Characterization of insulin-like growth factor-binding proteins from sheep thyroid cells.

Endocrinology
L K BachrachM C Eggo

Abstract

The insulin-like growth factors (IGFs) are bound by specific, high affinity binding proteins. Distinct classes of IGF-binding proteins have been described in human serum, amniotic fluid, cerebrospinal fluid, and conditioned medium from cultured cells. Sheep thyroid cells produce IGF-binding proteins under hormonal regulation. Cells grown without or with standard medium supplements (transferrin, glycyl-histidyl-lysine, hydrocortisone, somatostatin, insulin, and TSH) released binding proteins with apparent mol wt of 23, 29, and 32 kDa on Western ligand blot (nonreduced). Binding proteins from these cells appeared as 21, 26, 34, 36, and 41 kDa bands when cross-linked to [125I]IGF-I under reducing conditions. The addition of epidermal growth factor (EGF) or phorbol esters, thyroid cell mitogens stimulated the production of larger binding proteins with mol wt of 40-44 and 48-52 by ligand blot and cross-linking methods, respectively. Deglycosylation of conditioned medium cross-linked to [125I]IGF-I with endoglycosidase-F did not alter the size of the smaller binding proteins, but reduced EGF-stimulated binding proteins to 36-40 kDa. Similarly, tunicamycin treatment, which inhibits glycosylation, reduced only the size of this larger b...Continue Reading

Citations

Nov 1, 1993·Molecular and Cellular Endocrinology·V IlvesmäkiR Voutilainen
Jan 28, 1999·American Journal of Respiratory Cell and Molecular Biology·R RajahP Cohen
Dec 1, 1995·In Vitro Cellular & Developmental Biology. Animal·J D LinH F Weng
Aug 29, 2012·Journal of Oncology·Roberta MalaguarneraAntonino Belfiore
Jan 1, 1994·Japanese Journal of Cancer Research : Gann·T YashiroT Tsushima

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