Polymorphism of sarcoplasmic-reticulum adenosine triphosphatase of rabbit skeletal muscle

Damiani, Ernesto; Betto, Romeo; Salvatori, Sergio; Volpe, Pompeo; Salviati, G.; Margreth, Alfredo

doi:10.1042/bj1970245

Cited by 58 publications

(25 citation statements)

References 27 publications

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“…This may result from the specific activity of the calcium ATPase, the membrane density of the ATPase, or amounts of SR membrane in the fibers. Antibody studies suggest that the ATPase is not identical in all muscles (DeFoor et al, 1980;Damiani et al, 1981;Volpe et al, 1982), while polyclonal antibody and freeze-fracture studies suggest that there is 50% less ATPase in slow-twitch fibers (Beringer, 1976;Bray & Rayns, 1976;Heilmann, Mtiller & Pette, 1981;Jorgensen et al, 1982b). In contrast, ATPase crystal lattices (Dux & Martonosi, 1984) suggest that the different ATPase activities depend on the greater amount of ATPase containing membrane in faster fibers (Eisenberg & Kuda, 1976;Eisenberg, 1983).…”

Section: Introductionmentioning

confidence: 93%

Distribution of calcium ATPase in the sarcoplasmic reticulum of fast- and slow-twitch muscles determined with monoclonal antibodies

1987

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Four monoclonal antibodies against the calcium ATPase in sarcoplasmic reticulum (SR) of rabbit fast-twitch skeletal muscle were characterized using SDS-PAGE, Western blots and immunofluorescence. The ultrastructural distribution of the antigens was determined using post-embedding immunolabeling. The antibodies recognized the calcium ATPase in the SR but not in transverse (T-) tubule or plasma membranes. The antibody, D12, had the same binding affinity for the calcium ATPase from fast-twitch (rabbit sternomastoid) and slow-twitch (rabbit soleus) fibers and the affinity fell by 30% after fixation for electron microscopy in both types of muscle fiber. Ultrastructural studies revealed that the density of D12 antibody binding to the terminal cisternae membrane of extensor digitorum longus (edl) and sternomastoid fibers was on average seven times greater than in the slow-twitch soleus and semimembranosus fibers. Since the affinity of the ATPase for the antibody was the same in SR from fast- and slow-twitch muscles, the concentration of calcium ATPase in the terminal cisternae membrane of fast-twitch fibers was seven times greater than in slow-twitch fibers. This conclusion was supported by the fact that the concentration of calcium ATPase in light SR membranes was six times greater in SR from fast-twitch fibers than in SR from slow-twitch fibers. The results provide strong evidence that the different calcium accumulation rates in mammalian fast- and slow-twitch muscles are due to different concentrations of calcium ATPase molecules in the SR membrane.

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Section: Introductionmentioning

confidence: 93%

Distribution of calcium ATPase in the sarcoplasmic reticulum of fast- and slow-twitch muscles determined with monoclonal antibodies

1987

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“…The soleus and semitendinosus muscles of male New Zealand White rabbits were used as representative slow-twitch muscles, on account of previous characterization studies in this laboratory of the isoprotein composition of myosin and other myofibrillar proteins in whole muscle (Biral et al, 1982) and isolated, chemically-skinned fibres , of the membrane protein composition and biochemical properties of isolated SR fragments from the same muscles (Damiani et al, 1981;Salviati et al 1982 a, b), as well as because of their characteristics in SR Ca 2+-release . In each experiment, SR membranes were isolated from the pooled frozen muscles of 6-8 rabbits, using a modification (Inui et al, 1987) of the original method of Saito and co-workers (1984).…”

Section: Preparative Proceduresmentioning

confidence: 99%

Coexpression of two isoforms of calsequestrin in rabbit slow-twitch muscle

Damiani

Volpe

Margreth

1990

J Muscle Res Cell Motil

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The cardiac and fast-twitch skeletal muscle forms of the Ca2(+)-binding protein calsequestrin (CS) are the products of two different genes, both of which are transcribed in slow-twitch skeletal muscle, though at much different rates (Scott et al., 1988., Fliegel et al., 1989). We have investigated this problem more closely at the protein level, on isolated terminal cisternae (TC) of the sarcoplasmic reticulum (SR) of rabbit slow-twitch muscle, and following purification of two distinct forms of CS from whole tissue by DEAE-Cellulose chromatography and CA2(+)-dependent elution from phenyl-Sepharose. Two electrophoretically (apparent molecular mass of 64 kDa and 54 kDa, respectively), and antigenically distinct forms of CS, here shown to be related to the fast-twitch skeletal muscle and to cardiac-type isoform of CS, respectively, colocalize to junctional TC of slow-twitch muscle. The cardiac-type isoform that is expressed in slow-twitch muscle accounts for about 25% of total CS present in isolated TC, it binds Ca2+ as effectively as the major CS form, using a 45Ca-overlay technique, and it shares extensive similarities with dog cardiac CS, not only in size and antigenically, but also in pl, as well as in the DEAE-elution characteristics. No difference in behaviour with phenyl-Sepharose resin were observed between the two CS isoforms from slow-twitch muscle.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…To date, no slow-twitch fiber isomorphs have been detected for parvalbumin and calsequestrin. However, Damiani et al [18], using competitive ELISA analyses, demonstrated different affinities of anti-(CaATPase) from fast-twitch muscle for the antigens from fast and slow-twitch muscles. Likewise, these observations have been confirmed in the present study.…”

Section: Characterization Of Antibodiesmentioning

confidence: 99%

Immunochemical quantification of sarcoplasmic reticulum Ca-ATPase, of calsequestrin and of parvalbumin in rabbit skeletal muscles of defined fiber composition

1986

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Antibodies directed against purified Ca-ATPase from sarcoplasmic reticulum, calsequestrin and parvalbumin from rabbit fast-twitch muscle were raised in sheep. The specificity of the antibodies was shown by immunoblot analysis and by enzyme-linked immunoadsorbent assays (ELISAs). IgG against the sarcoplasmic reticulum CaATPase inhibited the catalytic activities of Ca-ATPase from fast-twitch (psoas, tibialis anterior) and slow-twitch (soleus) muscles to the same degree. In non-equilibrium competitive ELISAs the anti(Ca-ATPase) IgG displayed a slightly higher affinity for the Ca-ATPase from fast-twitch muscle than for that from slow-twitch muscle. This suggests a fiber-type-specific polymorphism of the sarcoplasmic reticulum Ca-ATPase. Quantification of CaATPase, calsequestrin and parvalbumin in various rabbit skeletal muscles of histochemically determined fiber composition was achieved by sandwich ELISA. Ca-ATPase was found to be 6-7 times higher in fast than in slow-twitch muscles. A slightly higher concentration was found in fast-twitch muscles with a higher percentage of IIb fibers when compared with fast-twitch muscles with a higher percentage of IIa fibers. Thus Ca-ATPase is distributed as follows, IIb 2 IIa & I. Calsequestrin was uniformly distributed in fast-twitch muscles independently of their IIa/Ilb fiber ratio and displayed 50% lower concentrations in slow than in fast-twitch muscles (IIb = IIa > I). Parvalbumin contents were 200-300-fold higher in fast than in slow-twitch muscles. Significantly lower parvalbumin concentrations were found in fast-twitch muscles with a higher percentage of IIa fibers than in fast-twitch muscles with a higher percentage of IIb fibers (IIb > IIa % I).The major components of the Ca-sequestering system in mammalian skeletal muscle are the Ca-pumping ATPase and the Ca-binding calsequestrin of the sarcoplasmic reticulum (SR). The functional properties and the amount of these components determine the Ca-sequestering capacity of a given muscle. It is now generally accepted that differences exist with regard to this system between fast and slow-twitch muscles. Studies on isolated microsomal preparations have shown higher Ca-uptake capacities and Ca-ATPase activities in SR from fast-twitch than in SR from slow-twitch mammalian muscles [l -121. In addition, electron microscopy has revealed a higher fractional volume of the SR in fast than in slowtwitch muscle fibers [13-161. These data are in accordance with the higher Ca-uptakc capacities measured in cryostat sections [I 71 and in homogenates of fast-twitch muscles [5, 91. More recently, evidence indicates that mammalian muscles contain fiber-type-specific Ca-ATPase isozymes [18, 191. It has been suggested that the acidic, cytosolic Ca-binding protein parvalbumin may also play a major role in Ca regulation (for reviews see [20 -221) parvalbumin [23 -251. Therefore, the suggested role of parvalbumin may be restricted to fast-twitch fibers.The aim of the present study was to investigate the concentrations of these major Ca-seq...

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Polymorphism of sarcoplasmic-reticulum adenosine triphosphatase of rabbit skeletal muscle

Cited by 58 publications

References 27 publications

Distribution of calcium ATPase in the sarcoplasmic reticulum of fast- and slow-twitch muscles determined with monoclonal antibodies

Distribution of calcium ATPase in the sarcoplasmic reticulum of fast- and slow-twitch muscles determined with monoclonal antibodies

Coexpression of two isoforms of calsequestrin in rabbit slow-twitch muscle

Immunochemical quantification of sarcoplasmic reticulum Ca-ATPase, of calsequestrin and of parvalbumin in rabbit skeletal muscles of defined fiber composition

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