Linked Life Data

11368520

Source:http://linkedlifedata.com/resource/pubmed/id/11368520

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-5-22
pubmed:databankReference
pubmed:abstractText
A protein possessing vascular smooth muscle cell (SMC) growth-promoting activity (VSGP) was purified from bovine ovarian follicular fluid. The purified protein showed a broad band on SDS-PAGE with an apparent molecular mass of 90-100 kDa. The purified protein was characterized by amino acid sequence analysis of its N-terminal and internal peptides. Based on the information of the peptide sequences, bovine ovarian cDNA library was screened and cDNA clones encoding the protein were isolated. Human homolog of the protein was also cloned from human ovarian cDNA library. Nucleotide sequence analysis revealed that bovine VSGP transcript has a 2421-bp open reading frame, which encodes a protein of 807 amino acid residues. A homology search indicated that bovine and human VSGP are counterparts of rat F-spondin, which has been previously identified as a promoter molecule of neurite extension in rat fetal floor plate. RNA blot analysis showed wide distribution of VSGP/F-spondin transcripts in fetal and adult human tissues. Especially the expression was highest in the adult human ovary. The purified bovine VSGP/F-spondin showed vascular SMC growth promoting activity with an ED(50) value of 10(-8) M. Together with these findings, we demonstrated here that VSGP/F-spondin is a major factor for vascular SMC proliferation in the ovary. In conclusion, our present study provides a distinct and important function of VSGP/F-spondin as a strong VSMC proliferation promoting factor, in addition to the previously proposed function in neuronal system, and also provides insight into mechanisms underlying vascular SMC proliferation during ovarian folliculogenesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0003-9861
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
390
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
93-100
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:11368520-Amino Acid Sequence, pubmed-meshheading:11368520-Animals, pubmed-meshheading:11368520-Base Sequence, pubmed-meshheading:11368520-Cattle, pubmed-meshheading:11368520-Cell Division, pubmed-meshheading:11368520-Cloning, Molecular, pubmed-meshheading:11368520-DNA, Complementary, pubmed-meshheading:11368520-DNA Primers, pubmed-meshheading:11368520-Extracellular Matrix Proteins, pubmed-meshheading:11368520-Female, pubmed-meshheading:11368520-Follicular Fluid, pubmed-meshheading:11368520-Growth Substances, pubmed-meshheading:11368520-Humans, pubmed-meshheading:11368520-Molecular Sequence Data, pubmed-meshheading:11368520-Muscle, Smooth, Vascular, pubmed-meshheading:11368520-Ovary, pubmed-meshheading:11368520-Peptides, pubmed-meshheading:11368520-RNA, Messenger, pubmed-meshheading:11368520-Sequence Homology, Amino Acid
pubmed:year
2001
pubmed:articleTitle
Isolation and characterization of vascular smooth muscle cell growth promoting factor from bovine ovarian follicular fluid and its cDNA cloning from bovine and human ovary.
pubmed:affiliation
Department of Biochemistry, Fukui Medical University, Shimoaizuki, Matsuoka, Fukui 910-1193, Japan. kmiyamot@fmsrsa.fukui-med.ac.jp
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't