Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1993-6-8
pubmed:abstractText
Epithelin 1 and 2 are cysteine-rich proteins that act as growth modulators of epithelial cells. In this report, we have characterized the epithelins receptors of MDA-MB-468 human breast carcinoma cells using both binding and cross-linking techniques. Equilibrium binding studies of iodinated epithelin 1 indicated that two classes of binding sites are expressed at the surface of breast carcinoma cells. The high affinity sites had a dissociation constant of approximately 2 x 10(-10) M, with approximately 290 receptors/cell. The low affinity sites had a dissociation constant of approximately 10(-8) M, with approximately 32,000 receptors/cell. Binding of iodinated epithelin 1 was specifically inhibited by unlabeled epithelin 1, 2, or 3, but not by other growth factors tested. We also performed competition binding studies of 125I-epithelin 1 to cell surface receptors in the presence of unlabeled epithelin 1, 2, or 3. Binding results analyzed by the method of Scatchard suggested that all three epithelins interact with a same receptor. A 140-145-kDa epithelin 1-binding protein complex was identified by chemical cross-linking of 125I-epithelin 1 to breast cancer cells. Formation of such a complex was prevented by coincubation of 125I-epithelin 1 with an excess of unlabeled epithelin 1, 2, or 3.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10458-62
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Biochemical analysis of the epithelin receptor.
pubmed:affiliation
Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, Washington 98121.
pubmed:publicationType
Journal Article