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,
JUDITH M. PODSKALNY,
ALAN C. MOSES
and
LINDA FRYKLUND
Diabetes Branch, National Institute of Arthritis, Metabolism, and Digestive Diseases, National Institutes of Health, Bethesda Maryland 20014
Metabolism Branch, National Cancer Institute, National Institutes of Health, Bethesda Maryland 20014
AB KABI, The Becip Polypeptide Laboratory, Stockholm Sweden
We have demonstrated a specific receptor for somatomedin-like growth polypeptides in human fibroblasts in culture using the closely related polypeptide, multiplication stimulating activity (MSA), as the radioligand. Polypeptides purified from human plasma, somatomedin A and acid soluble nonsuppressible insulin-like activity (NSILA-s), competed potently for 125I-MSA binding, as did unlabeled MSA. Although insulin and proinsulin also strongly inhibited MSA binding, the propertiesof the growth peptide receptor differed from those of the human fibroblast insulin receptor. Somatomedin A, NSILA-s, MSA, insulin and proinsulin all stimulated the incorporation of [3H]thymidine into DNA in human fibroblasts. We propose that these polypeptides induce DNA synthesis through their interaction with the growth peptide receptor.
* preliminary account of these results has been presented at the Thirty-third Annual Meeting of the American Federation for Clinical Research, Atlantic- City, New Jersey, May 1, 1976
Received November 17, 1975.
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