scholarly journals A Polymorphism in Type I Deiodinase Is Associated with Circulating Free Insulin-Like Growth Factor I Levels and Body Composition in Humans

2005 ◽  
Vol 90 (1) ◽  
pp. 256-263 ◽  
Author(s):  
Robin P. Peeters ◽  
Annewieke W. van den Beld ◽  
Hans van Toor ◽  
Andre G. Uitterlinden ◽  
Joop A. M. J. L. Janssen ◽  
...  
Keyword(s):  
Body Composition ◽  
Growth Factor ◽  
Type I ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Free Insulin ◽  
Growth Factor I

Insulin-Like Growth Factor-I in Human Malnutrition: Relationship with Some Body Composition and Nutritional Parameters

1989 ◽  
Vol 13 (4) ◽  
pp. 392-396 ◽  
Author(s):  
Francesco Minuto ◽  
Antonina Barreca ◽  
Gian Franco Adami ◽  
Patricia Fortini ◽  
Patrizia Del Monte ◽  
...  
Keyword(s):  
Body Composition ◽  
Growth Factor ◽  
Insulin Like Growth Factor ◽  
Nutritional Parameters ◽  
Factor I ◽  
Growth Factor I

Free Insulin-Like Growth Factor I (IGF-I) and IGF-II in Human Saliva*

1988 ◽  
Vol 66 (5) ◽  
pp. 1014-1018 ◽  
Author(s):  
D. COLM COSTIGAN ◽  
HARVEY J. GUYDA ◽  
BARRY I. POSNER
Keyword(s):  
Growth Factor ◽  
Human Saliva ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Free Insulin ◽  
Igf I ◽  
Growth Factor I

Role of free insulin-like growth factor-I in hyperglycemia in patients with type 1 diabetes mellitus

2000 ◽  
Vol 50 ◽  
pp. 417
Author(s):  
Kisho Kobayashi ◽  
Shin Amemiya ◽  
Koji Kobayashi ◽  
Mie Mochizuki ◽  
Tomoaki Sano ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Type 1 Diabetes ◽  
Growth Factor ◽  
Type 1 Diabetes Mellitus ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Free Insulin ◽  
Growth Factor I

scholarly journals Purified hybrid insulin/insulin-like growth factor-I receptors bind insulin-like growth factor-I, but not insulin, with high affinity

1993 ◽  
Vol 290 (2) ◽  
pp. 419-426 ◽  
Author(s):  
M A Soos ◽  
C E Field ◽  
K Siddle
Keyword(s):  
Monoclonal Antibody ◽  
Growth Factor ◽  
Insulin Receptors ◽  
Beta Subunit ◽  
Type I ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Igf Receptors ◽  
Igf I ◽  
Growth Factor I

Hybrid insulin/insulin-like growth factor-I (IGF-I) receptors have previously been described in human placenta, but it has not been possible to study their properties in the presence of classical insulin receptors and type I IGF receptors. To facilitate the purification of hybrids, we produced an anti-peptide monoclonal antibody IGFR 1-2, directed against the C-terminal peptide of the type I IGF receptor beta-subunit. The antibody bound native human and rat type I IGF receptors, and reacted specifically with the beta-subunit on immunoblots. Solubilized placental microsomal membranes were depleted of classical type I IGF receptors by incubation with an immobilized monoclonal antibody IGFR 24-55, which reacts well with type I receptors but very poorly with hybrid receptors. Residual hybrid receptors were then isolated by incubation with immobilized antibody IGFR 1-2, and recovered by elution with excess of synthetic peptide antigen. Binding properties of hybrids were compared with those of immuno-affinity-purified insulin receptors and type I IGF receptors, by using the radioligands 125I-IGF-I and 125I-insulin. Hybrids bound approx. 20 times as much 125I-IGF-I as 125I-insulin at tracer concentrations (approx. 0.1 nM). The binding of 125I-insulin, but not 125I-IGF-I, to hybrids increased after treatment with dithiothreitol to reduce disulphide bonds between the alpha-subunits. Hybrids behaved very similarly to type I receptors with respect to the inhibition of 125I-IGF-I binding by unlabelled IGF-I and insulin. By contrast, the affinity of hybrids for insulin was approx. 10-fold lower than that of classical insulin receptors, as assessed by inhibition of 125I-insulin binding by unlabelled hormone. It is concluded that the properties of insulin receptors, but not IGF receptors, are markedly affected by assembly as hybrid compared with classical structures, and that hybrids are more likely to be responsive to IGF-I than insulin under physiological conditions.

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