Immunocytochemical localization of a calcium-activated protease in skeletal muscle cells

Dayton, William R; Schollmeyer, Judith V.

doi:10.1016/0014-4827(81)90022-7

Cited by 71 publications

(20 citation statements)

References 26 publications

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“…5 4 0 times higher than control levels. Additionally, immunocytochemical localization of the 80 kDa subunit of CANP at the Zdisk of purified porcine myofibrils and in sectioned tissue (Dayton & Schollmeyer, 1981), further supports the theory that the proteinase plays a role in myofibrillar degradation, at least in pathological situations.…”

mentioning

confidence: 51%

Changes in the activity of skeletal muscle calcium-activated neutral proteinase (EC3. 4. 22. 17) and its specific inhibitor in chickens grown at different rates in response to graded levels of dietary protein

1988

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1. Two experiments are reported in which the effect of alteration in growth rate on the levels of avian skeletal muscle calcium-activated neutral proteinase (EC 3 . 4 . 2 2 . 17) (CANP or calpam) and its specific inhibitor (calpastatin), a system thought to be implicated in myofibrillar catabolism, was studied by means of manipulation of dietary protein concentration.2. In Expt 1 broiler chicks were given free access to diets containing 105, 149, 197 and 212 g protein/kg for 20 d. In Expt 2 the four dietary treatments were 119, 141, 182 and 227 g protein/kg diet given for 16 d. Chick growth rate and total leg skeletal muscle weight significantly increased ( P < 0.001) with increasing dietary protein concentration in both experiments. Total skeletal muscle protein increased with the level of dietary protein, the effect being significant ( P i 0.01 and P < 0,001 in Expts 1 and 2 respectively).3. Minced leg muscle was homogenized in low-salt buffers, and the extract chromatographed on DEAEcellulose to separate proteinase and inhibitor activity. The partially purified CANP enzyme and inhibitor proteins were present at a concentration broadly consistent with literature reports, and their elution characteristics and Ca" concentration dependence were not varied by dietary protein concentration.4. Both the muscle CANP and CANP inhibitor activities (units/kg muscle) exhibited upward trends with growth rate and increased muscle weight. However, these differences were not statistically significant ( P > 0.05) and were not present at all when the results were expressed as units/g muscle protein.

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mentioning

confidence: 51%

Changes in the activity of skeletal muscle calcium-activated neutral proteinase (EC3. 4. 22. 17) and its specific inhibitor in chickens grown at different rates in response to graded levels of dietary protein

1988

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“…Both calpain 1 and calpain 2 are present in moderate amounts within the muscle where they are localized to the Z disk of muscle fibers 27, 28 and have been associated with the in vitro degradation of sarcomeric proteins such as α-tropomyosin 29, 30 . The majority of the studies looking at calpain activity in the heart have focused on the role of this proteolytic system in response to pathological cardiac conditions, such as post-ischemic cardiac injury 31-33 .…”

Section: Calpains In the Heart In Health And Diseasementioning

confidence: 99%

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Patterson

Portbury

Schisler

et al. 2011

Circulation Research

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Cardiac hypertrophy develops most commonly in response to hypertension and is an independent risk factor for the development of heart failure. The mechanisms by which cardiac hypertrophy may be reversed to reduce this risk have not been fully determined to the point where mechanism-specific therapies have been developed. Recently, proteases in the calpain family have been implicated in regulating the development of cardiac hypertrophy in preclinical animal models. In this review, we summarize the molecular mechanisms by which calpain inhibition has been shown to modulate the development of cardiac (specifically ventricular) hypertrophy. The context within which calpain inhibition might be developed for therapeutic intervention of cardiac hypertrophy is then discussed.

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“…overload has been correlated with Z lines dissolution and/or myofibrillar disruption [21][22] and calpain is localised to the Z lines of myofibrils [23]. Second, contraction bands have also been observed in post-ischaemic reperfusion of myocardium [24] and these conditions are known to alter calpain activity [7].…”

Section: +mentioning

confidence: 99%

The Calpain-Calpastatin System and the Calcium Paradox in the Isolated Perfused Pigeon Heart

Gaitanaki

Papazafiri²,

Beis³

2003

Cell Physiol Biochem

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To examine whether the calpain-calpastatin system is activated during the calcium paradox in the isolated perfused pigeon heart, we separated the protease from its inhibitor calpastatin and studied its kinetic properties. The protease exhibits kinetic properties similar to those of mammalian m-calpains. Ca²⁺ requirements for half and maximum activities are 220 µM and 2 mM, respectively. In the absence of Ca²⁺ the protease is strongly activated by Mn²⁺ or Sr²⁺. In the presence of Ca²⁺, Mn²⁺ and Sr²⁺ exhibit a synergistic effect; Mg²⁺ and Ba²⁺ have no effect, whereas Co²⁺, Ni²⁺ and Cd²⁺ completely inhibit its activation. Furthermore, we measured the activity of calpain and calpastatin under either conditions inducing a calcium paradox, or protecting the heart against this phenomenon. Although the calpain/calpastatin ratio is lowered during Ca²⁺ depletion, during Ca²⁺ repletion it is markedly inverted. Calpain activation during reperfusion is inhibited by the presence of 200 µM Mn²⁺ or Ba²⁺, in the Ca²⁺-free medium. Gel filtration of calpastatin, isolated from either untreated hearts or during Ca²⁺ depletion, produces two main peaks of ñ150 and 40 kDa of molecular mass, respectively, whereas calpastatin isolated during the 2^nd min of reperfusion appears to be shifted to the 150 kDa form. All the above data suggest that this system may be involved in the induction of the calcium paradox in pigeon heart.

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Immunocytochemical localization of a calcium-activated protease in skeletal muscle cells

Cited by 71 publications

References 26 publications

Changes in the activity of skeletal muscle calcium-activated neutral proteinase (EC3. 4. 22. 17) and its specific inhibitor in chickens grown at different rates in response to graded levels of dietary protein

Changes in the activity of skeletal muscle calcium-activated neutral proteinase (EC3. 4. 22. 17) and its specific inhibitor in chickens grown at different rates in response to graded levels of dietary protein

Tear Me Down

The Calpain-Calpastatin System and the Calcium Paradox in the Isolated Perfused Pigeon Heart

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