Linked Life Data

9624159

Source:http://linkedlifedata.com/resource/pubmed/id/9624159

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1998-7-9
pubmed:databankReference
pubmed:abstractText
Phenotypic modulation of vascular smooth muscle cells plays an important role in the pathogenesis of arteriosclerosis. In a screen of proteins expressed in human aortic smooth muscle cells, we identified a novel gene product designated aortic carboxypeptidase-like protein (ACLP). The approximately 4-kilobase human cDNA and its mouse homologue encode 1158 and 1128 amino acid proteins, respectively, that are 85% identical. ACLP is a nonnuclear protein that contains a signal peptide, a lysine- and proline-rich 11-amino acid repeating motif, a discoidin-like domain, and a C-terminal domain with 39% identity to carboxypeptidase E. By Western blot analysis and in situ hybridization, we detected abundant ACLP expression in the adult aorta. ACLP was expressed predominantly in the smooth muscle cells of the adult mouse aorta but not in the adventitia or in several other tissues. In cultured mouse aortic smooth muscle cells, ACLP mRNA and protein were up-regulated 2-3-fold after serum starvation. Using a recently developed neural crest cell to smooth muscle cell in vitro differentiation system, we found that ACLP mRNA and protein were not expressed in neural crest cells but were up-regulated dramatically with the differentiation of these cells. These results indicate that ACLP may play a role in differentiated vascular smooth muscle cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15654-60
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9624159-Adult, pubmed-meshheading:9624159-Amino Acid Sequence, pubmed-meshheading:9624159-Animals, pubmed-meshheading:9624159-Base Sequence, pubmed-meshheading:9624159-Carboxypeptidases, pubmed-meshheading:9624159-Cell Differentiation, pubmed-meshheading:9624159-DNA, Complementary, pubmed-meshheading:9624159-Fungal Proteins, pubmed-meshheading:9624159-Humans, pubmed-meshheading:9624159-Lectins, pubmed-meshheading:9624159-Mice, pubmed-meshheading:9624159-Molecular Sequence Data, pubmed-meshheading:9624159-Muscle, Smooth, pubmed-meshheading:9624159-Muscle, Smooth, Vascular, pubmed-meshheading:9624159-Neural Crest, pubmed-meshheading:9624159-Protein Conformation, pubmed-meshheading:9624159-Protein Sorting Signals, pubmed-meshheading:9624159-Proteins, pubmed-meshheading:9624159-Protozoan Proteins, pubmed-meshheading:9624159-RNA, Messenger, pubmed-meshheading:9624159-Repressor Proteins, pubmed-meshheading:9624159-Up-Regulation
pubmed:year
1998
pubmed:articleTitle
Aortic carboxypeptidase-like protein, a novel protein with discoidin and carboxypeptidase-like domains, is up-regulated during vascular smooth muscle cell differentiation.
pubmed:affiliation
Cardiovascular Biology Laboratory, Harvard School of Public Health, Boston, Massachusetts 02115, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't