Linked Life Data

10706866

Source:http://linkedlifedata.com/resource/pubmed/id/10706866

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2000-4-7
pubmed:abstractText
Angiopoietin-1 (Ang-1) is required for developing vessels, and its absence leads to defects in vessel remodeling. Ang-1 has been identified as the ligand for the tyrosine kinase receptor Tie-2, which is expressed specifically on endothelial cells and early hematopoietic cells. In studying the role of Tie-2 and Ang-1 in megakaryocytopoiesis, 3 alternatively spliced species of Ang-1 mRNA (Ang-1.3 kb, Ang-0.9 kb, and Ang-0.7 kb) were identified in addition to the full-length Ang-1 (Ang-1.5 kb), in the megakaryocyte cell line CHRF by reverse transcription-polymerase chain reaction (RT-PCR), and then cloned and sequenced. The expression of 3 alternatively spliced isoforms of Ang-1 was confirmed by RT-PCR using specific primer pairs derived from junction sites and the 3' end of Ang-1 cDNA, and it was further demonstrated by nuclease protection assay, Northern blotting, and immunoblotting in CHRF cells. Expression of the Ang-1.3 kb isoform was also detected in human primary fibroblast cell line FS4, breast cancer cell line MDAMB-468, and CD34(+)CD41(+) cells of fetal liver and platelets. The function of the 1.5-kb, 1.3-kb, and 0.9-kb isoforms was examined. Recombinant proteins Ang-1.5 and 0.9 kb bind strongly to the recombinant Tie-2 receptor (Tie-2-Fc), whereas the 1.3-kb isoform does not. The Ang-1.3 kb isoform binds to the 1.5-kb isoform. Ang-1. 5 kb, but not the 1.3-kb and 0.9-kb isoforms, induces tyrosine phosphorylation of Tie-2 in human umbilical vein endothelial cells. These data suggest that isoforms 1.3 kb and 0.9 kb could serve as dominant negative molecules for the full-length Ang-1. The possible involvement of the newly identified Ang-1 isoforms in angiogenesis and in growth and differentiation of hematopoietic progenitor cells provides a greater complexity to these processes. (Blood. 2000;95:1993-1999)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1993-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10706866-Alternative Splicing, pubmed-meshheading:10706866-Angiopoietin-1, pubmed-meshheading:10706866-Base Sequence, pubmed-meshheading:10706866-Cell Line, pubmed-meshheading:10706866-Cloning, Molecular, pubmed-meshheading:10706866-Fibroblasts, pubmed-meshheading:10706866-Humans, pubmed-meshheading:10706866-Ligands, pubmed-meshheading:10706866-Megakaryocytes, pubmed-meshheading:10706866-Membrane Glycoproteins, pubmed-meshheading:10706866-Molecular Sequence Data, pubmed-meshheading:10706866-Multigene Family, pubmed-meshheading:10706866-Phosphorylation, pubmed-meshheading:10706866-Protein Binding, pubmed-meshheading:10706866-Protein Isoforms, pubmed-meshheading:10706866-Protein Structure, Tertiary, pubmed-meshheading:10706866-RNA, Messenger, pubmed-meshheading:10706866-Recombinant Fusion Proteins, pubmed-meshheading:10706866-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:10706866-Sequence Homology, Nucleic Acid, pubmed-meshheading:10706866-Tumor Cells, Cultured, pubmed-meshheading:10706866-Tyrosine
pubmed:year
2000
pubmed:articleTitle
Identification of a family of alternatively spliced mRNA species of angiopoietin-1.
pubmed:affiliation
New York University School of Medicine and Kaplan Cancer Center, New York, NY 10016, USA. huangy02@mcrcr6.med.nyu.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't