A calcium-activated neutral protease in normal and dystrophic human muscle

Kar, Nirmal C.; Pearson, Carl M.

doi:10.1016/0009-8981(76)90175-3

Cited by 135 publications

(47 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The diabetic state does not influence the activity of serum and skeletal muscle CPK (Table 1). In this regard, the diabetic animals differ from those with muscular dystrophy, which had increased intracellular Ca ions (Maunder-Sewry et al, 1980;Bertorini et al, 1982;Oberc et al, 1977;Bodensteiner et al, 1978;Emery and Burt, 1980), CANP activity (Kar and Pearson, 1976;Neerunjun and Dubowitz, 1979) and serum CPK activity (Ebashi et al, 1959). a-actinin is recognized as a structural component of skeletal muscle myofibrils.…”

Section: Discussionmentioning

confidence: 99%

“…The amount of Ca in skeletal muscles of the diabetic KK-CAy and alloxan-diabetic mice is significantly increased, compared with the nondiabetic control (Nakagawa et al, 1989). In Duchenne muscular dystrophy (DMD), Ca in skeletal muscles is reported to be increased (MaunderSewry et al, 1980 ;Bertorini et al, 1982;Oberc and Engel, 1977 ;Bodensteiner and Engel, 1978 ;Emery and Burt, 1980), and Ca-activated neutral proteinase (CANP) is activated in the skeletal muscles (Kar and Pearson, 1976 ;Neerunjun and Dubowitz, 1979). We now report changes in the sensitivity of CANP to Ca2+ in the diabetic state as well as its degradation of Triton X-100-soluble protein components in plasma membranes of skeletal muscles of diabetic KK-CAy and the alloxan-diabetic mice.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Diabetic State-Induced Activation of Calcium-Activated Neutral Proteinase in Mouse Skeletal Muscle.

et al. 1989

View full text Add to dashboard Cite

The effect of a diabetic state in the diabetic KK-CAY mouse on calcium activated neutral proteinase (CANP) of hind-limb skeletal muscles was investigated. In the diabetic state, there was an increased sensitivity to activation of CANP by calcium (Ca). In addition, there was an enhancement of maximal activity of the enzyme. The effect was induced by secondary modification of the diabetic state, but not genetical factors. Several lines of evidence suggest that the CANP is responsible for 92 K dalton protein in diabetic skeletal muscles. Among the evidence are the following:a) The 92 K band in the diabetic muscles was lower than in the prediabetic mouse and restored by the addition of 2mM EDTA and 2mM EGTA, b) The band was reduced by increasing the Ca content and neutral pH in the non-diabetic normal muscles. c) E-64-C, a CANP inhibitor, restored the 92K component reduced by the diabetic state. Since the band in denervated muscles was not changed by the Ca chelating agents, the reduction of the band in the diabetic muscles is related with musclotrophic factors, not diabetic neuropathy.These results suggest that diabetic amyotrophy may be regarded as a phenomenon linked to an increase in intracellular Ca ions and an increase in CANP activity.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Diabetic State-Induced Activation of Calcium-Activated Neutral Proteinase in Mouse Skeletal Muscle.

et al. 1989

View full text Add to dashboard Cite

show abstract

“…After several "re-identifications" [18,65,75,101,130,161], calpain, which was called CANP (calcium-activated neutral protease) at that time, was purified to homogeneity by Ishiura et al in 1978 [68]. In 1980, the endogenous specific inhibitor protein named calpastatin was purified by Murachi et al [109].…”

Section: The History and Nomenclature Of Calpainmentioning

confidence: 99%

Expanding Members and Roles of the Calpain Superfamily and Their Genetically Modified Animals

2010

View full text Add to dashboard Cite

Abstract:Calpains are intracellular Ca 2+ -dependent cysteine proteases (Clan CA, family C02, EC 3.4.22.17) found in almost all eukaryotes and some bacteria. Calpains display limited proteolytic activity at neutral pH, proteolysing substrates to transform and modulate their structures and activities, and are therefore called "modulator proteases". The human genome has 15 genes that encode a calpain-like protease domain, generating diverse calpain homologues that possess combinations of several functional domains such as Ca 2+ -binding domains and Zn-finger domains. The importance of the physiological roles of calpains is reflected in the fact that particular defects in calpain functionality cause a variety of deficiencies in many different organisms, including lethality, muscular dystrophies, lissencephaly, and tumorigenesis. In this review, the unique characteristics of this distinctive protease superfamily are introduced in terms of genetically modified animals, some of which are animal models of calpain deficiency diseases.

show abstract

“…4a indicates 0.2 11m. activities have been measured in many dystrophic animals 22 -24) but the results differ. Kar and Pearson 22 ) found a great increase of CAP activity in Duchenne and Becker dystrophy. Klamut et al 23 ) have shown an increased activity of CAP in hamster skeletal muscles but no elevation in heart and tongue muscle which are usually more severely affected than skeletal muscle.…”

Section: Discussionmentioning

confidence: 94%

Ca²⁺-activated Protease Activity in Vitamin E-Deficient Rats

Otsuka

Kumojima

Ishikawa

et al. 1985

Agricultural and Biological Chemistry

View full text Add to dashboard Cite

A calcium-activated neutral protease in normal and dystrophic human muscle

Cited by 135 publications

References 14 publications

Diabetic State-Induced Activation of Calcium-Activated Neutral Proteinase in Mouse Skeletal Muscle.

Diabetic State-Induced Activation of Calcium-Activated Neutral Proteinase in Mouse Skeletal Muscle.

Expanding Members and Roles of the Calpain Superfamily and Their Genetically Modified Animals

Ca²⁺-activated Protease Activity in Vitamin E-Deficient Rats

Contact Info

Product

Resources

About

A calcium-activated neutral protease in normal and dystrophic human muscle

Cited by 135 publications

References 14 publications

Diabetic State-Induced Activation of Calcium-Activated Neutral Proteinase in Mouse Skeletal Muscle.

Diabetic State-Induced Activation of Calcium-Activated Neutral Proteinase in Mouse Skeletal Muscle.

Expanding Members and Roles of the Calpain Superfamily and Their Genetically Modified Animals

Ca2+-activated Protease Activity in Vitamin E-Deficient Rats

Contact Info

Product

Resources

About

Ca²⁺-activated Protease Activity in Vitamin E-Deficient Rats