The participation of parvalbumins in the activation—relaxation cycle of vertebrate fast skeletal‐muscle

Péchère, Jean-Claude; Derancourt, Jean; Haiech, Jacques

doi:10.1016/0014-5793(77)80064-1

Cited by 125 publications

(39 citation statements)

References 14 publications

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“…Both of these results were predicted (see Introduction) from the hypothesis that PA promotes muscle relaxation (Briggs, 1975;Gerday & Gillis, 1976;Pechere et al 1977) and that the contribution of PA to relaxation rate is greater at lower temperatures (Gillis et al 1982). According to this hypothesis, the PA-Mg promotes relaxation by exchanging Ca2+ for Mg2+ during relaxation.…”

Section: Discussionsupporting

confidence: 63%

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Effect of temperature on relaxation rate and Ca2+, Mg2+ dissociation rates from parvalbumin of frog muscle fibres.

Hou

Johnson

Rall

1992

The Journal of Physiology

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SUMMARY1. Influence of temperature on relaxation rate as a function of isometric tetanus duration and on Ca2" and Mg2" dissociation rates from purified parvalbumin (PA) was examined to test the hypothesis that PA promotes relaxation in frog skeletal muscle. Single fibres and PA IVB from Rana temporaria skeletal muscle were utilized.2. The magnitude of slowing of relaxation rate with increasing tetanus duration, relative to the final, steady value of relaxation rate, is 3-fold greater at 0 than at 10 OC.3. In the 0-10°C range, the Qlo for relaxation rate increases from 2-3 to 3-7 with increasing tetanus duration.

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Section: Discussionsupporting

confidence: 63%

“…Parvalbumin (PA), an intracellular Ca2+-binding protein, has been proposed to promote relaxation in fast-contracting skeletal muscle (Briggs, 1975;Gerday & Gillis, 1976; Pechere, Derancourt & Haiech, 1977). According to this view, the sarcoplasmic reticulum (SR) and PA operate in parallel to sequester Ca2+ during relaxation.…”

Section: Introductionmentioning

confidence: 99%

Effect of temperature on relaxation rate and Ca2+, Mg2+ dissociation rates from parvalbumin of frog muscle fibres.

Hou

Johnson

Rall

1992

The Journal of Physiology

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“…This role could involve interacting with other proteins, or facilitating calcium diffusion (10,39), or providing shortterm buffering for local calcium concentration in the cytosol. A calcium-buffering role in neurons has been suggested both for calbindin (5,29,30) and for parvalbumin (9,13,18), by analogy with evidence that they have calcium-buffeting roles respectively in intestinal calcium absorption (60) and in muscle contraction (26,48).…”

Section: Function Of Cabps In Neuronsmentioning

confidence: 99%

Calretinin: a gene for a novel calcium-binding protein expressed principally in neurons [published erratum appears in J Cell Biol 1990 May;110(5):1845]

Rogers

1987

The Journal of Cell Biology

554

296

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Abstract.A novel gene of the calmodulin superfamily, encoding a 29-kD neuronal protein here named "calretinin; has been isolated as a cDNA clone from chick retina. The encoded sequence includes four putative calcium-binding sites and a fusion protein binds calcium. The most similar protein known is the 28-kD intestinal calcium-binding protein, calbindin (58% homology). Both genes date from before the divergence of chicks from mammals. The distribution of calretinin and calbindin mRNAs in chick tissues has been mapped using RNA gel blots and in situ hybridization. RNAs from both genes are abundant in the retina and in many areas of the brain, but calretinin RNA is absent from intestine and other nonneural tissues. Calretinin and calbindin are expressed in different sets of neurons throughout the brain. Calretinin RNA is particularly abundant in auditory neurons with precisely timed discharges.T HE superfamily of calcium-binding proteins, whose prototype is calmodulin, contains at least a dozen members which perform a wide variety of calciumdependent functions in different tissues. Calmodulin itself regulates several important enzymes in most cell types (34). Troponin C and the myosin light chains regulate muscle contraction (1). Parvalbumin, another muscle protein, appears to be involved in terminating fast contractions (26). Another important member of the superfamily is the 28-kD vitamin D-dependent intestinal calcium-binding protein (70), also known as cholecalcin 28k, spot 35, or visinin (47a), and now re-named calbindin DEak-hereafter "calbindin." Calbindin appears to be involved in intestinal calcium transport, but is also present in kidney, bone, and several other tissues (30,46,65). The calbindin gene has been cloned by several groups (21,27,28,71,72).Many neurons in the brains of mammals and of birds exhibit immunoreactivity for parvalbumin (7,9,13,15,17,18) or for calbindin (5,20,22,29,30,33,57). Each is present only in some neurons, commonly throughout the whole neuron including the dendritic tree and axonal terminals. They are both very abundant in the Purkinje cells of the cerebellum, and calbindin constitutes "~15 % of the soluble protein of these cells (5, 6,30,40,47,64). But elsewhere in the brain, calbindin and parvalbumin immunoreactivities are mostly in separate neurons (9,11,24). Both are also present in rat retina (17,50), and calbindin immunoreactivity is present in chick retina (25,53,58).The function of these proteins in neurons is unknown. An initial suggestion that parvalbumin was colocalized with GABA (15) has not been generally confirmed by more extensive surveys (13, 18). Parvalbumin-containing neurons do generally have rapid firing rates (9, 14). The numerous calbindin-immunoreactive cells are not known to have any common features.I now report the isolation from chick retina of an mRNA encoding a new member of the superfamily, which is expressed in the retina and in brain neurons. Because of its homology with calcium-binding proteins and its tissue of origin, I refer to the encoded p...

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“…A more rapid rate of relaxation is also aided by the higher fractional volumes (Eisenberg, Kuda & Peter, 1974;Eisenberg & Kuda, 1975;Kryvi, 1977;Johnston, 1980b) and greater rates of Ca2+ uptake (Briggs, Poland & Solaro 1977;McArdle & Johnston, 1981) of fast muscle sarcoplasmic reticulum. The fast muscles of fish also contain high concentrations of parvalbumins, cytoplasmic Ca2+ binding proteins, which are thought to aid rapid relaxation (Gerday & Gillis, 1976;Pechere, Derancourt & Harech, 1977).…”

Section: Residual Tensionmentioning

confidence: 99%

The pCa‐tension and force‐velocity characteristics of skinned fibres isolated from fish fast and slow muscles

Altringham

Johnston

1982

The Journal of Physiology

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SUMMARY1. Single fast fibres and small bundles of two to six slow fibres were dissected from the myotomal muscles of the cod, GadUs morhua, and the dogfish, Scyliorhinus canicula. Fibres were chemically skinned with the non-ionic detergent Brij 58.2. The isometric tension properties were investigated. Maximal isometric tensions (mean+S.E. of mean) were 18-65+1-18 (n = 11) and 8-34±+098 (n = 13) N cm-2 for cod fast and slow fibres, and 18'34+O088 (n = 28) and 8-24±+039 (n = 12) N cm-2 for dogfish fast and slow fibres respectively. The values are comparable to those observed in mammalian and amphibian skinned fibres. The lower tensions generated by the slow fibres cannot be fully explained on the basis of their lower myofibrillar fractional volume.3. In common with previous studies, a steep sigmoid relationship between pCa and tension was observed. The threshold for tension generation was around pCa 7-2. Half-maximal pCas were 6-08 and 6-42 for cod fast and slow muscle, and 6-41 and 6-50 for dogfish fast and slow fibres respectively. Cod fibres were maximally activated at around pCa 5-18, and dogfish fibres at pCa 5-62.4. Contraction-induced residual tensions were observed in cod fast fibres after return to relaxing solution. This phenomenon is a feature common to many skinned fibre studies, but the mechanism behind it has yet to be resolved.5. The force-velocity characteristics of fast and slow fibres have been investigated (at 8°C). 6. Points below 0-6 P0 on the P-V curves could be fitted to a linear form of the 7. Contraction velocity in cod slow fibres decreased continuously to produce markedly non-linear velocity transients, similar to those reported for amphibian slow fibres.8. The effect of altering Ca2+ concentration on the shape of the isotonic velocity curve (at low loads) was studied in dogfish fast fibres (0 5-1°C). Contraction velocity * Current address:

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The participation of parvalbumins in the activation—relaxation cycle of vertebrate fast skeletal‐muscle

Cited by 125 publications

References 14 publications

Effect of temperature on relaxation rate and Ca2+, Mg2+ dissociation rates from parvalbumin of frog muscle fibres.

Effect of temperature on relaxation rate and Ca2+, Mg2+ dissociation rates from parvalbumin of frog muscle fibres.

Calretinin: a gene for a novel calcium-binding protein expressed principally in neurons [published erratum appears in J Cell Biol 1990 May;110(5):1845]

The pCa‐tension and force‐velocity characteristics of skinned fibres isolated from fish fast and slow muscles

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