Àá½Ã¸¸ ±â´Ù·Á ÁÖ¼¼¿ä. ·ÎµùÁßÀÔ´Ï´Ù.
KMID : 1134819970260020285
Journal of the Korean Society of Food Science and Nutrition
1997 Volume.26 No. 2 p.285 ~ p.290
Distribution of Insulin - Like Growth Factor - Binding Proteins(IGFBPs) and IGFBP - 3 Proteolysis in Noninsulin - Dependent Diabetes Mellitus Serum
Lee Hwa-Jin

Kim Sung-Hyun
Kwon Mi-Jin
Nam Tak-Jeong
Abstract
The insulin-like growth factors(IGFs) are bound to several binding proteins(IGFBPs) that appear to regulate IGF transport, receptor binding, and its action. The concentration of these peptides are altered by catabolic conditions. To determine IGF-I and IGFBP levels in noninsulin-dependent diabetes mellitus (NIDDM), sera was obtained from 5 patients and 7 controls. Serum levels of IGF-I in NIDDM were lower than those in either of the controls. By western immunoblot analysis, especially IGFBP-1 levels are increased, whereas IGFBP-3 levels decreased and their fragments was increased in NIDDM serum. IGFBP-3 proteolytic activity in NIDDM sera was inhibited by phenylmethylsulfonylfluoride (PMSF), aprotinin, and ethylenediaminetetraacetic acid(EDTA). This pattern of inhibition was consistent with a metal-dependent serine protease. By gelatin zymography, these proteolytic enzymes were identified as the size of 97 and 69 kDa. IGFBP-1, which is primarily insulin regulated, was increased in NIDDM and may modulate circulating IGF-I levels by regulating capillary passage of IGF-I. IGFBP-3 proteolysis markedly reduces its affinity for the IGFs, particularly for IGF-I. This accelerates their kinetics of dissociation, thereby increasing the proportions of IGF-I in free form and its availability to the cells.
KEYWORD
noninsulin-dependent diabetes mellitus, insulin-like growth factor binding proteins, IGFBP-3 proteolysis, protease inhibitor
FullTexts / Linksout information
Listed journal information
ÇмúÁøÈïÀç´Ü(KCI)