Association of calpain (Ca2+-dependent thiol protease) with its endogenous inhibitor calpastatin in myoblasts

Barnoy, Sivia; Zipser, Yehudit; Glaser, Tova; Grimberg, Yelena; Kosower, Nechama S.

doi:10.1002/(sici)1097-4644(19990915)74:4<522::aid-jcb2>3.0.co;2-i

Cited by 46 publications

(7 citation statements)

References 47 publications

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“…Calpains coexist with calpastatin, the endogenous inhibitor in the cell (2). Under normal conditions, calpastatin is localized in specific structures rather than distributed in a diffused form in the cytosol (8).…”

Section: Discussionmentioning

confidence: 99%

Calpains mediate acute renal cell death: role of autolysis and translocation

Liu

Rainey

Harriman

et al. 2001

American Journal of Physiology-Renal Physiology

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The goals of this study were to determine 1) the expression of calpain isoforms in rabbit renal proximal tubules (RPT); 2) calpain autolysis and translocation, and calpastatin levels during RPT injury; and 3) the effect of a calpain inhibitor (PD-150606) on calpain levels, mitochondrial function, and ion transport during RPT injury. RT-PCR, immunoblot analysis, and FITC-casein zymography demonstrated the presence of only mu- and m-calpains in rabbit RPT. The mitochondrial inhibitor antimycin A decreased RPT mu- and m-calpain and calpastatin levels in conjunction with cell death and increased plasma membrane permeability. No increases in either mu- or m-calpain were observed in the membrane nor were increases observed in autolytic forms of either mu- or m-calpain in antimycin A-exposed RPT. PD-150606 blocked antimycin A-induced cell death, preserved calpain levels in antimycin A-exposed RPT, and promoted the recovery of mitochondrial function and active Na+ transport in RPT after hypoxia and reoxygenation. The present study suggests that calpains mediate RPT injury without undergoing autolysis or translocation, and ultimately they leak from cells subsequent to RPT injury/death. Furthermore, PD-150606 allows functional recovery after injury.

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Section: Discussionmentioning

confidence: 99%

Calpains mediate acute renal cell death: role of autolysis and translocation

Liu

Rainey

Harriman

et al. 2001

American Journal of Physiology-Renal Physiology

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“…The aliquots were precleared by rotation at 4 mC for 1 h with 20 µl of Protein A-Sepharose (Amersham Pharmacia Biotech) and 5 µl of normal rabbit serum, then centrifuged. Polyclonal anti-calpain antibody that recognizes the large subunits of both µ-calpain and mcalpain [20] was added to two aliquots, and normal rabbit serum was added to the third. The aliquots were incubated by rotation at 4 mC for 4 h, then mixed with 30 µl of Protein A-Sepharose and samples were incubated for additional 16 h. The samples were then centrifuged, the pellets washed three times with IP buffer, solubilized in Laemmli sample buffer, and separated on SDS\PAGE (7.5 % acrylamide).…”

Section: Metabolic Labelling and Immunoprecipitation (Ip) Of Calpainmentioning

confidence: 99%

Regulation of calpain and calpastatin in differentiating myoblasts: mRNA levels, protein synthesis and stability

Barnoy¹,

SUPINO-ROSIN²,

Kosower³

2000

Biochem. J.

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Calpain (Ca# +-dependent intracellular protease)-induced proteolysis has been considered to play a role in myoblast fusion to myotubes. We found previously that calpastatin (the endogenous inhibitor of calpain) diminishes transiently during myoblast differentiation. To gain information about the regulation of calpain and calpastatin in differentiating myoblasts, we evaluated the stability and synthesis of calpain and calpastatin, and measured their mRNA levels in L8 myoblasts. We show here that µ-calpain and m-calpain are stable, long-lived proteins in both dividing and differentiating L8 myoblasts. Calpain is synthesized in differentiating myoblasts, and calpain mRNA levels do not change during differentiation. In contrast, calpastatin (though also a long-lived protein in myoblasts), is less stable in differentiating myoblasts than in the dividing cells, and its synthesis is inhibited upon initiation of differentiation. Inhibition of cal

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“…Calpain family members are calcium-dependent thiol proteases that carry out intracellular processing of proteins. They have been implicated in calcium-mediated cell-signaling pathways, including those involved in cytoskeleton remodeling, cell cycle regulation, cell differentiation, and membrane fusion (Croall and DeMartino, 1991;Carafoli and Molinari, 1998;Barnoy et al, 1999). They exist as heterodimers of one of various large (~80 kDa) subunits and a common small (~30kDa) subunit (Murachi et al, 1981;Carafoli and Molinari, 1998).…”

Section: Introductionmentioning

confidence: 99%

Calpain 11 is unique to mouse spermatogenic cells

Ben‐Aharon

Brown

Shalgi

et al. 2006

Molecular Reproduction Devel

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The calpains are a family of calcium-dependent thiol proteases involved in intracellular processing of proteins. They occur as heterodimers containing one of various large subunits and a common small subunit. Some of the large subunits are expressed ubiquitously and others are expressed in a restricted set of tissues. We have cloned the cDNA for mouse calpain 11 and demonstrated that it is expressed specifically in the mouse testis. The mRNA begins to accumulate in the testis between days 14 and 16 after birth, corresponding to the period of pachytene spermatocyte development. The protein is detected by day 18 after birth, during mid to late pachytene spermatocyte development, and is present in the acrosomal region of spermatozoa from the cauda epididymis. The expression of calpain 11 during spermatogenesis and its localization in spermatozoa suggest that it is involved in regulating calcium-dependent signal transduction events during meiosis and sperm functional processes.

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Association of calpain (Ca2+-dependent thiol protease) with its endogenous inhibitor calpastatin in myoblasts

Cited by 46 publications

References 47 publications

Calpains mediate acute renal cell death: role of autolysis and translocation

Calpains mediate acute renal cell death: role of autolysis and translocation

Regulation of calpain and calpastatin in differentiating myoblasts: mRNA levels, protein synthesis and stability

Calpain 11 is unique to mouse spermatogenic cells

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