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Download Current Directions in Insulin-Like Growth Factor Research by Martin L. Adamo, Stefan Neuenschwander (auth.), Derek Le PDF

By Martin L. Adamo, Stefan Neuenschwander (auth.), Derek Le Roith M.D., Ph.D., Mohan K. Raizada Ph.D. (eds.)

The learn of the insulin-like development issue (IGF) kin has turn into a thrilling quarter of research. at first, this kin consisted of ligands (insulin, IGF-I and IGF-m and receptors (the insulin receptor, the kind I or IGF-I receptor and the kind II or IGF-IYM-6-P receptor). in this case, it used to be stumbled on that six particular binding proteips (lGFBPs 1-6) playa significant function within the activities of this development issue family members. additionally, there are actually extra strength receptors while one considers the potential roles of the insulin-receptor comparable receptor (IRR) and hybrid receptor dimers composed of insulin and IGF-I receptor (half-receptors). one other vital point of this region of study is the conclusion that the IGFs will not be basically crucial for regular development and improvement yet, moreover play an enormous function within the common really good function(s) of all tissues of the physique, together with the worried process, skeleton, reproductive approach, kidney, and the immune method, to call yet a couple of. the improvement of recombi!tant human IGF-I for scientific trying out has been an important leap forward for investigators. power makes use of comprise wound therapeutic, reversal of catabolic states, diabetes, bone home improvement, restoration from acute renal failure and so on. will ensure either its use and its power hazards.

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Shoelson, Heteronuclear 2D NMR studies of an engineered insulin monomer: Assignment and characterization of the receptor-binding surface by selective 2H and 13C labeling with application to protein design, Biochemistry 30:7373 (1991). 16. D. C. Howey, S. A. Hooper and R. R. Bowsher, [Lys(B28), Pro(B29)]-Human insulin: An equipotent analtlg of insulin with rapid onset and short duration of at:tion, Diabetes 4O(Supp 1): 423A (1991). 17. L. J. Slieker and K. L. Sundell, Modifications in the 28-29 position of the insulin B-chain alter binding to the IGF-I receptor with minimal effect on insulin receptor binding, Diabetes 4O(Supp 1): 168A (1991).

1992, Functional analysis of rat insulin-like growth factor-I gene and identification of an IGF-I gene promoter, DNA and Cell Bioi. 11:301. J. , 1990, Different half lives of insulin-like growth factor-I mRNAs that differ in length of 3' -untranslated regions, Endocrinology 127:1550. , Postel-Vinay, M-C. , 1991, The prolactin/growth honnonereceptor family, Endocrine Rev. 12:235. L. T. , 1987, Differential expression of alternative 5' untranslated regions in mRNAs encoding rat insulin-like growth factor I, Proc.

Mfinities of each analog are relative to insulin or IOF-I =100% (± SEM, n in parentheses). 01 (2) IGFBP 100 151 ± 15 (3) 226±66 (4) 154± 37 (4) 69± 17(3) two-chain molecule by clipping between residues 41-42 (BC:A) had no effect on IGF receptor affinity, but clipping on the other side of the C domain at residues 29-30 dramatically reduced affinity, suggesting that the absolute presence of the C domain is insufficient if the conformation is not restricted. Interestingly, removal or derestriction of the C domain appears to enhance affinity for the serum IGFBPs.

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