Read e-book online Retinoids: The Biochemical and Molecular Basis of Vitamin A PDF

By N. Noy (auth.), Professor Dr.Dr.h.c. Heinz Nau, William S. Blaner Ph.D. (eds.)

In the longer term' the last decade of the Nineties will be considered as a Golden Age for retinoid study. there were exceptional examine earnings within the figuring out of retinoid activities and body structure; because the retinoid nuclear receptors have been first pointed out and the significance of retinoic acid in boost­ psychological approaches was once first extensively famous within the overdue Nineteen Eighties. among then and now, our wisdom of retinoid motion has developed from one among a close to whole lack of expertise of ways retinoids act inside cells to at least one of refined knowing of the molecular procedures during which retinoids modulate transcription. during this quantity, we now have attempted to supply a complete replace of the current knowing of retinoid activities, with an emphasis on re­ cent advances. The preliminary chapters of the amount, or part A, concentrate on the physicochemical homes and metabolism of clearly taking place retinoids: - N OY offers an uncommonly encountered view of retinoid results from the point of view of the physiochemical houses of retinoids. - V AKIANI and dollar lend a viewpoint at the organic incidence and activities of unfashionable- and anhydro-retinoids. part B considers either the retinoid nuclear receptors and their mechanisms of motion in addition to artificial retinoids which were used exper­ imentally to supply mechanistic insights into receptor activities and feature power healing use for treating disorder: - PIEDRAFITA and PFAHL offer a complete assessment of retinoid nuclear receptor biochemistry and molecular biology.

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Additional info for Retinoids: The Biochemical and Molecular Basis of Vitamin A and Retinoid Action

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1ml blood); v = k[TTR-RBPretinolhlood' b A diffusion-controlled reaction (CONNORS 1990). cValue of k from Noy and Xu (1990a). umol PM lipids (COOK 1958). An additional assumption is that retinol is equally distributed between the outer and in the inner leaflets of the PM. 5 nmollg tissue; v = k[retinol]pm/out. dValue of k from Noy et al. (1995). v = k[retinol]pm/in where [retinol]pm/in was calculated as detailed in footnote c, above. e Lower limit of k calculated from the upper limit of the Kd (Table 3) and the kOf!

1988). These considerations raise the question of whether the carboxyl group of RA is protonated or negatively charged at physiological pH, and whether the self-association characteristics of RA affect the compound's ionization state. These questions were examined in a study that utilized the large spectral shift of the absorption maximum of RA upon protonation of the carboxyl end group to monitor the ionization behavior of RA in water (Noy 1992a). The concentration dependence of the pK of RA indicated that the CMC of this retinoid is lower than 111M.

Biochemistry 34:11928-11937 Katakura Y, Totsuka M, Ametani A, Kaminogawa S (1994) Tryptophan-19 of betalactoglobulin, the only residue completely conserved in the lipocalin superfamily, is not essential for binding retinol, but relevant to stabilizing bound retinol and maintaining its structure. Biochim Biophys Acta 1207:58-67 Kersten S, Pan L, Chambon P, Gronemeyer H, Noy N (1995a) Role of ligand in retinoid signaling: 9-cis-retinoic acid modulates the oligomeric state of the retinoid X receptor.

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