Parvalbumins and Other Soluble High-Affinity Calcium-Binding Proteins from Muscle

Wnuk, W; Cox, Jos A.; Stein, Eric A.

doi:10.1016/b978-0-12-171402-4.50014-9

Cited by 88 publications

(42 citation statements)

References 85 publications

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“…1c), as well as its low Mr and acid pl, suggested that it may be identical to the Ca2"-binding parvalbumin (for recent reviews see refs. [23][24][25]. Mouse parvalbumin isolated by conventional methods (26,27) and by high-performance liquid chromatography (HPLC; refs.…”

Section: Methodsmentioning

confidence: 99%

Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties.

Stuhlfauth¹,

Reininghaus²,

Jockusch³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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To elucidate the biochemical basis of hereditary muscle diseases in an experimental mammal, we performed polypeptide analyses on skeletal muscles of neuromuscular mutants of the mouse. In one of these, "arrested development of righting response" (adr), the concentration of the soluble Ca2 -binding protein parvalbumin was drastically reduced in comparison to wild type. This reduction was not an unspecific consequence of muscle disease, as it was not observed in two other neuromuscular mouse mutants, "wobbler" (wr) and "motor endplate disease" (med or medi0). Isometric twitches of adr muscle had only slightly prolonged contraction and half-relaxation times, yet long-lasting after-contractions were observed upon repeated (20-100 Hz) direct stimulation. Thus, parvalbumin may be mainly involved in the relaxation after tetanic contraction of fast-twitch fibers.Currently under investigation are an increasing number of mutant mice that are affected in the development or maintenance of the neuromuscular system (1, 2). Apart from their

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Section: Methodsmentioning

confidence: 99%

Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties.

Stuhlfauth¹,

Reininghaus²,

Jockusch³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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“…90% or 50% relaxation 9 0 % a n t e r i o r 9 0 % p o s t e r i o r 5 0 % a n t e r i o r 5 0 % p o s t e r i o r Force production is related to Ca 2+ concentration (Kerrick and Donaldson, 1975;Rome et al, 1996): the amount of Ca 2+ available to bind troponin C correlates with the number of crossbridges that can be formed. PARV is a strong Ca 2+ buffer and, as such, affects both the shape and size of the Ca 2+ transient (Wnuk et al, 1982;Pauls et al, 1996). A lower PARV content may not only reduce the rate of relaxation but also facilitate an increase in the intensity of the Ca 2+ signal, so contributing to the increase in muscle force production.…”

Section: +mentioning

confidence: 99%

“…These include the ion channels and pumps in the cell membrane and sarcoplasmic reticulum (SR) that control the release and reuptake of Ca 2+ ; troponin-C, which modulates the effect of Ca 2+ on the contractile proteins; and the Ca 2+ binding proteins, of which the most significant is parvalbumin (PARV). PARV is a small (~12 kDa) sarcoplasmic protein that plays a key role in muscle relaxation (Lannergren et al, 1993;Muntener et al, 1995;Jiang et al, 1996;Baylor and Hollingworth, 1998;Vornanen et al, 1999), acting as an intracellular Ca 2+ buffer to determine the duration and magnitude of the activating Ca 2+ signal (Wnuk et al, 1982;Pauls et al, 1996) and thus the force and duration of contraction. This role is highlighted by the fact that PARV permits muscle relaxation in the absence of all other Ca 2+ sequestration mechanisms (Jiang et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Regional variation in parvalbumin isoform expression correlates with muscle performance in common carp (Cyprinus carpio)

Brownridge

Mello

Peters

et al. 2009

Journal of Experimental Biology

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SUMMARYThe mechanical properties of the axial muscles vary along the length of a fishʼs body. This variation in performance correlates with the expression of certain muscle proteins. Parvalbumin (PARV) is an important calcium binding protein that helps modulate intracellular calcium levels which set the size and shape of the muscle calcium transient. It therefore has a central role in determining the functional properties of the muscle. Transcript data revealed eight specific isoforms of PARV in common carp (Cyprinus carpio) skeletal muscle which we classified as α1 and β1-7. This study is the first to show expression of all eight skeletal muscle PARV isoforms in carp at the protein level and relate regional differences in expression to performance. All of the PARV isoforms were characterised at the protein level using 2D-PAGE and tandem mass spectrometry. Comparison of carp muscle from different regions of the fish revealed a higher level of expression of PARV isoforms β4 and β5 in the anterior region, which was accompanied by an increase in the rate of relaxation. We postulate that changes in specific PARV isoform expression are an important part of the adaptive change in muscle mechanical properties in response to varying functional demands and environmental change.

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“…SCPs constitute a group of homologous proteins that are structurally related to the intracellular calcium-binding proteins mentioned above [8,9]. Their presence has been demonstrated so far in certain arthropods, annelids and molluscs, as well as in cephalochordates [1,. Crayfish SCP, the best characterized among them, is composed of two subunits of M , = 22000 [lo] and possesses six high-affinity Ca2+-binding sites, among which only four bind MgZ+ in a competitive way [13,14].…”

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confidence: 99%

Polymorphism in High‐Affinity Calcium‐Binding Proteins from Crustacean Sarcoplasm

Wnuk

Jáuregui-Adell

1983

European Journal of Biochemistry

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The sarcoplasmic calcium-binding proteins (SCP) from crayfish, lobster and shrimp myogen have been purified to homogeneity. These proteins exist as dimers and dissociate in the presence of sodium dodecyl sulfate or urea in subunits of 22000 molecular weight. During the last step of purification (DEAE-cellulose chromatography), SCP emerges in three peaks in the ratio of 14: 1.5: 1 for crayfish, of 7:2: 1 for lobster and of 3: 2: 1 for shrimp. Gel electrophoresis and isoclcctrofocusing experiments, under native and denaturing conditions, indicate that among the three SCP isotypes there are only two diflerent polypeptide chains, LX and p, which appear in the form of three dimers: ~2 , L X~ and /j2. The x and fi subunits differ slightly in polypeptide chain composition as found by amino acid analyses of thc crayfish and lobster SCPs, and also by comparison of tryptic peptides for crayfish SCPs. The polymorphism observed in crustacean SCPs, which is increased by their ability to form dimers, contrasts with the situation prevailing among other invertebrate SCPs and vertebrate parvalbumins where only monomeric isotypcs are found. Equilibrium binding studies show that all three SCP isotypes from both crayfish and lobster display the same metal-binding properties. They have in their dimeric form six Ca2+-binding sites : two calcium-specific sites, two Ca/Mg sites that interact with positive cooperativity and two Ca/Mg sites that interact with negative cooperativity. Interactions between the two subunits of SCP seem to result in cooperative binding of Ca", which in turn may control more efficiently Ca2+ fluxes in crustacean muscle.

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Parvalbumins and Other Soluble High-Affinity Calcium-Binding Proteins from Muscle

Cited by 88 publications

References 85 publications

Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties.

Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties.

Regional variation in parvalbumin isoform expression correlates with muscle performance in common carp (Cyprinus carpio)

Polymorphism in High‐Affinity Calcium‐Binding Proteins from Crustacean Sarcoplasm

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