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  • Parvalbumin
  • Springer  (14)
  • Annual Reviews  (1)
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  • Springer  (14)
  • Annual Reviews  (1)
  • Elsevier  (35)
  • 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
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  • 2
    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.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 30 (1990), S. 522-562 
    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.
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  • 4
    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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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 40 (1984), S. 910-921 
    ISSN: 1420-9071
    Keywords: Parvalbumin ; calcium-binding protein ; muscle ; mammalian
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
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  • 6
    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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  • 7
    Electronic Resource
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    Springer
    Cell & tissue research 292 (1998), S. 211-218 
    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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  • 8
    Electronic Resource
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    Springer
    Cell & tissue research 271 (1993), S. 181-208 
    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
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  • 9
    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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  • 10
    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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  • 11
    Electronic Resource
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    Cell & tissue research 243 (1986), S. 213-217 
    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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  • 12
    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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  • 13
    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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  • 14
    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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  • 15
    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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