Linked Life Data

10575000

Source:http://linkedlifedata.com/resource/pubmed/id/10575000

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
49
pubmed:dateCreated
2000-2-3
pubmed:databankReference
pubmed:abstractText
We have shown previously that vascular endothelial growth factor (VEGF) synthesized by the cellular constituents of small vessels per se, viz. endothelial cells and pericytes, participates in the hypoxia-driven proliferation of both cell types (Nomura, M., Yamagishi, S., Harada, S., Hayashi, Y., Yamashima, T., Yamashita, J., Yamamoto, H. (1995) J. Biol. Chem. 270, 28316-28324; Yamagishi, S., Yonekura, H., Yamamoto, Y., Fujimori, H., Sakurai, S., Tanaka, N., and Yamamoto, H. (1999) Lab. Invest. 79, 501-509). In this study, we examined the expression of the recently isolated VEGF gene family members (placenta growth factor (PlGF), VEGF-B, and VEGF-C) in human dermal microvascular endothelial cells and bovine retinal pericytes cultured under various oxygen tensions. Quantitative reverse transcription-polymerase chain reaction analyses demonstrated that the two cell types possess not only VEGF (VEGF-A) mRNA, but also VEGF-B, VEGF-C, and PlGF mRNAs. Among them, only VEGF-A mRNA was induced under hypoxia. Competitive reverse transcription-polymerase chain reaction showed that, under normoxic conditions, the rank order of mRNA content in endothelial cells was PlGF > VEGF-B > VEGF-C > VEGF-A and that mRNA coding for PlGF was expressed at >100-fold higher levels than VEGF-A mRNA. In pericytes, the rank order was VEGF-C > VEGF-A > VEGF-B > PlGF, and approximately 7-fold higher levels of VEGF-C mRNA compared with VEGF-A mRNA were noted in this cell type. Furthermore, antisense inhibition of PlGF protein production lowered the endothelial cell synthesis of DNA under hypoxic conditions. The results suggest that these VEGF family members may also take active parts in angiogenesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
35172-8
pubmed:dateRevised
2009-11-25
pubmed:meshHeading
pubmed-meshheading:10575000-Amino Acid Sequence, pubmed-meshheading:10575000-Animals, pubmed-meshheading:10575000-Cattle, pubmed-meshheading:10575000-Cell Hypoxia, pubmed-meshheading:10575000-Cells, Cultured, pubmed-meshheading:10575000-Endothelial Growth Factors, pubmed-meshheading:10575000-Endothelium, Vascular, pubmed-meshheading:10575000-Gene Expression Regulation, Developmental, pubmed-meshheading:10575000-Humans, pubmed-meshheading:10575000-Molecular Sequence Data, pubmed-meshheading:10575000-Oligonucleotides, Antisense, pubmed-meshheading:10575000-Pericytes, pubmed-meshheading:10575000-Precipitin Tests, pubmed-meshheading:10575000-Pregnancy Proteins, pubmed-meshheading:10575000-Retina, pubmed-meshheading:10575000-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:10575000-Sequence Homology, Amino Acid, pubmed-meshheading:10575000-Vascular Endothelial Growth Factor A, pubmed-meshheading:10575000-Vascular Endothelial Growth Factor B, pubmed-meshheading:10575000-Vascular Endothelial Growth Factor C
pubmed:year
1999
pubmed:articleTitle
Placenta growth factor and vascular endothelial growth factor B and C expression in microvascular endothelial cells and pericytes. Implication in autocrine and paracrine regulation of angiogenesis.
pubmed:affiliation
Department of Biochemistry, Kanazawa University School of Medicine, Kanazawa 920-8640, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't