Elevated levels of a calcium-activated muscle protease in rapidly atrophying muscles from vitamin E-deficient rabbits

Dayton, William R; Schollmeyer, Judith V.; Chan, Alvin C.; Allen, C. E.

doi:10.1016/0304-4165(79)90266-6

Cited by 61 publications

(20 citation statements)

References 19 publications

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“…Calpains are activated by calcium, and treatment of purified myofibrils with calcium causes rapid and complete loss of the Z disk (28). Calpains are also activated in conditions of muscle wasting, including vitamin E deficiency (29), Duchenne muscular dystrophy (30), and fasting (31). Calpain mRNA concentrations are increased markedly during fasting (32).…”

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confidence: 99%

Role of calpain in skeletal-muscle protein degradation

Huang

Forsberg

1998

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

296

209

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Although protein degradation is enhanced in muscle-wasting conditions and limits the rate of muscle growth in domestic animals, the proteolytic system responsible for degrading myofibrillar proteins in skeletal muscle is not well defined. The goals of this study were to evaluate the roles of the calpains (calcium-activated cysteine proteases) in mediating muscle protein degradation and the extent to which these proteases participate in protein turnover in muscle. Two strategies to regulate intracellular calpain activities were developed: overexpression of dominant-negative m-calpain and overexpression of calpastatin inhibitory domain. To express these constructs, L8 myoblast cell lines were transfected with LacSwitch plasmids, which allowed for isopropyl ␤-Dthiogalactoside-dependent expression of the gene of interest. Inhibition of calpain stabilized fodrin, a well characterized calpain substrate. Under conditions of accelerated degradation (serum withdrawal), inhibition of m-calpain reduced protein degradation by 30%, whereas calpastatin inhibitory domain expression reduced degradation by 63%. Inhibition of calpain also stabilized nebulin. These observations indicate that calpains play key roles in the disassembly of sarcomeric proteins. Inhibition of calpain activity may have therapeutic value in treatment of muscle-wasting conditions and may enhance muscle growth in domestic animals.

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mentioning

confidence: 99%

Role of calpain in skeletal-muscle protein degradation

Huang

Forsberg

1998

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

296

209

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“…The structural changes observed in rapidly atrophying muscles (Cullen and Pluskal 1977;Cullen and Fulthorpe 1982) are mimicked closely by treatment of myofibrils from normal muscle with µ-calpain (Dayton et al 1981;Goll et al 1991Goll et al , 1992b or m-calpain (Dayton et al 1975(Dayton et al , 1976bGoll et al 1991Goll et al , 1992b. SDS-PAGE has shown that the calpains cause the same degradative changes in myofibrils as those seen in Duchenne muscular dystrophy (Sugita et al 1980) or other rapidly atrophying muscle (Dayton et al 1979;Ishiura et al 1980).…”

Section: Role Of the Calpain System In Skeletal Muscle Growthmentioning

confidence: 93%

The calpain system and skeletal muscle growth

Goll¹,

Thompson²,

Taylor³

et al. 1998

Can. J. Anim. Sci.

109

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. 1998. The calpain system and skeletal muscle growth. Can. J. Anim. Sci. 78: 503-512. The first protein of a group of proteins now identified as belonging to the calpain system was purified in 1976. The calpain system presently is known to be constituted of three well-characterized proteins; several lesser studied proteins that have been isolated from invertebrates; and 10 mRNAs, two each in Drosophila and C. elegans and six in vertebrates, that encode proteins, which, based on sequence homology, belong to the calpain family. The three well-characterized proteins in the calpain family include two Ca 2+ -dependent proteolytic enzymes, µ-calpain and m-calpain, and a protein, calpastatin, that has no known activity other than to inhibit the two calpains. A substantial amount of experimental evidence accumulated during the past 25 yr has shown that the calpain system has an important role both in rate of skeletal muscle growth and in rate and extent of postmortem tenderization. Calpastatin seems to be the variable component of the calpain system, and skeletal muscle calpastatin activity is highly related to rate of muscle protein turnover and rate of postmortem tenderization. The current paradigm is that high calpastatin activity: 1) decreases rate of muscle protein turnover and hence is associated with an increased rate of skeletal muscle growth; and 2) decreases calpain activity in postmortem muscle and hence is associated with a lower rate of postmortem tenderization. This article summarizes some of the known properties of the calpain system and discusses the potential importance of the calpain system to animal science.Key words: Calpain, calpastatin, postmortem tenderization, skeletal muscle growth Goll, D. E., Thompson, V. F., Taylor, R. G. et Ouali, A. 1998. Le système des calpaïnes et la croissance des muscles squeletiques. Can. J. Anim. Sci. 78: 503-512. La première protéine d'un groupe désormais identifié comme appartenant au système des calpaïnes a été purifiée en 1976. On sait aujourd'hui que ce système comprend trois protéines bien caractérisées. Plusieurs protéines moins étudiées, isolées chez les invertébrés et 10 ARNm codant pour les protéines,dont deux chacun trouvés chez Drosophila et chez C. elegans et six, chez les vertébrés, appartiendraient également d'après l'homologie séquentielle à la famille des calpaïnes. Les trois protéines bien caractérisées, mentionnées plus haut, comprennent deux enzymes protéolytiques Ca 2+ -dépendantes, la µ-calpaïne et la m-calpaïne, et une protéine, la calpastatine qui semble n'avoir d'autre fonction que d'inhiber l'activité des deux calpaïnes. Un corpus substantiel d'évidence expérimentale accumulé au cours des 25 dernières années révèle que le système des calpaïnes joue un rôle important à la fois à l'égard du taux de croissance des muscules squelettiques et du degré d'attendrissage de la viande postmortem. La calpastatine semble être la composante variable du système et son activité dans les muscles squelettiques est étroitement reliée au taux de renouvellement ...

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“…Since calpain has the ability to degrade myofibrillar proteins, especially at the Z line (Dayton et al 1975), a plausible model in which calpain initiates the limited proteolysis of the contractile proteins which are then taken into the lysosomes has been discussed (Gerard & Schneider, 1980;Kay, 1983;Pemrick & Grebenau, 1984). However, while increased calpain activity has been associated with increased proteolysis in atrophying or dystrophic muscle (Kar & Pearson, 1976;Dayton et al 1979), muscle calpain and calpastatin activity in chicks growing normally, albeit at different rates, in response to dietary protein levels did not vary (Ballard et al 1988). Chicken calpain in vitro, however, requires a relatively high Ca2+ concentration for activity, in excess of expected physiological levels.…”

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confidence: 99%

The relation between dietary restriction or clenbuterol (a selective β2 agonist) treatment on muscle growth and calpain proteinase (EC3.4.22.17) and calpastatin activities in lambs

et al. 1988

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I. Lamb growth trials were designed to modify growth and protein content of muscle by diet and also by P-agonist treatment, and to correlate any changes to the activities of calpain proteinases (EC 3.4.22.17) and their inhibitor calpastatin.2. Wether lambs in a control group were fed on a barley-based diet designed to give a growth rate of 350 g/d; a second group was fed on the same diet but the intake was restricted to give an expected gain of 44 g/d; a third group was fed on the same diet as the first group but the diet included 2 mg clenbuterol/kg. At the end of a 6-week trial, longissimus dorsi wet weights were 635 (n6), 377 (n4) and 788 g (n6) (standard error of difference 53.0) in the three groups respectively.3. Minced L. dorsi was extracted in low-salt buffers and analysed by a fast protein liquid-chromatographic system for calpain I (low calcium-requiring), calpain 11 (high Ca2+-requiring) and calpastatin activities. No significant changes in the three activities were associated with reduced muscle weight in the restricted-intake group. The inclusion of clenbuterol in the diet, however, led to highly significant increases (P i 0001) in calpain I1 and calpastatin to approximately double the control values.4. The results did not support a direct relation between these activities and muscle growth, except when protein accretion was stimulated by a P-agonist, suggesting a role for this enzyme system in the mechanism by which these agents exert their effect.

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Elevated levels of a calcium-activated muscle protease in rapidly atrophying muscles from vitamin E-deficient rabbits

Cited by 61 publications

References 19 publications

Role of calpain in skeletal-muscle protein degradation

Role of calpain in skeletal-muscle protein degradation

The calpain system and skeletal muscle growth

The relation between dietary restriction or clenbuterol (a selective β2 agonist) treatment on muscle growth and calpain proteinase (EC3.4.22.17) and calpastatin activities in lambs

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