Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1986-6-11
pubmed:abstractText
The scarcity of purified materials has prevented studies of the mechanism of insulin-like growth factor I (IGF-I) action. Recently, an IGF-I analog, Thr59-IGF-I, was synthesized by recombinant DNA technology. We found that this analog had binding characteristics similar to those of natural IGF-I in the radioreceptor assay system. We used this analog to characterize human erythrocyte IGF-I receptors as follows. Erythrocytes from 33 normal subjects specifically bound 6.9 +/- 0.7% (mean +/- SD)/2.8 X 10(9) cells/ml. Scatchard analysis of the binding data showed that the total number of receptors per erythrocyte was 13, and the affinity constant was 1.26 X 10(9) M-1, similar to that of other human IGF-I receptors previously reported. We also examined IGF-I receptors in patients with insulin receptor abnormalities. Although the specific values of IGF-I binding to erythrocytes were decreased or increased in parallel with those of insulin, the degrees of decrease or increase were much smaller. This suggests that the expression of insulin receptors and that of IGF-I receptors are discordant.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-972X
pubmed:author
pubmed:issnType
Print
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1206-12
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Characteristics of human erythrocyte insulin-like growth factor I receptors.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't