Download Collagen: Primer in Structure, Processing and Assembly by Jürgen Brinckmann (auth.), Jürgen Brinckmann, Holger PDF

By Jürgen Brinckmann (auth.), Jürgen Brinckmann, Holger Notbohm, P. K. Müller (eds.)

J. Brinckmann: Collagens at a Glance.-

J. Engel, H.P. Bächinger: constitution, balance and Folding of the Collagen Triple Helix.-

S. Ricard-Blum, F. Ruggiero, M. van der leisure: The Collagen Superfamily.-

T. Koide, ok. Nagata: Collagen Biosynthesis.-

J. Myllyharju: Intracellular Post-Translational transformations of Collagens.-

D.S. Greenspan: Biosynthetic Processing of Collagen Molecules.-

D.E. Birk, P. Bruckner: Collagen Suprastructures.-

D.R. Eyre, J.-J. Wu: Collagen Cross-Links

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Additional resources for Collagen: Primer in Structure, Processing and Assembly

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Corneal Endothelial Dystrophies . . . . . . . . Schmid Metaphyseal Chondrodysplasia . . . . . . 5 Collagens and Neurodegenerative Diseases 6 References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . Abstract The collagen family is highly complex and shows a remarkable diversity in molecular and supramolecular organization, tissue distribution and function. Collagen types are classified in several sub-families according to sequence homologies and to similarities in their structural organization and supramolecular assembly.

Null mice showed perinatal lethality and the analysis of their phenotype revealed that collagen XIX is required for esophageal muscle transdifferentiation [58]. This finding is in good concordance with the previously established expression pattern of collagen XIX in developing embryos. Notably, collagen XIX expression was confined to few sites including the smooth muscle layers of the stomach and esophagus [56]. 3 Collagens XX, XXI and XXII Chick collagen XX is very closely related to collagen XIV and found to be localized to corneal epithelium, a pattern very close to that of collagen XII [59].

No covalent cross-linking involving these collagen types could be demonstrated and the current point of view is that collagens XII and XIV might interact with fibrils through the matrix small proteoglycans decorin and fibromodulin [37–39]. Functions of collagens XII and XIV have not been fully elucidated but a line of 54 S. Ricard-Blum et al. evidence puts forward a role in stabilizing and/or in organizing fibrillar network in extracellular matrix. Collagen XIV was reported to promote gel contraction [40] and might act as a regulating factor of fibril growth in developing tendon [41].

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