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Home / Equine Research Bank / Proc Natl Acad Sci U S A / Correlation of parvalbumin concentration with relaxation spe...
Proceedings of the National Academy of Sciences of the United States of America1982; 79(23); 7243-7247; doi: 10.1073/pnas.79.23.7243

Correlation of parvalbumin concentration with relaxation speed in mammalian muscles.

Abstract: The physiological role of the Ca2+-binding protein parvalbumin in skeletal muscle has been investigated by measuring the parvalbumin content by HPLC in a variety of mammalian muscles, including man, and comparing the results with the respective muscle relaxation properties and fiber type compositions. The parvalbumin concentrations were highest in the skeletal muscles of the smallest animal investigated (mouse, gastrocnemius: 4.9 g/kg), which has the highest relaxation speed, and lowest in the larger animals (horse, deep gluteal muscle: less than or equal to 0.001 g/kg) and man (vastus, triceps: less than or equal to 0.001 g/kg), which have much lower relaxation speeds. Analysis of three type-homogeneous muscles of the guinea pig revealed highest parvalbumin concentrations (0.25 g/kg) in sartorius (type IIB) and lowest concentrations (less than or equal to 0.007 g/kg) in soleus (type I), consistent with the different half-relaxation times of fast and slow muscles. Denervation of the rat extensor digitorum longus, which increases the half-relaxation time from 9.4 to 19 msec, resulted in a 20% decrease of the parvalbumin content. Given this close correlation between parvalbumin content and relaxation speed in a variety of muscles and species, we suggest that parvalbumin is involved directly in the relaxation process in fast muscles.
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Publication Date: 1982-12-01 PubMed ID: 6961404PubMed Central: PMC347315DOI: 10.1073/pnas.79.23.7243Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research reveals a relationship between the concentration of parvalbumin, a calcium-binding protein, in muscles and the speed at which these muscles relax, where higher parvalbumin content associates with faster muscle relaxation.

Introduction

  • The study explores the biological role of parvalbumin, a protein that binds with calcium ions (Ca2+), in skeletal muscle functioning.
  • The research hypothesizes a correlation between parvalbumin content in muscles and their relaxation speed, observed across various mammals including humans.

Methodology

  • High Performance Liquid Chromatography (HPLC) was used to quantify the parvalbumin content in different types of muscles across mammalian species, including humans.
  • These observations were then compared with the respective muscle relaxation properties and fiber type compositions.

Results

  • Findings showed that parvalbumin concentrations were highest in the skeletal muscles of smaller animals (mouse), which demonstrated the highest relaxation speed.
  • In contrast, larger animals (horse) and man, which have lower muscle relaxation speed, showed the lowest concentrations of parvalbumin.
  • Analysis of parvalbumin concentrations in various muscles in a guinea pig revealed the highest level in the sartorius muscle (type IIB) and the lowest in the soleus muscle (type I), consistent with the different half-relaxation times of fast and slow muscles.

Additional Experiments

  • When the rat extensor digitorum longus was denervated, thereby increasing its half-relaxation time, there was a 20% decrease in the parvalbumin content.

Conclusion

  • Taken together, the results suggest that parvalbumin content may directly impact the relaxation speed in fast muscles across various species.

Cite This Article

APA
Heizmann CW, Berchtold MW, Rowlerson AM. (1982). Correlation of parvalbumin concentration with relaxation speed in mammalian muscles. Proc Natl Acad Sci U S A, 79(23), 7243-7247. https://doi.org/10.1073/pnas.79.23.7243

Publication

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
NlmUniqueID: 7505876
Country: United States
Language: English
Volume: 79
Issue: 23
Pages: 7243-7247

Researcher Affiliations

Heizmann, C W
    Berchtold, M W
      Rowlerson, A M

        MeSH Terms

        • Animals
        • Calcium / physiology
        • Guinea Pigs
        • Horses
        • Humans
        • In Vitro Techniques
        • Mice
        • Muscle Contraction
        • Muscle Denervation
        • Muscle Proteins / physiology
        • Muscle Relaxation
        • Parvalbumins / physiology
        • Rats
        • Time Factors

        References

        This article includes 30 references
        1. Close R. Properties of motor units in fast and slow skeletal muscles of the rat.. J Physiol 1967 Nov;193(1):45-55.
          pubmed: 16992287doi: 10.1113/jphysiol.1967.sp008342google scholar: lookup
        2. Kugelberg E. Histochemical composition, contraction speed and fatiguability of rat soleus motor units.. J Neurol Sci 1973 Oct;20(2):177-98.
          pubmed: 4270833doi: 10.1016/0022-510x(73)90029-4google scholar: lookup
        3. Vaughan HS, Aziz-Ullah, Goldspink G, Nowell NW. Sex and stock differences in the histochemical myofibrillar adenosine triphosphatase reaction in the soleus muscle of the mouse.. J Histochem Cytochem 1974 Mar;22(3):155-9.
          pubmed: 4132626doi: 10.1177/22.3.155google scholar: lookup
        4. Close RI, Luff AR. Dynamic properties of inferior rectus muscle of the rat.. J Physiol 1974 Jan;236(2):259-70.
          pubmed: 16992434doi: 10.1113/jphysiol.1974.sp010434google scholar: lookup
        5. Sica RE, McComas AJ. Fast and slow twitch units in a human muscle.. J Neurol Neurosurg Psychiatry 1971 Apr;34(2):113-20.
          pubmed: 4255199doi: 10.1136/jnnp.34.2.113google scholar: lookup
        6. Lewis DM, Kean CJ, McGarrick JD. Trophic functions of the neuron. II. Denervation and regulation of muscle. Dynamic properties of slow and fast muscle and their trophic regulation.. Ann N Y Acad Sci 1974 Mar 22;228(0):105-20.
          pubmed: 4526278doi: 10.1111/j.1749-6632.1974.tb20505.xgoogle scholar: lookup
        7. Celio MR, Heizmann CW. Calcium-binding protein parvalbumin is associated with fast contracting muscle fibres.. Nature 1982 Jun 10;297(5866):504-6.
          pubmed: 6211622doi: 10.1038/297504a0google scholar: lookup
        8. Jentoft N, Dearborn DG. Labeling of proteins by reductive methylation using sodium cyanoborohydride.. J Biol Chem 1979 Jun 10;254(11):4359-65.
          pubmed: 571437
        9. Berchtold MW, Heizmann CW, Wilson KJ. Primary structure of parvalbumin from rat skeletal muscle.. Eur J Biochem 1982 Oct;127(2):381-9.
          pubmed: 6754379doi: 10.1111/j.1432-1033.1982.tb06883.xgoogle scholar: lookup
        10. Brooke MH, Kaiser KK. Muscle fiber types: how many and what kind?. Arch Neurol 1970 Oct;23(4):369-79.
          pubmed: 4248905doi: 10.1001/archneur.1970.00480280083010google scholar: lookup
        11. Luff AR. Dynamic properties of the inferior rectus, extensor digitorum longus, diaphragm and soleus muscles of the mouse.. J Physiol 1981;313:161-71.
          pubmed: 7277215doi: 10.1113/jphysiol.1981.sp013656google scholar: lookup
        12. Milner-Brown HS, Stein RB, Yemm R. The orderly recruitment of human motor units during voluntary isometric contractions.. J Physiol 1973 Apr;230(2):359-70.
          pubmed: 4350770doi: 10.1113/jphysiol.1973.sp010192google scholar: lookup
        13. Ariano MA, Armstrong RB, Edgerton VR. Hindlimb muscle fiber populations of five mammals.. J Histochem Cytochem 1973 Jan;21(1):51-5.
          pubmed: 4348494doi: 10.1177/21.1.51google scholar: lookup
        14. Celio MR, Heizmann CW. Calcium-binding protein parvalbumin as a neuronal marker.. Nature 1981 Sep 24;293(5830):300-2.
          pubmed: 7278987doi: 10.1038/293300a0google scholar: lookup
        15. Parry DJ, Parslow HG. Fiber type susceptibility in the dystrophic mouse.. Exp Neurol 1981 Sep;73(3):674-85.
          pubmed: 7262262doi: 10.1016/0014-4886(81)90204-1google scholar: lookup
        16. Billeter R, Heizmann CW, Howald H, Jenny E. Analysis of myosin light and heavy chain types in single human skeletal muscle fibers.. Eur J Biochem 1981 May 15;116(2):389-95.
          pubmed: 6454576doi: 10.1111/j.1432-1033.1981.tb05347.xgoogle scholar: lookup
        17. Andrew BL, Part NJ. Properties of fast and slow motor units in hind limb and tail muscles of the rat.. Q J Exp Physiol Cogn Med Sci 1972 Apr;57(2):213-25.
          pubmed: 4482075doi: 10.1113/expphysiol.1972.sp002151google scholar: lookup
        18. Laskey RA, Mills AD. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography.. Eur J Biochem 1975 Aug 15;56(2):335-41.
          pubmed: 1175627doi: 10.1111/j.1432-1033.1975.tb02238.xgoogle scholar: lookup
        19. Taylor A, Stephens JA. Study of human motor unit contractions by controlled intramuscular microstimulation.. Brain Res 1976 Nov 26;117(2):331-5.
          pubmed: 990920doi: 10.1016/0006-8993(76)90742-3google scholar: lookup
        20. Finol HJ, Lewis DM, Owens R. The effects of denervation on contractile properties or rat skeletal muscle.. J Physiol 1981;319:81-92.
          pubmed: 7320930doi: 10.1113/jphysiol.1981.sp013893google scholar: lookup
        21. Pechère JF, Derancourt J, Haiech J. The participation of parvalbumins in the activation-relaxation cycle of vertebrate fast skeletal-muscle.. FEBS Lett 1977 Mar 15;75(1):111-4.
          pubmed: 404185doi: 10.1016/0014-5793(77)80064-1google scholar: lookup
        22. ITZHAKI RF, GILL DM. A MICRO-BIURET METHOD FOR ESTIMATING PROTEINS.. Anal Biochem 1964 Dec;9:401-10.
          pubmed: 14239476doi: 10.1016/0003-2697(64)90200-3google scholar: lookup
        23. Haiech J, Derancourt J, Pechère JF, Demaille JG. Magnesium and calcium binding to parvalbumins: evidence for differences between parvalbumins and an explanation of their relaxing function.. Biochemistry 1979 Jun 26;18(13):2752-8.
          pubmed: 113029doi: 10.1021/bi00580a010google scholar: lookup
        24. Lewis DM, Parry DJ, Rowlerson A. Isometric contractions of motor units and immunohistochemistry of mouse soleus muscle.. J Physiol 1982 Apr;325:393-401.
          pubmed: 7050345doi: 10.1113/jphysiol.1982.sp014157google scholar: lookup
        25. O'Farrell PH. High resolution two-dimensional electrophoresis of proteins.. J Biol Chem 1975 May 25;250(10):4007-21.
          pubmed: 236308
        26. Barnard RJ, Edgerton VR, Furukawa T, Peter JB. Histochemical, biochemical, and contractile properties of red, white, and intermediate fibers.. Am J Physiol 1971 Feb;220(2):410-4.
          pubmed: 4250606doi: 10.1152/ajplegacy.1971.220.2.410google scholar: lookup
        27. Buchthal F, Schmalbruch H. Motor unit of mammalian muscle.. Physiol Rev 1980 Jan;60(1):90-142.
          pubmed: 6766557doi: 10.1152/physrev.1980.60.1.90google scholar: lookup
        28. Spurway NC. Objective characterization of cells in terms of microscopical parameters: an example from muscle histochemistry.. Histochem J 1981 Mar;13(2):269-317.
          pubmed: 6166594doi: 10.1007/BF01006884google scholar: lookup
        29. Close R. Dynamic properties of fast and slow skeletal muscles of the rat after nerve cross-union.. J Physiol 1969 Oct;204(2):331-46.
          pubmed: 5824642doi: 10.1113/jphysiol.1969.sp008916google scholar: lookup
        30. Robertson SP, Johnson JD, Potter JD. The time-course of Ca2+ exchange with calmodulin, troponin, parvalbumin, and myosin in response to transient increases in Ca2+.. Biophys J 1981 Jun;34(3):559-69.
          pubmed: 7195747doi: 10.1016/S0006-3495(81)84868-0google scholar: lookup

        Citations

        This article has been cited 91 times.
        1. Xiong W, Jin L, Zhao Y, Wu Y, Dong J, Guo Z, Zhu M, Dai Y, Pan Y, Zhu X. Deletion of Transferrin Receptor 1 in Parvalbumin Interneurons Induces a Hereditary Spastic Paraplegia-Like Phenotype.. J Neurosci 2023 Jul 5;43(27):5092-5113.
          doi: 10.1523/JNEUROSCI.2277-22.2023pubmed: 37308296google scholar: lookup
        2. Dijkstra JM, Kondo Y. Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species.. Biology (Basel) 2022 Nov 25;11(12).
          doi: 10.3390/biology11121713pubmed: 36552222google scholar: lookup
        3. Bolaños P, Calderón JC. Excitation-contraction coupling in mammalian skeletal muscle: Blending old and last-decade research.. Front Physiol 2022;13:989796.
          doi: 10.3389/fphys.2022.989796pubmed: 36117698google scholar: lookup
        4. Permyakov EA, Uversky VN. What Is Parvalbumin for?. Biomolecules 2022 Apr 30;12(5).
          doi: 10.3390/biom12050656pubmed: 35625584google scholar: lookup
        5. Lasa-Elgarresta J, Mosqueira-Martín L, González-Imaz K, Marco-Moreno P, Gerenu G, Mamchaoui K, Mouly V, López de Munain A, Vallejo-Illarramendi A. Targeting the Ubiquitin-Proteasome System in Limb-Girdle Muscular Dystrophy With CAPN3 Mutations.. Front Cell Dev Biol 2022;10:822563.
          doi: 10.3389/fcell.2022.822563pubmed: 35309930google scholar: lookup
        6. Nogueira L, Gilmore NK, Hogan MC. Role of parvalbumin in fatigue-induced changes in force and cytosolic calcium transients in intact single mouse myofibers.. J Appl Physiol (1985) 2022 Apr 1;132(4):1041-1053.
          doi: 10.1152/japplphysiol.00861.2021pubmed: 35238653google scholar: lookup
        7. Barclay CJ, Curtin NA. The legacy of A. V. Hill's Nobel Prize winning work on muscle energetics.. J Physiol 2022 Apr;600(7):1555-1578.
          doi: 10.1113/JP281556pubmed: 35114037google scholar: lookup
        8. Rincón OA, Milán AF, Calderón JC, Giraldo MA. Comprehensive Simulation of Ca(2+) Transients in the Continuum of Mouse Skeletal Muscle Fiber Types.. Int J Mol Sci 2021 Nov 17;22(22).
          doi: 10.3390/ijms222212378pubmed: 34830262google scholar: lookup
        9. Climer LK, Cox AM, Reynolds TJ, Simmons DD. Oncomodulin: The Enigmatic Parvalbumin Protein.. Front Mol Neurosci 2019;12:235.
          doi: 10.3389/fnmol.2019.00235pubmed: 31649505google scholar: lookup
        10. Barclay CJ, Launikonis BS. Components of activation heat in skeletal muscle.. J Muscle Res Cell Motil 2021 Mar;42(1):1-16.
          doi: 10.1007/s10974-019-09547-5pubmed: 31346851google scholar: lookup
        11. Schwaller B. Cytosolic Ca(2+) Buffers Are Inherently Ca(2+) Signal Modulators.. Cold Spring Harb Perspect Biol 2020 Jan 2;12(1).
          doi: 10.1101/cshperspect.a035543pubmed: 31308146google scholar: lookup
        12. Eckhardt J, Bachmann C, Sekulic-Jablanovic M, Enzmann V, Park KH, Ma J, Takeshima H, Zorzato F, Treves S. Extraocular muscle function is impaired in ryr3 (-/-) mice.. J Gen Physiol 2019 Jul 1;151(7):929-943.
          doi: 10.1085/jgp.201912333pubmed: 31085573google scholar: lookup
        13. Eimre M, Paju K, Peet N, Kadaja L, Tarrend M, Kasvandik S, Seppet J, Ivask M, Orlova E, Kõks S. Increased Mitochondrial Protein Levels and Bioenergetics in the Musculus Rectus Femoris of Wfs1-Deficient Mice.. Oxid Med Cell Longev 2018;2018:3175313.
          doi: 10.1155/2018/3175313pubmed: 30584460google scholar: lookup
        14. Fettiplace R, Nam JH. Tonotopy in calcium homeostasis and vulnerability of cochlear hair cells.. Hear Res 2019 May;376:11-21.
          doi: 10.1016/j.heares.2018.11.002pubmed: 30473131google scholar: lookup
        15. Franzini-Armstrong C. The relationship between form and function throughout the history of excitation-contraction coupling.. J Gen Physiol 2018 Feb 5;150(2):189-210.
          doi: 10.1085/jgp.201711889pubmed: 29317466google scholar: lookup
        16. Calderón JC, Bolaños P, Caputo C. The excitation-contraction coupling mechanism in skeletal muscle.. Biophys Rev 2014 Mar;6(1):133-160.
          doi: 10.1007/s12551-013-0135-xpubmed: 28509964google scholar: lookup
        17. Carafoli E, Krebs J. Why Calcium? How Calcium Became the Best Communicator.. J Biol Chem 2016 Sep 30;291(40):20849-20857.
          doi: 10.1074/jbc.R116.735894pubmed: 27462077google scholar: lookup
        18. Toral-Ojeda I, Aldanondo G, Lasa-Elgarresta J, Lasa-Fernández H, Fernández-Torrón R, López de Munain A, Vallejo-Illarramendi A. Calpain 3 deficiency affects SERCA expression and function in the skeletal muscle.. Expert Rev Mol Med 2016 Apr 8;18:e7.
          doi: 10.1017/erm.2016.9pubmed: 27055500google scholar: lookup
        19. Ferretti R, Marques MJ, Khurana TS, Santo Neto H. Expression of calcium-buffering proteins in rat intrinsic laryngeal muscles.. Physiol Rep 2015 Jun;3(6).
          doi: 10.14814/phy2.12409pubmed: 26109185google scholar: lookup
        20. Lynch CJ, Xu Y, Hajnal A, Salzberg AC, Kawasawa YI. RNA sequencing reveals a slow to fast muscle fiber type transition after olanzapine infusion in rats.. PLoS One 2015;10(4):e0123966.
          doi: 10.1371/journal.pone.0123966pubmed: 25893406google scholar: lookup
        21. Lamboley CR, Kake Guena SA, Touré F, Hébert C, Yaddaden L, Nadeau S, Bouchard P, Wei-LaPierre L, Lainé J, Rousseau EC, Frenette J, Protasi F, Dirksen RT, Pape PC. New method for determining total calcium content in tissue applied to skeletal muscle with and without calsequestrin.. J Gen Physiol 2015 Feb;145(2):127-53.
          doi: 10.1085/jgp.201411250pubmed: 25624449google scholar: lookup
        22. Lopez RJ, Mosca B, Treves S, Maj M, Bergamelli L, Calderon JC, Bentzinger CF, Romanino K, Hall MN, Rüegg MA, Delbono O, Caputo C, Zorzato F. Raptor ablation in skeletal muscle decreases Cav1.1 expression and affects the function of the excitation-contraction coupling supramolecular complex.. Biochem J 2015 Feb 15;466(1):123-35.
          doi: 10.1042/BJ20140935pubmed: 25431931google scholar: lookup
        23. Calderón JC, Bolaños P, Caputo C. Tetanic Ca2+ transient differences between slow- and fast-twitch mouse skeletal muscle fibres: a comprehensive experimental approach.. J Muscle Res Cell Motil 2014 Dec;35(5-6):279-93.
          doi: 10.1007/s10974-014-9388-7pubmed: 25233987google scholar: lookup
        24. Jayasinghe ID, Munro M, Baddeley D, Launikonis BS, Soeller C. Observation of the molecular organization of calcium release sites in fast- and slow-twitch skeletal muscle with nanoscale imaging.. J R Soc Interface 2014 Oct 6;11(99).
          doi: 10.1098/rsif.2014.0570pubmed: 25100314google scholar: lookup
        25. Nelson FE, Hollingworth S, Rome LC, Baylor SM. Intracellular calcium movements during relaxation and recovery of superfast muscle fibers of the toadfish swimbladder.. J Gen Physiol 2014 May;143(5):605-20.
          doi: 10.1085/jgp.201411160pubmed: 24733838google scholar: lookup
        26. Lamboley CR, Murphy RM, McKenna MJ, Lamb GD. Endogenous and maximal sarcoplasmic reticulum calcium content and calsequestrin expression in type I and type II human skeletal muscle fibres.. J Physiol 2013 Dec 1;591(23):6053-68.
          doi: 10.1113/jphysiol.2013.265900pubmed: 24127619google scholar: lookup
        27. Dayanidhi S, Kutch JJ, Valero-Cuevas FJ. Decrease in muscle contraction time complements neural maturation in the development of dynamic manipulation.. J Neurosci 2013 Sep 18;33(38):15050-5.
          doi: 10.1523/JNEUROSCI.1968-13.2013pubmed: 24048835google scholar: lookup
        28. Fuxjager MJ, Longpre KM, Chew JG, Fusani L, Schlinger BA. Peripheral androgen receptors sustain the acrobatics and fine motor skill of elaborate male courtship.. Endocrinology 2013 Sep;154(9):3168-77.
          doi: 10.1210/en.2013-1302pubmed: 23782945google scholar: lookup
        29. Hollingworth S, Baylor SM. Comparison of myoplasmic calcium movements during excitation-contraction coupling in frog twitch and mouse fast-twitch muscle fibers.. J Gen Physiol 2013 May;141(5):567-83.
          doi: 10.1085/jgp.201310961pubmed: 23630340google scholar: lookup
        30. Schlinger BA, Barske J, Day L, Fusani L, Fuxjager MJ. Hormones and the neuromuscular control of courtship in the golden-collared manakin (Manacus vitellinus).. Front Neuroendocrinol 2013 Aug;34(3):143-56.
          doi: 10.1016/j.yfrne.2013.04.001pubmed: 23624091google scholar: lookup
        31. Fuxjager MJ, Barske J, Du S, Day LB, Schlinger BA. Androgens regulate gene expression in avian skeletal muscles.. PLoS One 2012;7(12):e51482.
          doi: 10.1371/journal.pone.0051482pubmed: 23284699google scholar: lookup
        32. Leung NY, Wai CY, Shu S, Wang J, Kenny TP, Chu KH, Leung PS. Current immunological and molecular biological perspectives on seafood allergy: a comprehensive review.. Clin Rev Allergy Immunol 2014 Jun;46(3):180-97.
          doi: 10.1007/s12016-012-8336-9pubmed: 23242979google scholar: lookup
        33. Barclay CJ. Quantifying Ca2+ release and inactivation of Ca2+ release in fast- and slow-twitch muscles.. J Physiol 2012 Dec 1;590(23):6199-212.
          doi: 10.1113/jphysiol.2012.242073pubmed: 23027818google scholar: lookup
        34. Smargiassi M, Daghfous G, Leroy B, Legreneur P, Toubeau G, Bels V, Wattiez R. Chemical basis of prey recognition in thamnophiine snakes: the unexpected new roles of parvalbumins.. PLoS One 2012;7(6):e39560.
          doi: 10.1371/journal.pone.0039560pubmed: 22761824google scholar: lookup
        35. Chiu KH, Hsieh FM, Chen YY, Huang HW, Shiea J, Mok HK. Parvalbumin characteristics in the sonic muscle of a freshwater ornamental grunting toadfish (Allenbatrachus grunniens).. Fish Physiol Biochem 2013 Apr;39(2):107-19.
          doi: 10.1007/s10695-012-9683-4pubmed: 22744796google scholar: lookup
        36. Baylor SM, Hollingworth S. Intracellular calcium movements during excitation-contraction coupling in mammalian slow-twitch and fast-twitch muscle fibers.. J Gen Physiol 2012 Apr;139(4):261-72.
          doi: 10.1085/jgp.201210773pubmed: 22450485google scholar: lookup
        37. McTaggart JS, Lee S, Iberl M, Church C, Cox RD, Ashcroft FM. FTO is expressed in neurones throughout the brain and its expression is unaltered by fasting.. PLoS One 2011;6(11):e27968.
          doi: 10.1371/journal.pone.0027968pubmed: 22140494google scholar: lookup
        38. Hollingworth S, Kim MM, Baylor SM. Measurement and simulation of myoplasmic calcium transients in mouse slow-twitch muscle fibres.. J Physiol 2012 Feb 1;590(3):575-94.
          doi: 10.1113/jphysiol.2011.220780pubmed: 22124146google scholar: lookup
        39. Zhang J, Shettigar V, Zhang GC, Kindell DG, Liu X, López JJ, Yerrimuni V, Davis GA, Davis JP. Engineering Parvalbumin for the Heart: Optimizing the Mg Binding Properties of Rat β-Parvalbumin.. Front Physiol 2011;2:77.
          doi: 10.3389/fphys.2011.00077pubmed: 22059076google scholar: lookup
        40. Schwaller B. Cytosolic Ca2+ buffers.. Cold Spring Harb Perspect Biol 2010 Nov;2(11):a004051.
          doi: 10.1101/cshperspect.a004051pubmed: 20943758google scholar: lookup
        41. Casas M, Figueroa R, Jorquera G, Escobar M, Molgó J, Jaimovich E. IP(3)-dependent, post-tetanic calcium transients induced by electrostimulation of adult skeletal muscle fibers.. J Gen Physiol 2010 Oct;136(4):455-67.
          doi: 10.1085/jgp.200910397pubmed: 20837675google scholar: lookup
        42. Zeiger U, Mitchell CH, Khurana TS. Superior calcium homeostasis of extraocular muscles.. Exp Eye Res 2010 Nov;91(5):613-22.
          doi: 10.1016/j.exer.2010.07.019pubmed: 20696159google scholar: lookup
        43. Baylor SM, Hollingworth S. Calcium indicators and calcium signalling in skeletal muscle fibres during excitation-contraction coupling.. Prog Biophys Mol Biol 2011 May;105(3):162-79.
          doi: 10.1016/j.pbiomolbio.2010.06.001pubmed: 20599552google scholar: lookup
        44. Lucas EK, Markwardt SJ, Gupta S, Meador-Woodruff JH, Lin JD, Overstreet-Wadiche L, Cowell RM. Parvalbumin deficiency and GABAergic dysfunction in mice lacking PGC-1alpha.. J Neurosci 2010 May 26;30(21):7227-35.
          doi: 10.1523/JNEUROSCI.0698-10.2010pubmed: 20505089google scholar: lookup
        45. Weiss N, Andrianjafiniony T, Dupré-Aucouturier S, Pouvreau S, Desplanches D, Jacquemond V. Altered myoplasmic Ca(2+) handling in rat fast-twitch skeletal muscle fibres during disuse atrophy.. Pflugers Arch 2010 Mar;459(4):631-44.
          doi: 10.1007/s00424-009-0764-xpubmed: 19997852google scholar: lookup
        46. Permyakov SE, Bakunts AG, Permyakova ME, Denesyuk AI, Uversky VN, Permyakov EA. Metal-controlled interdomain cooperativity in parvalbumins.. Cell Calcium 2009 Sep;46(3):163-75.
          doi: 10.1016/j.ceca.2009.07.001pubmed: 19651438google scholar: lookup
        47. Calderón JC, Bolaños P, Torres SH, Rodríguez-Arroyo G, Caputo C. Different fibre populations distinguished by their calcium transient characteristics in enzymatically dissociated murine flexor digitorum brevis and soleus muscles.. J Muscle Res Cell Motil 2009;30(3-4):125-37.
          doi: 10.1007/s10974-009-9181-1pubmed: 19543797google scholar: lookup
        48. Rada JA, Wiechmann AF. Ocular expression of avian thymic hormone: changes during the recovery from induced myopia.. Mol Vis 2009;15:778-92.
          pubmed: 19390653
        49. Tikunov BA, Rome LC. Is high concentration of parvalbumin a requirement for superfast relaxation?. J Muscle Res Cell Motil 2009;30(1-2):57-65.
          doi: 10.1007/s10974-009-9175-zpubmed: 19387850google scholar: lookup
        50. Barclay CJ, Woledge RC, Curtin NA. Energy turnover for Ca2+ cycling in skeletal muscle.. J Muscle Res Cell Motil 2007;28(4-5):259-74.
          doi: 10.1007/s10974-007-9116-7pubmed: 17882515google scholar: lookup
        51. Baylor SM, Hollingworth S. Simulation of Ca2+ movements within the sarcomere of fast-twitch mouse fibers stimulated by action potentials.. J Gen Physiol 2007 Sep;130(3):283-302.
          doi: 10.1085/jgp.200709827pubmed: 17724162google scholar: lookup
        52. Hackney CM, Mahendrasingam S, Penn A, Fettiplace R. The concentrations of calcium buffering proteins in mammalian cochlear hair cells.. J Neurosci 2005 Aug 24;25(34):7867-75.
          doi: 10.1523/JNEUROSCI.1196-05.2005pubmed: 16120789google scholar: lookup
        53. Barclay CJ, Weber CL. Slow skeletal muscles of the mouse have greater initial efficiency than fast muscles but the same net efficiency.. J Physiol 2004 Sep 1;559(Pt 2):519-33.
          doi: 10.1113/jphysiol.2004.069096pubmed: 15243139google scholar: lookup
        54. Schwaller B, Meyer M, Schiffmann S. 'New' functions for 'old' proteins: the role of the calcium-binding proteins calbindin D-28k, calretinin and parvalbumin, in cerebellar physiology. Studies with knockout mice.. Cerebellum 2002 Dec;1(4):241-58.
          doi: 10.1080/147342202320883551pubmed: 12879963google scholar: lookup
        55. Baylor SM, Hollingworth S. Sarcoplasmic reticulum calcium release compared in slow-twitch and fast-twitch fibres of mouse muscle.. J Physiol 2003 Aug 15;551(Pt 1):125-38.
          doi: 10.1113/jphysiol.2003.041608pubmed: 12813151google scholar: lookup
        56. Coutu P, Metzger JM. Optimal range for parvalbumin as relaxing agent in adult cardiac myocytes: gene transfer and mathematical modeling.. Biophys J 2002 May;82(5):2565-79.
          doi: 10.1016/S0006-3495(02)75599-9pubmed: 11964244google scholar: lookup
        57. John LM, Mosquera-Caro M, Camacho P, Lechleiter JD. Control of IP(3)-mediated Ca2+ puffs in Xenopus laevis oocytes by the Ca2+-binding protein parvalbumin.. J Physiol 2001 Aug 15;535(Pt 1):3-16.
          doi: 10.1111/j.1469-7793.2001.t01-2-00003.xpubmed: 11507154google scholar: lookup
        58. Raymackers JM, Gailly P, Schoor MC, Pette D, Schwaller B, Hunziker W, Celio MR, Gillis JM. Tetanus relaxation of fast skeletal muscles of the mouse made parvalbumin deficient by gene inactivation.. J Physiol 2000 Sep 1;527 Pt 2(Pt 2):355-64.
          doi: 10.1111/j.1469-7793.2000.00355.xpubmed: 10970436google scholar: lookup
        59. Bugajska-Schretter A, Grote M, Vangelista L, Valent P, Sperr WR, Rumpold H, Pastore A, Reichelt R, Valenta R, Spitzauer S. Purification, biochemical, and immunological characterisation of a major food allergen: different immunoglobulin E recognition of the apo- and calcium-bound forms of carp parvalbumin.. Gut 2000 May;46(5):661-9.
          doi: 10.1136/gut.46.5.661pubmed: 10764710google scholar: lookup
        60. Feher JJ, Waybright TD, Fine ML. Comparison of sarcoplasmic reticulum capabilities in toadfish (Opsanus tau) sonic muscle and rat fast twitch muscle.. J Muscle Res Cell Motil 1998 Aug;19(6):661-74.
          doi: 10.1023/a:1005333215172pubmed: 9742450google scholar: lookup
        61. Szentesi P, Jacquemond V, Kovács L, Csernoch L. Intramembrane charge movement and sarcoplasmic calcium release in enzymatically isolated mammalian skeletal muscle fibres.. J Physiol 1997 Dec 1;505 ( Pt 2)(Pt 2):371-84.
          doi: 10.1111/j.1469-7793.1997.371bb.xpubmed: 9423180google scholar: lookup
        62. Carroll SL, Klein MG, Schneider MF. Decay of calcium transients after electrical stimulation in rat fast- and slow-twitch skeletal muscle fibres.. J Physiol 1997 Jun 15;501 ( Pt 3)(Pt 3):573-88.
          doi: 10.1111/j.1469-7793.1997.573bm.xpubmed: 9218218google scholar: lookup
        63. Rome LC, Syme DA, Hollingworth S, Lindstedt SL, Baylor SM. The whistle and the rattle: the design of sound producing muscles.. Proc Natl Acad Sci U S A 1996 Jul 23;93(15):8095-100.
          doi: 10.1073/pnas.93.15.8095pubmed: 8755609google scholar: lookup
        64. Westerblad H, Allen DG. Slowing of relaxation and [Ca2+]i during prolonged tetanic stimulation of single fibres from Xenopus skeletal muscle.. J Physiol 1996 May 1;492 ( Pt 3)(Pt 3):723-36.
          doi: 10.1113/jphysiol.1996.sp021341pubmed: 8734985google scholar: lookup
        65. Barclay CJ, Arnold PD, Gibbs CL. Fatigue and heat production in repeated contractions of mouse skeletal muscle.. J Physiol 1995 Nov 1;488 ( Pt 3)(Pt 3):741-52.
          doi: 10.1113/jphysiol.1995.sp021005pubmed: 8576863google scholar: lookup
        66. Kosaka T, Kosaka K, Nakayama T, Hunziker W, Heizmann CW. Axons and axon terminals of cerebellar Purkinje cells and basket cells have higher levels of parvalbumin immunoreactivity than somata and dendrites: quantitative analysis by immunogold labeling.. Exp Brain Res 1993;93(3):483-91.
          doi: 10.1007/BF00229363pubmed: 8519337google scholar: lookup
        67. Garcia J, Schneider MF. Calcium transients and calcium release in rat fast-twitch skeletal muscle fibres.. J Physiol 1993 Apr;463:709-28.
          doi: 10.1113/jphysiol.1993.sp019618pubmed: 8246202google scholar: lookup
        68. Müntener M, Käser L, Weber J, Berchtold MW. Increase of skeletal muscle relaxation speed by direct injection of parvalbumin cDNA.. Proc Natl Acad Sci U S A 1995 Jul 3;92(14):6504-8.
          doi: 10.1073/pnas.92.14.6504pubmed: 7604022google scholar: lookup
        69. Stuhlfauth I, Reininghaus J, Jockusch H, Heizmann CW. Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties.. Proc Natl Acad Sci U S A 1984 Aug;81(15):4814-8.
          doi: 10.1073/pnas.81.15.4814pubmed: 6589628google scholar: lookup
        70. Pfyffer GE, Haemmerli G, Heizmann CW. Calcium-binding proteins in human carcinoma cell lines.. Proc Natl Acad Sci U S A 1984 Nov;81(21):6632-6.
          doi: 10.1073/pnas.81.21.6632pubmed: 6387708google scholar: lookup
        71. Heizmann CW. Parvalbumin, an intracellular calcium-binding protein; distribution, properties and possible roles in mammalian cells.. Experientia 1984 Sep 15;40(9):910-21.
          doi: 10.1007/BF01946439pubmed: 6205895google scholar: lookup
        72. Carraro U, Morale D, Mussini I, Lucke S, Cantini M, Betto R, Catani C, Dalla Libera L, Danieli Betto D, Noventa D. Chronic denervation of rat hemidiaphragm: maintenance of fiber heterogeneity with associated increasing uniformity of myosin isoforms.. J Cell Biol 1985 Jan;100(1):161-74.
          doi: 10.1083/jcb.100.1.161pubmed: 3965469google scholar: lookup
        73. Endo T, Kobayashi M, Kobayashi S, Onaya T. Immunocytochemical and biochemical localization of parvalbumin in the retina.. Cell Tissue Res 1986;243(1):213-7.
          doi: 10.1007/BF00221870pubmed: 3943121google scholar: lookup
        74. Berchtold MW, Means AR. The Ca2+-binding protein parvalbumin: molecular cloning and developmental regulation of mRNA abundance.. Proc Natl Acad Sci U S A 1985 Mar;82(5):1414-8.
          doi: 10.1073/pnas.82.5.1414pubmed: 3856270google scholar: lookup
        75. Endo T, Onaya T. Parvalbumin is reduced in the peripheral nerves of diabetic rats.. J Clin Invest 1986 Nov;78(5):1161-4.
          doi: 10.1172/JCI112697pubmed: 3771787google scholar: lookup
        76. Leberer E, Pette D. Neural regulation of parvalbumin expression in mammalian skeletal muscle.. Biochem J 1986 Apr 1;235(1):67-73.
          doi: 10.1042/bj2350067pubmed: 3741391google scholar: lookup
        77. Rogers JH. Calretinin: a gene for a novel calcium-binding protein expressed principally in neurons.. J Cell Biol 1987 Sep;105(3):1343-53.
          doi: 10.1083/jcb.105.3.1343pubmed: 3654755google scholar: lookup
        78. Kay BK, Shah AJ, Halstead WE. Expression of the Ca2+-binding protein, parvalbumin, during embryonic development of the frog, Xenopus laevis.. J Cell Biol 1987 Apr;104(4):841-7.
          doi: 10.1083/jcb.104.4.841pubmed: 3558484google scholar: lookup
        79. Dulhunty AF. Internal citrate ions reduce the membrane potential for contraction threshold in mammalian skeletal muscle fibers.. Biophys J 1988 Apr;53(4):609-16.
          doi: 10.1016/S0006-3495(88)83139-4pubmed: 3382714google scholar: lookup
        80. Klug GA, Leberer E, Leisner E, Simoneau JA, Pette D. Relationship between parvalbumin content and the speed of relaxation in chronically stimulated rabbit fast-twitch muscle.. Pflugers Arch 1988 Feb;411(2):126-31.
          doi: 10.1007/BF00582304pubmed: 3357751google scholar: lookup
        81. Iaizzo PA. The effects of temperature on relaxation in frog skeletal muscle: the role of parvalbumin.. Pflugers Arch 1988 Jul;412(1-2):195-202.
          doi: 10.1007/BF00583750pubmed: 3262859google scholar: lookup
        82. Dulhunty AF. The rate of tetanic relaxation is correlated with the density of calcium ATPase in the terminal cisternae of thyrotoxic skeletal muscle.. Pflugers Arch 1990 Jan;415(4):433-9.
          doi: 10.1007/BF00373620pubmed: 2138281google scholar: lookup
        83. Satoh J, Tabira T, Sano M, Nakayama H, Tateishi J. Parvalbumin-immunoreactive neurons in the human central nervous system are decreased in Alzheimer's disease.. Acta Neuropathol 1991;81(4):388-95.
          doi: 10.1007/BF00293459pubmed: 2028743google scholar: lookup
        84. Ohshima T, Endo T, Onaya T. Distribution of parvalbumin immunoreactivity in the human brain.. J Neurol 1991 Sep;238(6):320-2.
          doi: 10.1007/BF00315329pubmed: 1940981google scholar: lookup
        85. Laforet C, Feller G, Narinx E, Gerday C. Parvalbumin in the cardiac muscle of normal and haemoglobin-myoglobin-free antarctic fish.. J Muscle Res Cell Motil 1991 Oct;12(5):472-8.
          doi: 10.1007/BF01738332pubmed: 1939611google scholar: lookup
        86. Westerblad H, Lännergren J. Slowing of relaxation during fatigue in single mouse muscle fibres.. J Physiol 1991 Mar;434:323-36.
          doi: 10.1113/jphysiol.1991.sp018472pubmed: 1902516google scholar: lookup
        87. Schmitt TL, Pette D. Fiber type-specific distribution of parvalbumin in rabbit skeletal muscle. A quantitative microbiochemical and immunohistochemical study.. Histochemistry 1991;96(6):459-65.
          doi: 10.1007/BF00267071pubmed: 1837548google scholar: lookup
        88. Hou TT, Johnson JD, Rall JA. Parvalbumin content and Ca2+ and Mg2+ dissociation rates correlated with changes in relaxation rate of frog muscle fibres.. J Physiol 1991 Sep;441:285-304.
          doi: 10.1113/jphysiol.1991.sp018752pubmed: 1816377google scholar: lookup
        89. Gerday C, Goffard P, Taylor SR. Isolation and characterization of parvalbumins from skeletal muscles of a tropical amphibian, Leptodactylus insularis.. J Comp Physiol B 1991;161(5):475-81.
          doi: 10.1007/BF00257902pubmed: 1744247google scholar: lookup
        90. Schleef M, Zühlke C, Jockusch H, Schöffl F. The structure of the mouse parvalbumin gene.. Mamm Genome 1992;3(4):217-25.
          doi: 10.1007/BF00355722pubmed: 1611216google scholar: lookup
        91. Berquin A, Lebacq J. Parvalbumin, labile heat and slowing of relaxation in mouse soleus and extensor digitorum longus muscles.. J Physiol 1992 Jan;445:601-16.
          doi: 10.1113/jphysiol.1992.sp018942pubmed: 1501147google scholar: lookup
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