ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Ca2+ release
  • Springer  (12)
  • Annual Reviews  (1)
  • 2005-2009  (1)
  • 1990-1994  (3)
  • 1985-1989  (7)
  • 1980-1984  (2)
Collection
Publisher
Years
Year
  • 1
    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
    Format: application/pdf
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 66 (1982), S. 193-201 
    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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 103 (1988), S. 67-77 
    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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 6
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 76 (1983), S. 165-171 
    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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 21 (1989), S. 215-225 
    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.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 21 (1989), S. 335-345 
    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+.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 21 (1989), S. 295-320 
    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.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 49 (1993), S. 282-284 
    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.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 11
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 20 (1988), S. 749-757 
    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.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 12
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 82 (1988), S. 81-84 
    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.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 13
    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.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...