Mitochondrial calpain 10 activity and expression in the kidney of multiple species

Giguere, Christopher J.; Covington, Marisa D.; Schnellmann, Rick G.

doi:10.1016/j.bbrc.2007.11.133

Cited by 23 publications

(11 citation statements)

References 25 publications

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“…In other words, it is possible that calpain-3 may interact with RyR and/or triadin in the RyR-triadin-CSQ1 complex that spans the SR membrane. Alternatively, it is also possible that calpain-3 is located in the luminal SR, since other calpain members have been reported to exist in luminal compartments of organelles such as mitochondria 23,24,25,26. Further study is required to clarify the interaction of calpain-3 with CSQ1.…”

Section: Discussionmentioning

confidence: 99%

Non-Proteolytic Functions of Calpain-3 in Sarcoplasmic Reticulum in Skeletal Muscles

Ojima

Ono

Ottenheijm

et al. 2011

Journal of Molecular Biology

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Mutations in CAPN3/Capn3, which codes for skeletal muscle-specific calpain-3/p94 protease, are responsible for limb-girdle muscular dystrophy type 2A (LGMD2A). Using "knock-in" (referred to as Capn3 CS/CS ) mice, in which the endogenous calpain-3 is replaced with a mutant calpain-3:C129S, that is proteolytically inactive but structurally intact calpain-3, our previous studies demonstrated that loss of calpain-3 protease activity caused muscular dystrophy. However, compared to Capn3 null (Capn3 −/− ) mice, Capn3 CS/CS mice showed less severe dystrophic symptoms. This suggests that calpain-3 also has a non-proteolytic function. This study aimed to elucidate non-protease calpain-3 functions, by comparison of Capn3 CS/CS mice with Capn3 −/− mice. We found that calpain-3 is a component of the sarcoplasmic reticulum (SR), and that calpain-3 interacts with, but does not proteolyze, typical SR components such as ryanodine receptor and calsequestrin. Furthermore, Capn3 CS/CS mice showed that the non-enzymatic role of calpain-3 is required for proper Ca 2+ efflux from the SR to cytosol during contraction of muscles. These results indicate that calpain-3 functions as a non-enzymatic element for the Ca 2+ efflux machinery in the SR rather than as a protease. Thus, defects of the non-enzymatic function of calpain-3 must also be involved in pathogenesis of LGMD2A.

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Section: Discussionmentioning

confidence: 99%

Non-Proteolytic Functions of Calpain-3 in Sarcoplasmic Reticulum in Skeletal Muscles

Ojima

Ono

Ottenheijm

et al. 2011

Journal of Molecular Biology

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“…In renal mitochondria, activation of mitochondrial calpain 10 impairs the electron transport chain by proteolytic digestion of complex I subunits [35,86]. Genetic ablation of complex I subunits sensitizes to the MPTP opening in mouse heart mitochondria [87].…”

Section: Mitochondrial Calpain 1 Within the Matrixmentioning

confidence: 99%

Heart mitochondria and calpain 1: Location, function, and targets

Chen¹,

Lesnefsky²

2015

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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Calpain 1 is an ubiquitous Ca(2+)-dependent cysteine protease. Although calpain 1 has been found in cardiac mitochondria, the exact location within mitochondrial compartments and its function remain unclear. The aim of the current review is to discuss the localization of calpain 1 in different mitochondrial compartments in relationship to its function, especially in pathophysiological conditions. Briefly, mitochondrial calpain 1 (mit-CPN1) is located within the intermembrane space and mitochondrial matrix. Activation of the mit-CPN1 within intermembrane space cleaves apoptosis inducing factor (AIF), whereas the activated mit-CPN1 within matrix cleaves complex I subunits and metabolic enzymes. Inhibition of the mit-CPN1 could be a potential strategy to decrease cardiac injury during ischemia-reperfusion.

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“…Calpain 10 is a ubiquitous calpain (30) and our laboratory showed that calpain 10 is resident in kidney mitochondria of rabbits, rats, and mice (4,16). Arrington et al (4) identified calpain 10 as a mitochondrial calpain capable of cleaving complex 1 proteins (ND6 and NDUFV2) and inhibiting state 3 respiration after mitochondrial Ca 2ϩ overload.…”

mentioning

confidence: 97%

Calpain 10 is required for cell viability and is decreased in the aging kidney

Covington¹,

Arrington²,

Schnellmann³

2009

American Journal of Physiology-Renal Physiology

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Aging is associated with abnormalities in kidney function, but the exact mechanisms are unknown. We examined calpains 1, 2, and 10 protein levels in kidneys from rats, mice, and humans of various ages and determined whether calpain 10 is required for cell viability. Calpain 10 protein expression decreased in the kidney, but not in the liver, of aging Fischer 344 rats, and this decrease was attenuated with caloric restriction. There was no change in calpains 1 or 2 levels in the kidney or liver in control and caloric-restricted aging rats. Aging mice also exhibited decreased calpain 10 protein levels. Calpain 10 protein and mRNA levels decreased linearly in human kidney samples with age in the absence of changes in calpains 1 or 2. Our laboratory previously found calpain 10 to be expressed in both the cytosol and mitochondria of rabbit renal proximal tubular cells (RPTC). Adenoviral-delivered shRNA to rabbit RPTC decreased mitochondrial calpain 10 expression below detectable levels by 3 days while cytosolic calpain 10 levels remained unchanged at 3 days and decreased to approximately 20% of control by 5 days. Knockdown of mitochondrial calpain 10 resulted in nuclear condensation and cleaved procaspase 3, markers of apoptosis. In summary, mitochondrial calpain 10 is required for cell viability and calpain 10 levels specifically decrease in aging rat, mice, and human kidney tissues when renal function decreases, suggesting that calpain 10 is required for renal function and is a biomarker of the aging kidney.

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Mitochondrial calpain 10 activity and expression in the kidney of multiple species

Cited by 23 publications

References 25 publications

Non-Proteolytic Functions of Calpain-3 in Sarcoplasmic Reticulum in Skeletal Muscles

Non-Proteolytic Functions of Calpain-3 in Sarcoplasmic Reticulum in Skeletal Muscles

Heart mitochondria and calpain 1: Location, function, and targets

Calpain 10 is required for cell viability and is decreased in the aging kidney

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