rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
28
|
pubmed:dateCreated |
1994-8-17
|
pubmed:databankReference |
|
pubmed:abstractText |
Endothelin (ET) is a 21-residue potent vasoconstrictive peptide produced by vascular endothelial cells and formed from its precursor, big endothelin (big ET), by endothelin-converting enzyme (ECE). Here we report the cloning and functional expression of a complementary DNA encoding a rat ECE from endothelial cells. Rat ECE is a highly glycosylated protein consisting of 10 possible N-linked glycosylation sites, a zinc-binding domain, and a single membrane-spanning region. It has structural and sequence homology to neutral endopeptidase and Kell blood group protein, a putative neutral endopeptidase. Monoclonal antibody risen against purified rat lung ECE recognized broad glycosylated bands in membrane fractions prepared from both rat lung and COS cells transfected with a rat ECE expression vector. Expressed ECE was inhibited by phosphoramidon, but not by thiorphan. It also cleaved big ET-1 efficiently but not big ET-2 or big ET-3. Northern blot analysis revealed that ECE messenger RNA is widely expressed in many tissues.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
269
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
18275-8
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:8034569-Amino Acid Sequence,
pubmed-meshheading:8034569-Animals,
pubmed-meshheading:8034569-Aspartic Acid Endopeptidases,
pubmed-meshheading:8034569-Base Sequence,
pubmed-meshheading:8034569-Blotting, Northern,
pubmed-meshheading:8034569-Cell Line,
pubmed-meshheading:8034569-Cercopithecus aethiops,
pubmed-meshheading:8034569-Cloning, Molecular,
pubmed-meshheading:8034569-Consensus Sequence,
pubmed-meshheading:8034569-DNA, Complementary,
pubmed-meshheading:8034569-DNA Primers,
pubmed-meshheading:8034569-Endothelium, Vascular,
pubmed-meshheading:8034569-Gene Expression,
pubmed-meshheading:8034569-Humans,
pubmed-meshheading:8034569-Kinetics,
pubmed-meshheading:8034569-Lung,
pubmed-meshheading:8034569-Metalloendopeptidases,
pubmed-meshheading:8034569-Molecular Sequence Data,
pubmed-meshheading:8034569-Polymerase Chain Reaction,
pubmed-meshheading:8034569-RNA, Messenger,
pubmed-meshheading:8034569-Rats,
pubmed-meshheading:8034569-Sequence Homology, Amino Acid,
pubmed-meshheading:8034569-Transfection
|
pubmed:year |
1994
|
pubmed:articleTitle |
Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells.
|
pubmed:affiliation |
Biological Research Laboratories, Sankyo Co., Ltd., Tokyo, Japan.
|
pubmed:publicationType |
Journal Article,
Comparative Study
|