cDNA cloning of human plasminogen activator-inhibitor from endothelial cells.
AUTOR(ES)
Ginsburg, D
RESUMO
Full-length cDNA for plasminogen activator inhibitor (PAI-1) was isolated from a human umbilical vein endothelial cell (HUVEC) lambda gt11 cDNA library. Three overlapping clones were identified by immunologic screening of 10(6) recombinant phage using a rabbit anti-human fibrosarcoma PAI-1 antiserum. The fusion proteins encoded by these three clones also react strongly with a monoclonal mouse anti-human fibrosarcoma PAI-1 antibody. By nucleotide sequence analysis, PAI-1 cDNA encodes a protein containing 402 amino acids with a predicted, nonglycosylated molecular mass of 45 kD. Identity of this material as authentic PAI-1 was confirmed by the presence of high level homology with the primary amino acid sequence of an internal peptide prepared from purified rat hepatoma PAI-1. The predicted amino acid sequence also reveals extensive homology with other members of the serine protease inhibitor gene family. Cultured HUVECs contain two PAI-1 mRNA species, both encoded by a single gene, differing by 1 kb in the 3' untranslated region. The PAI-1 gene is located on human chromosome 7.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=423941Documentos Relacionados
- Thrombin induction of plasminogen activator-inhibitor in cultured human endothelial cells.
- Tissue plasminogen activator, plasminogen activator inhibitors, and activator-inhibitor complex in liver disease.
- Variant tissue-type plasminogen activator (PLAT) cDNA obtained from human endothelial cells
- Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor.
- Nucleotide sequence of the tissue-type plasminogen activator cDNA from human fetal lung cells.