By J. S. Sussenbach, P. H. Steenbergh, E. Jansen, P. Holthuizen, D. Meinsma (auth.), Mohan K. Raizada, Derek LeRoith (eds.)
This quantity addresses a primary puzzle in biology and medication, particularly, how does tissue improve, fix and change itself. the reply appears to be like to lie in development components and their rules. To thrive and continue to exist we'd like development components and this booklet concentrates on components which are concerning progress hormone. progress hormone doesn't act at once on all tissues, yet mediates lots of its activities throughout the unencumber of insulin-like progress elements from the liver. the expansion components have been initially known as somatomedins by means of McConaghey and Sledge (1), who chanced on that they mediated growth-like results of progress hormone. notwithstanding, the standards have been purified at the foundation in their insulinomimetic activities on fats and muscle and it really is their courting to the insulin kin of pep tides that now offers them their identify (2,3) of insulin-like progress components (IGFs). They mediate the activities of. progress hormone at the proteoglycan synthesis of cartilage and bring mitogenic results in fibroblast cultures.
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Additional info for Molecular Biology and Physiology of Insulin and Insulin-Like Growth Factors
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D. d. d. d. d. d. d. d. d. d. d. d. d. = not determined ~ In contrast to these data, large changes in the A-, B- and D-regions of IGF I have minimal effects on binding to the type 1 IGF receptor. Replacement of residues 1-16 of IGF I with residues 1-17 of the B-chain of insulin (B-chain mutant) or of residues 42-56 with residues 1-15 of the A-chain of insulin (A-chain mutant) has a minimal effect on type 1 IGF receptor affinity but results in a loss in type 2 IGF receptor affinity (4,5). In addition, deletion of residues 63-70 (D-region) of IGF I has no effect on type 1 receptor binding but results in slightly increased affinity for insulin receptors (l).
1988) Endocrinology, 123, 373-381. S. L. (1989) J. Cell. , 139, 181-188. , Mills-Dunlop, B. H. (1987) J. Clin. Endocrinol. , 64, 501-507. L. H. (1990) J. Clin. , in press. H. R. (1987) Proc. Natl. Acad. Sci. USA, 84, 3254-3258. R. (1988) J. Biol. , 263, 14203-14210. L. (1989) Endocrinology, 125, 1910. , Bayne, M. A. (1990) Endocrinology, in press. INSULIN-LIKE GROWTH FACTOR II: COMPLEXITY OF BIOSYNTHESIS AND RECEPTOR BINDING Steen Gammeltoft, Jan Christiansen, Finn C. Nielsen, and Sten Verland Department of Clinical Chemistry, Bispebjerg Hospital DK 2400 Copenhagen NV, Denmark.
The diversity in IGF-II actions in different cell types during development and postnatal life may 39 be related to the existence of multiple signalling pathways like stimulation of protein tyrosine kinase activity and activation of G-protein-coupled enzymes. In conclusion, the spectrum of regulatory levels and the complex relationship between biosynthesis, receptor binding and signalling of IGF-II agrees well with the concept that IGF-II acts in an autocrine or paracrine manner and that IGF-II exerts diverse cellular actions under a variety of conditions.