Insulin-like growth factor-binding proteins from vascular endothelial cells: purification, characterization, and intrinsic biological activities.

Endocrinology
R S BarB L Dake

Abstract

Insulin-like growth factor (IGF)-binding proteins are produced by several cell types, including vascular endothelial cells. The production of IGF-binding proteins by endothelial cells is of particular interest, since these cells are directly bathed by the circulating IGFs and form the initial barrier to the passage of circulating IGFs from the bloodstream to subendothelial tissues. We have purified IGF-binding proteins from medium conditioned by cultured bovine endothelial cells by sequential passage over Bio-Gel P-60, multiplication-stimulating activity affinity, anion exchange (DEAE cellulose) and/or hydrophobic (phenyl-Sepharose) chromatography. Two peaks of IGF-binding activity were eluted from the phenyl-Sepharose column. After cross-linking, each peak contained two to five protein bands on gels that specifically bound IGF-I and -II with mol wt ranging from about 28-44K. Material in peak 1 bound IGF-I congruent to IGF-II and had no affinity for insulin and proinsulin. Peak 2 IGF-binding proteins bound IGF-II with substantially higher affinity than IGF-I and did not recognize insulin or proinsulin. Peak 1 material from phenyl-Sepharose chromatography was a potent stimulator of both glucose transport and aminoisobutyric acid...Continue Reading

Citations

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