Ciba Foundation Symposium 114 - Fibrosis

Chapter 1 creation (pages 1–3): Allen J. Bailey
Chapter 2 The Fibroblast in Morphogenesis and Fibrosis: cellphone Topography and Surface?Related capabilities (pages 4–19): Robert L. Trelstad and David E. Birk
Chapter three Structural and practical experiences at the Interstitial Collagen Genes (pages 20–33): Benoit De Crombrugghe, Gene Liau, Chiaki Setoyama, Azriel Schmidt, Catherine McKeon and Maria Mudryj
Chapter four Synthesis of Collagen: Chemical rules of Post?Translational occasions (pages 34–64): Kari I. Kivirikko and Kari Majamaa
Chapter five The constitution of Collagen (pages 65–79): A. Miller, J. Bradshaw, E. Y. Jones, R. D. B. Fraser, T. P. Macrae and E. Suzuki
Chapter 6 Intermolecular Cross?Linking in Fibrotic Collagen (pages 80–96): A. J. Bailey and N. D. Light
Chapter 7 The Turnover and Degradation of Collagen (pages 97–110): Stephen M. Krane
Chapter eight Fibronectin in Formation and Degradation of the Pericellular Matrix (pages 111–126): Antti Vaheri, Eeva?Marjatta Salonen and Tapio Vartio
Chapter nine telephone Interactions in Post?Traumatic Fibrosis (pages 127–149): T. ok. Hunt, M. J. Banda and that i. A. Silver
Chapter 10 Chemoattractants in Fibrotic issues (pages 150–163): G. R. Grotendorst, L. Paglia, C. Mcivor, S. Barsky, Y. Martinet and D. Pencev
Chapter eleven HLA institutions in Fibrotic illness (pages 164–174): okay. I. Welsh
Chapter 12 Host Immune components Regulating Fibrosis (pages 175–195): Sharon M. Wahl
Chapter thirteen Collagen Deposition in Autoimmune illnesses: The increasing position of the Fibroblast in Human Fibrotic sickness (pages 196–207): E. Carwile Leroy
Chapter 14 rules of Fibroblast Proliferation by means of Kupffer Cells and Monocytes (pages 208–221): Marcos Rojkind and Gerardo Valadez
Chapter 15 Biochemical Pathways resulting in Collagen Deposition in Pulmonary Fibrosis (pages 222–240): Geoffrey J. Laurent
Chapter sixteen precis (pages 241–244): Allen J. Bailey

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One systematic difference is that the Ki values of all the aliphatic and aromatic 2-oxoglutarate analogues are distinctly higher in the case of lysyl hydroxylase than for prolyl4-hydroxylase and prolyl3-hydroxylase (K. Majamaa et al, unpublished work 1985). Another distinct difference is that the most effective inhibitor of lysyl hydroxylase and prolyl3-hydroxylase is pyridine 2,4-dicarboxylate, whereas the most potent inhibitor of prolyl 4-hydroxylase is pyridine 2,5dicarboxylate (Table 2). These data suggest the existence of significant differences between the three hydroxylases in the catalytic sites.

Biochim Biophys Acta 609321-328 Anttinen H , Ryhanen L. Puistola U . Arranto A . Oikarinen A 1984 Decrease in liver collagen CHEMICAL REGULATION O F COLLAGEN PROCESSING 47 accumulation in carbon tetrachloride-injured and normal growing rats upon administration of zinc. Gastroenterology 86532-539 Chvapil M 1982 Experimental modifications of collagen synthesis and degradation and their therapeutic applications. In: Weiss JB, Jayson MIV (eds) Collagen in health and disease. Churchill Livingstone, Edinburgh, p 206-217 De Jong L, Kemp A 1984 Stoichiometry and kinetics of the prolyl4-hydroxylase partial reaction.

2). 3,4-Dihydroxybenzoate also possesses the structural domains essential for binding at subsites 1-111 of the 2-oxoglutarate site (Fig. 3) and is an effective prolyl 4-hydroxylase inhibitor, with a Ki of about 5 p M (K. Majamaa et al, unpublished work 1985). Data on many related compounds again demonstrate the importance of an optimal interaction at all three subsites for effective binding (Fig. 3). The aliphatic compounds known at present to compete with 2-oxoglutarate have significantly higher K , values than those recorded for the most potent aromatic inhibitors.

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