About: Protein Never in Mitosis Gene A Interacting-1 regulates calpain activity and the degradation of cyclooxygenase-2 in endothelial cells

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About: Protein Never in Mitosis Gene A Interacting-1 regulates calpain activity and the degradation of cyclooxygenase-2 in endothelial cells Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Protein Never in Mitosis Gene A Interacting-1 regulates calpain activity and the degradation of cyclooxygenase-2 in endothelial cells
Creator	Huang, Yongcheng Keshvara, Lakhu Liu, Tongzheng Shah, Vaibhav Hoyt, Dale Likhotvorik, Rostislav Schneider, Ryan
Source	Medline; PMC
abstract	BACKGROUND: The peptidyl-proline isomerase, Protein Never in Mitosis Gene A Interacting-1 (PIN1), regulates turnover of inducible nitric oxide synthase (iNOS) in murine aortic endothelial cells (MAEC) stimulated with E. coli endotoxin (LPS) and interferon-γ (IFN). Degradation of iNOS was reduced by a calpain inhibitor, suggesting that PIN1 may affect induction of other calpain-sensitive inflammatory proteins, such as cyclooxygenase (COX)-2, in MAEC. METHODS: MAEC, transduced with lentivirus encoding an inactive control short hairpin (sh) RNA or one targeting PIN1 that reduced PIN1 by 85%, were used. Cells were treated with LPS/IFN, calpain inhibitors (carbobenzoxy-valinyl-phenylalaninal (zVF), PD150606), cycloheximide and COX inhibitors to determine the effect of PIN1 depletion on COX-2 and calpain. RESULTS: LPS or IFN alone did not induce COX-2. However, treatment with 10 μg LPS plus 20 ng IFN per ml induced COX-2 protein 10-fold in Control shRNA MAEC. Induction was significantly greater (47-fold) in PIN1 shRNA cells. COX-2-dependent prostaglandin E2 production increased 3-fold in KD MAEC, but did not increase in Control cells. The additional increase in COX-2 protein due to PIN1 depletion was post-transcriptional, as induction of COX-2 mRNA by LPS/IFN was the same in cells containing or lacking PIN1. Instead, the loss of COX-2 protein, after treatment with cycloheximide to block protein synthesis, was reduced in cells lacking PIN1 in comparison with Control cells, indicating that degradation of the enzyme was reduced. zVF and PD150606 each enhanced the induction of COX-2 by LPS/IFN. zVF also slowed the loss of COX-2 after treatment with cycloheximide, and COX-2 was degraded by exogenous μ-calpain in vitro. In contrast to iNOS, physical interaction between COX-2 and PIN1 was not detected, suggesting that effects of PIN1 on calpain, rather than COX-2 itself, affect COX-2 degradation. While cathepsin activity was unaltered, depletion of PIN1 reduced calpain activity by 55% in comparison with Control shRNA cells. CONCLUSION: PIN1 reduced calpain activity and slowed the degradation of COX-2 in MAEC, an effect recapitulated by an inhibitor of calpain. Given the sensitivity of COX-2 and iNOS to calpain, PIN1 may normally limit induction of these and other calpain substrates by maintaining calpain activity in endothelial cells.
has issue date	2009-06-22(xsd:dateTime)
bibo:doi	10.1186/1476-9255-6-20
bibo:pmid	19545424
has license	cc-by
sha1sum (hex)	d0ce640c27c2c8ef5f83e71bec07d829327d69d6
schema:url	https://doi.org/10.1186/1476-9255-6-20
resource representing a document's title	Protein Never in Mitosis Gene A Interacting-1 regulates calpain activity and the degradation of cyclooxygenase-2 in endothelial cells
has PubMed Central identifier	PMC2708161
has PubMed identifier	19545424
schema:publication	J Inflamm (Lond)
resource representing a document's body	covid:d0ce640c27c2c8ef5f83e71bec07d829327d69d6#body_text
is schema:about of	named entity 'INTERACTING' named entity 'PIN1' named entity 'endothelial cells' named entity 'Inflammation' named entity 'GENE A' named entity 'MAEC' named entity 'REDUCED' named entity 'PIN1' named entity 'ENDOTHELIAL CELLS' named entity 'PROTEIN ' named entity 'AORTIC' named entity 'CYCLOOXYGENASE' named entity 'MURINE' named entity 'NEVER' named entity 'INTERFERON' named entity 'CALPAIN INHIBITOR' named entity 'STIMULATED' named entity 'MITOSIS' named entity 'INFLAMMATORY' named entity 'DEGRADATION' named entity 'ISOMERASE' named entity 'INDUCTION' named entity 'INTERACTING' named entity 'CALPAIN ACTIVITY' named entity 'JOURNAL ' named entity 'DEGRADATION' named entity 'CALPAIN' named entity 'ENDOTHELIAL CELLS' named entity 'NEVER' named entity 'PROTEIN ' named entity 'MITOSIS' named entity 'SENSITIVE' named entity 'INOS' named entity 'PEPTIDYL-PROLINE' named entity 'INDUCIBLE NITRIC OXIDE SYNTHASE' named entity 'AFFECT' named entity 'INFLAMMATION' named entity 'PROTEINS' named entity 'TURNOVER' named entity 'CYCLOOXYGENASE-2' named entity 'ENDOTOXIN' named entity 'E. COLI' named entity 'GENE A' covid:arg/d0ce640c27c2c8ef5f83e71bec07d829327d69d6 named entity 'turnover' named entity 'interferon-γ' named entity 'iNOS' named entity 'calpain' named entity 'proline' named entity 'calpain' named entity 'E. coli' named entity 'PIN1' named entity 'murine' named entity 'interferon-γ' named entity 'endothelial cells' named entity 'inducible nitric oxide synthase' named entity 'endothelial cells' named entity 'Mitosis' named entity 'Protein' named entity 'Cayman Chemical' named entity 'COX-2' named entity 'COX-2' named entity 'PIN1' named entity 'protein' named entity 'NaCl' named entity 'β-actin' named entity 'cDNA' named entity 'mice' named entity 'proline' named entity 'Gels' named entity 'COX-2' named entity 'PIN1' named entity 'amino-terminal' named entity 'prolyl isomerase' named entity 'sonicated'

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