 2-Deoxyglucose uptake primarily reflects energy demands of actual electrical activity, i.e., of the Na+-K+ pump, while cytochrome oxidase supposedly indicates the long-term energy demands of various metabolic pathways. Consequently, high cytochrome oxidase activity together with large 2-deoxyglucose uptake in the tecto-fugal pathway might be due to the high spontaneous and evoked electrical activity. Parvalbumin concentrations in the same areas (and in auditory areas, see Braun et al. 1985I) suggest as one possibility that special Ca2+ mechanisms are present in neuronal systems that can reach high levels of electrical activity.
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    URL: http://dx.doi.org/10.1007/BF00217564
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    Distribution of parvalbumin, cytochrome oxidase activity and 14C-2-deoxyglucose uptake in the brain of the zebra finch (1985)
    Springer
    Cell & tissue research 240 (1985), S. 101-115 
    Details
    ISSN: 1432-0878
    Keywords: Auditory system ; Vocal motor system ; Parvalbumin ; Cytochrome oxidase ; 2-Deoxyglucose ; Calcium ; Plasticity ; CNS ; Song birds ; Zebra finch
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The auditory and vocal motor systems of adult zebra finches were investigated 1) immunocytochemically for the distribution of the Ca2+-binding protein parvalbumin, 2) for the activity of the respiratory enzyme cytochrome oxidase, and 3) for the uptake of 2-deoxyglucose. All auditory nuclei (field L, nucleus ovoidalis, ansa lenticularis, nucleus spiriformis lateralis, nucleus mesencephalicus lateralis-pars dorsalis, nucleus tegmenti pedunculo-pontinus) and vocal motor nuclei (nucleus magnocellularis of the anterior neostriatum, area X, nucleus interfacialis, hyperstriatum ventrale-pars caudalis, nucleus robustus archistriatalis, nucleus intercollicularis) showed high levels of parvalbumin and cytochrome oxidase. Auditory nuclei in addition showed high spontaneous 2-deoxyglucose uptake, while the vocal motor nuclei either remained at background intensity (nucleus magnocellularis of the anterior neostriatum, hyperstriatum ventrale-pars caudalis, nucleus interfacialis and nucleus intercollicularis) or even below background levels (area X, nucleus robustus archistriatalis). Cytochrome oxidase activity supposedly reflects the energy demand of various aspects of metabolism, while 2-deoxyglucose uptake is primarily related to the demands of electrical activity and the Na+-K+ pump. Consequently, it is argued (i) that the congruently high cytochrome oxidase activity and 2-deoxyglucose uptake in the auditory system are due to the high spontaneous electrical activity of neurons, and (ii) that high cytochrome oxidase activity in vocal motor nuclei is related to other than electrical events since 2-deoxyglucose uptake is low. There is evidence of Ca2 + potentials in some parvalbumin-positive neuron types. Ca2+ potentials must lead to Ca2+ flooding of the cytoplasm which could be buffered by parvalbumin thus preventing interference with Ca2+ dependent metabolic reactions or shuttling the ion to sites of such reactions. The unique morphological plasticity reported from the parvalbumin-positive vocal motor nuclei may put a strain on microtubular transport which is Ca2+ dependent. This leads to the idea that parvalbumin reflects local buffering and redistribution mechanisms for Ca2+, and that cytochrome oxidase indicates the underlying energy demand.
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    URL: http://dx.doi.org/10.1007/BF00217563
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    Ultrastructural localization of the calcium-binding protein parvalbumin in neurons of the song system of the zebra finch, Poephila guttata (1985)
    Springer
    Cell & tissue research 241 (1985), S. 77-83 
    Details
    ISSN: 1432-0878
    Keywords: Vocal motor system ; Songbirds (zebra finch) ; Calcium-binding proteins ; Parvalbumin ; Electron microscopy ; Plasticity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of parvalbumin (PV) within neurons of the vocal motor nucleus hyperstriatum ventralepars caudalis (HVc) was investigated in the forebrain of adult male zebra finches by means of light and electron microscopy using the indirect immunoperoxidase technique. Parvalbumin-reaction product was located in the amorphous material of perikarya, dendrites and nuclei, and associated to microtubuli, postsynaptic densities and intracellular membranes; it was found in some axons and Gray type-2 boutons, but rarely in type-1 boutons and never in the Golgi apparatus. These observations suggest that parvalbumin may regulate calcium-dependent processes at the postsynaptic membrane and in the cytosol. Furthermore, the partial association of parvalbumin to microtubuli points to an involvement in calcium-dependent tubular functions. Calcium currents and microtubular assembly or transport may be relevant for the known functions of HVc in song learning.
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    URL: http://dx.doi.org/10.1007/BF00214628
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    Developmental appearance of the Ca2+-binding proteins parvalbumin, calbindin D-28K, S-100 proteins and calmodulin during testicular development in the rat (1988)
    Springer
    Cell & tissue research 252 (1988), S. 359-365 
    Details
    ISSN: 1432-0878
    Keywords: Calcium ; Parvalbumin ; Calbindin D-28K ; S-100 proteins ; Calmodulin ; Testis ; Male sexual hormones ; Leydig cells ; Spermatogenesis ; Rat (SIV-50)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Calcium and intracellular Ca2+-binding proteins are possibly involved in hormone production and spermatogenesis in rat testis. Parvalbumin, calbindin D-28K, S-100 proteins and calmodulin were localized in the Leydig cells, which are sites of testosterone synthesis. Only the appearance of parvalbumin-immunoreactivity is closely correlated to testosterone production during development of the testes. Calbindin D-28K-immunoreactivity persisted in foetal-type Leydig cells and in adult-type Leydig cells at all stages of development. S-100-immunoreactivity was low during all foetal stages, absent between birth and puberty, and increased thereafter. Calmodulin staining is most prominent in the cytoplasm of developing spermatocytes and of maturing spermatids. All four proteins co-exist in the seminiferous tubules. The distinct localization and developmental appearance of these proteins suggests different regulatory roles in Leydig cell function and spermatogenesis.
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    URL: http://dx.doi.org/10.1007/BF00214378
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    Evidence of an auxin-mediated phosphoinositide turnover and an inositol (1,4,5)trisphosphate effect on isolated membranes of Daucus carota L. (1989)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 40 (1989), S. 331-340 
    Details
    ISSN: 0730-2312
    Keywords: auxin action ; phosphoinositide phosphorylation in vitro ; Ca2+ release ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Microsomal membranes from carrot suspension cells were phosphorylated in vitro with [γ-32P]ATP. In the presence of submicromolar concentrations of the natural auxin indoleacetic acid (IAA), a rapid, but transient decrease of the [32P] label could be detected in the phospholipid extracts of the membranes. The phytohormone effect was not the result of an inhibition of the lipid phosphorylation reactions, but was caused by a simultaneous release of water-soluble compounds, which, according to their chromatographic properties, were assumed to contain inositol polyphosphates. Although the [32P]-labeled lipids, as well as the inositol polyphosphates, were not identified unequivocally by chemical analysis, these findings point to an auxin-mediated control of a phosphoinositidase C-like reaction similar to the hormone-stimulated phosphoinositide response in animals. Exogenously applied inositol (1,4,5)trisphosphate [(1,4,5)IP3] was found to release 45Ca2+ from preloaded membrane vesicles of carrot cells. Both the detection of the auxin-stimulated phosphoinositide response and the (1,4,5)IP3-mediated Ca2+ release on isolated cell membranes offer new experimental approaches for the identification of the putative auxin receptor and its signal transduction pathway.
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    URL: http://dx.doi.org/10.1002/jcb.240400309
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