Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1980-9-28
pubmed:abstractText
The binding of insulin to cultured human lymphocytes of the IM-9 line was investigated at near-physiological conditions, i.e. 37 degrees C, pH 7.4, using a monoiodinated insulin exclusively labeled in tyrosyl residue 14 of the A chain. Although the apparent dissociation constant did not differ much from that found in rat adipocytes, the rate constants were about 1 order of magnitude greater. The rate of dissociation of 60 pM of labeled insulin was accelerated more in the lymphocytes than in adipocytes by the addition of 50 nM insulin to the wash-out medium. In rat adipocytes insulin is degraded both by receptor-independent and receptor-mediated processes (Gliemann, J., and Sonne, O. (1978) J. Biol. Chem. 253, 7857-7863). Lymphocytes possessed a receptor-independent insulin-degrading system with the same properties as that of adipocytes. However, receptor-mediated degradation was absent and insulin binding is therefore a true reversible process. The following is concluded: 1) The binding sites of the receptors in IM-9 lymphocytes are different from those of the insulin-responsive adipocytes and hepatocytes. 2) The lymphocytes lack the enzyme responsible for the receptor-mediated degradation or a coupling factor between the receptor and the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
255
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7449-54
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Insulin receptors of cultured human lymphocytes (IM-9). Lack of receptor-mediated degradation.
pubmed:publicationType
Journal Article