150-kDa oxygen-regulated protein attenuates myocardial ischemia–reperfusion injury in rat heart

Aleshin, Alexey N.; Sawa, Yoshiki; Kitagawa-Sakakida, Satoru; Bandô, Yoshio; Ono, Masamichi; Memon, Imran A.; Tohyama, Masaya; Ogawa, Satoshi; Matsuda, Hikaru

doi:10.1016/j.yjmcc.2005.01.001

Cited by 31 publications

(40 citation statements)

References 37 publications

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“…Transgenic mice and Madin-Darby canine kidney cells exposed to hypoxic conditions in this study had decreased caspase 3 activation. Similarly, the same investigators showed a protective role for ORP150 after myocardial infarction in the rat heart (1). Rat hearts infected with adenovirus expressing ORP150 exhibited a blunting in Ca 2ϩ release, cellular calpain activity, cytochrome c release, and caspase 3 activation.…”

mentioning

confidence: 70%

“…Recent studies using cardiac ischemia as a model system revealed that the overexpression of ORP150 negatively regulates cytosolic calpain activity by blocking the ischemia-induced release of ER Ca 2ϩ stores (1). Given that ORP150 (this work) and calpain 10 (2) are both localized to the mitochondrial matrix, we sought to determine whether these proteins interacted within isolated mitochondria.…”

Section: Orp150 Expression Is Regulated By the Transcription Factor Cmentioning

confidence: 99%

“…The functions of ORP150 have not been fully elucidated, but it appears to play a role in apoptosis (1, 6, 12-14, 21, 23, 24, 27, 30), insulin secretion (15,16), protein transport (26), and wound healing (26,31). Much of what is known about ORP150 arises from studies utilizing antisense, adenovirus-mediated, or whole animal knockdown of protein expression (1,6,14). These studies have shown the importance of ORP150 in protecting cells from ischemia-reperfusion injury in neural, cardiac, and renal in vivo models (1,6,12).…”

mentioning

confidence: 99%

“…Much of what is known about ORP150 arises from studies utilizing antisense, adenovirus-mediated, or whole animal knockdown of protein expression (1,6,14). These studies have shown the importance of ORP150 in protecting cells from ischemia-reperfusion injury in neural, cardiac, and renal in vivo models (1,6,12). Similarly, ORP150 has been shown to provide anti-apoptotic signals in neuronal cell models (14,23,24,27,30) and in a variety of cancers such as prostate (22), breast (32), and bladder (3,17) as well as decreasing the metastatic potential of these tumor lines (18).…”

mentioning

confidence: 99%

“…The mitochondrial localization of ORP150 would provide insight into the cytoprotective and anti-apoptotic activities of this molecule observed in various in vitro and in vivo models. The preservation of mitochondrial energy production due to chaperone activity could also explain the potent protection observed during whole organ ischemia-reperfusion injury (1,6,12).…”

mentioning

confidence: 99%

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Targeting of the molecular chaperone oxygen-regulated protein 150 (ORP150) to mitochondria and its induction by cellular stress

Arrington

Schnellmann²

2008

American Journal of Physiology-Cell Physiology

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Arrington DD, Schnellmann RG. Targeting of the molecular chaperone oxygen-regulated protein 150 (ORP150) to mitochondria and its induction by cellular stress. Am J Physiol Cell Physiol 294: C641-C650, 2008. First published December 19, 2007 doi:10.1152/ajpcell.00400.2007 is an inducible endoplasmic reticulum (ER) chaperone molecule that is upregulated after numerous cellular insults and has a cytoprotective role in renal, neural, and cardiac models of ischemiareperfusion injury. ORP150 also has been shown to play a role in cellular Ca 2ϩ homeostasis, and in turn, regulating calpain activity. In this study, we identified ORP150 in whole rat renal cortical mitochondria and matrix fractions, demonstrated the targeting of an ORP150-GFP construct to the mitochondria of NIH-3T3 cells, and showed that the NH2-terminal 13 amino acids of ORP150 are sufficient for this translocation. ORP150 expression was found to be regulated by the anti-C/enhancer-binding protein homologous protein (CHOP)/ GADD153 transcription factor and ORP150 levels increased in the mitochondria and ER of COS-7 cells after diverse stresses, including hypoxia, serum starvation, prolyl hydroxylase inhibition with dimethyloxaloylglycine, and exposure to tunicamycin, ethidium, bromide, and 2-deoxyglucose. Induction of the mitochondrial specific stress response in COS-7 cells through expression of an ornithine transcarbamylase mutant (⌬OTC) increased mitochondrial ORP150 levels and mitochondrial calpain activity. To determine whether mitochondrial ORP150 and mitochondrial calpain 10 interact, rat cortical mitochondria exposed to Ca 2ϩ resulted in ORP150 cleavage in a calpain inhibitor-dependent manner, revealing that ORP150 is a substrate and may be regulated by calpain 10. These data reveal a novel cellular localization for ORP150 and that mitochondrial ORP150 is upregulated by CHOP/GADD153 in response to mitochondrial and ER stress. Our data also reveal that ORP150 is a substrate for mitochondrial calpain 10.

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mentioning

confidence: 70%

Section: Orp150 Expression Is Regulated By the Transcription Factor Cmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Targeting of the molecular chaperone oxygen-regulated protein 150 (ORP150) to mitochondria and its induction by cellular stress

Arrington

Schnellmann²

2008

American Journal of Physiology-Cell Physiology

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Identification of osteocyte‐selective proteins

et al. 2010

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Since little is known regarding osteocytes, cells embedded within the mineralized bone matrix, a proteomics approach was used to discover proteins more highly expressed in osteocytes than in osteoblasts to determine osteocyte specific function. Two proteomic profiles obtained by two different proteomic approaches using total cell lysates from the osteocyte cell line MLO-Y4 and the osteoblast cell line MC3T3 revealed unique differences. Three protein clusters, one related to glycolysis, (Phosphoglycerate kinase 1, fructose-bisphosphate aldolase A, hypoxia up-regulated 1 [ORP150], triosephosphate isomerase), one to protein folding (Mitochondrial Stress-70 protein, ORP150, Endoplasmin), and one to actin cytoskeleton regulation (Macrophage-capping protein [CapG], destrin, forms of lamin A and vimentin) were identified. Higher protein expression of ORP-150, Cap G, and destrin in MLO-Y4 cells compared to MC3T3 cells was validated by gene expression, Western blotting, and in vivo expression. These proteins were shown to be selective in osteocytes in vivo using immuno-staining of mouse ulnae. Destrin was most highly expressed in embedding osteoid osteocytes, GapG in embedded osteocytes, and ORP150 in deeply embedded osteocytes. In summary, the proteomic approach has yielded important information regarding molecular mechanisms used by osteocytes for embedding in matrix, the formation of dendritic processes, and protection within a hypoxic environment.

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Endoplasmic Reticulum Stress: An Opportunity for Neuroprotective Strategies After Stroke

Louessard

Lemarchand

Ali

et al. 2017

Springer Series in Translational Stroke Research

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150-kDa oxygen-regulated protein attenuates myocardial ischemia–reperfusion injury in rat heart

Cited by 31 publications

References 37 publications

Targeting of the molecular chaperone oxygen-regulated protein 150 (ORP150) to mitochondria and its induction by cellular stress

Targeting of the molecular chaperone oxygen-regulated protein 150 (ORP150) to mitochondria and its induction by cellular stress

Identification of osteocyte‐selective proteins

Endoplasmic Reticulum Stress: An Opportunity for Neuroprotective Strategies After Stroke

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