Download e-book for kindle: Ciba Foundation Symposium 145 - Carbohydrate Recognition in by CIBA Foundation Symposium

By CIBA Foundation Symposium

ISBN-10: 0470513829

ISBN-13: 9780470513828

ISBN-10: 0471923079

ISBN-13: 9780471923077

Participants to this quantity discover the function of carbohydrates in communique among cells of multicellular organisms. issues coated contain the thermodynamics and spatial regulations of oligosaccharide-protein interactions, the position of carbohydrates in popularity and as parts of mobilephone adhesion molecules, and irregular glycosylation in different sickness states.

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Presumably the chicken and the frog perform their physiological functions quite well without the binding of IGF-I1 to that receptor. We know chickens have IGF-I1 in their serum and their IGF-I1 is structurally similar to that of the human and the rat. Why was it important for such a high affinity IGF-11-binding site to evolve on this receptor so late in evolution? While we don’t know the answer as yet, the chicken data give us a way of approaching the structural question by looking at chimeric constructs.

The activation of S6 kinase or kinases occurs within minutes at nanomolar concentrations of insulin, paralleling the time course and dose response for insulin-stimulated S6 phosphorylation in vivo. Another novel insulin-stimulated Mn2+ -dependent serine kinase of estimated M , 50000-60000 from rat adipocytes has been characterized (Yu et a1 1987b). This cytosolic kinase activity was stimulated two-fold in insulin-treated cells using Kemptide (Leu-Arg-Arg-Ala-Ser-Leu-Gly) as substrate. A 4-fold stimulation of adipocyte Mn2 -dependent cytosolic kinase by insulin was observed after + Czech et a1 38 DEAE-Sephacel and molecular sieve chromatography.

This kinase activity is characterized by its preferential phosphorylation of histone V-S on serine and, to a lesser extent, threonine. In contrast to the insulin receptor, the HDM kinase activity does not adsorb to wheat germ agglutinin-agarose, indicating that it may not be substantially glycosylated (Yu et a1 1987a). Insulin and other growth factors markedly increase the phosphorylation of ribosomal protein S6 in 32P-labelled cells. The activities of at least two kinases, protease-activated kinase I1 (Traugh & Pendergast 1986) and S6 kinase (Tabarini et a1 1987, Erikson & Maller 1986, Ballou et a1 1988), are stimulated in extracts of insulin-treated cells.

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Ciba Foundation Symposium 145 - Carbohydrate Recognition in Cellular Function by CIBA Foundation Symposium


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