Source:http://linkedlifedata.com/resource/pubmed/id/19945429
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions |
umls-concept:C0020289,
umls-concept:C0026844,
umls-concept:C0041538,
umls-concept:C0109317,
umls-concept:C0205088,
umls-concept:C0596260,
umls-concept:C0752312,
umls-concept:C0851285,
umls-concept:C1150579,
umls-concept:C1333340,
umls-concept:C1366882,
umls-concept:C1370600,
umls-concept:C1658578,
umls-concept:C1705767,
umls-concept:C1705791,
umls-concept:C1879547
|
pubmed:issue |
1
|
pubmed:dateCreated |
2010-1-27
|
pubmed:abstractText |
Deubiquitinating enzymes (DUBs) appear to be critical regulators of a multitude of processes such as proliferation, apoptosis, differentiation, and inflammation. We have recently demonstrated that a DUB of ubiquitin carboxyl terminal hydrolase L1 (UCH-L1) inhibits vascular lesion formation via suppressing inflammatory responses in vasculature. However, the precise underlying mechanism remains to be defined. Herein, we report that a posttranscriptional up-regulation of UCH-L1 provides a negative feedback to tumor necrosis factor alpha (TNFalpha)-mediated activation of extracellular signal-regulated kinases (ERK) and proliferation in vascular smooth muscle cells (VSMCs). In rat adult VSMCs, adenoviral over-expression of UCH-L1 inhibited TNFalpha-induced activation of ERK and DNA synthesis. In contrast, over-expression of UCH-L1 did not affect platelet derived growth factor (PDGF)-induced VSMC proliferation and activation of growth stimulating cascades including ERK. TNFalpha hardly altered UCH-L1 mRNA expression and stability; however, up-regulated UCH-L1 protein expression via increasing UCH-L1 translation. These results uncover a novel mechanism by which UCH-L1 suppresses vascular inflammation.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Signal-Regulated MAP...,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/UCHL1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin Thiolesterase
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
1090-2104
|
pubmed:author | |
pubmed:copyrightInfo |
Copyright 2009 Elsevier Inc. All rights reserved.
|
pubmed:issnType |
Electronic
|
pubmed:day |
1
|
pubmed:volume |
391
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
852-6
|
pubmed:dateRevised |
2011-9-22
|
pubmed:meshHeading |
pubmed-meshheading:19945429-Animals,
pubmed-meshheading:19945429-Cell Proliferation,
pubmed-meshheading:19945429-Cells, Cultured,
pubmed-meshheading:19945429-Enzyme Activation,
pubmed-meshheading:19945429-Extracellular Signal-Regulated MAP Kinases,
pubmed-meshheading:19945429-Humans,
pubmed-meshheading:19945429-Muscle, Smooth, Vascular,
pubmed-meshheading:19945429-Myocytes, Smooth Muscle,
pubmed-meshheading:19945429-Protein Biosynthesis,
pubmed-meshheading:19945429-Rats,
pubmed-meshheading:19945429-Rats, Sprague-Dawley,
pubmed-meshheading:19945429-Tumor Necrosis Factor-alpha,
pubmed-meshheading:19945429-Ubiquitin Thiolesterase,
pubmed-meshheading:19945429-Vasculitis
|
pubmed:year |
2010
|
pubmed:articleTitle |
Ubiquitin carboxyl terminal hydrolase L1 negatively regulates TNFalpha-mediated vascular smooth muscle cell proliferation via suppressing ERK activation.
|
pubmed:affiliation |
Department of Cell Biology and Anatomy, University of South Carolina School of Medicine, Columbia, SC 29208, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|