Collagen fibril-forming

The 19 types of collagen mentioned above can be subdivided into a niimbet of classes based primarily on the sttucmtes they fotm (Table 48-2). In this chaptet, we shall be primarily concerned with the fibril-forming collagens I and II, the majot collagens of skin and bone and of cattilage, tespectively. However, mention will be made of some of the othet collagens. 

Kadler, K. (1994). Extracellular matrix fibril forming collagen. Protein Profile 1, 519-638. 

Collagen fibrils contain a number of collagen gene products. These can be conveniently divided into two classes (a) fibril-forming collagens and (b) fibril-associated collagens with interrupted triple helices (FACIT... 

The distribution of minor collagen types as surface molecules is more obvious for some types than others. Fibril-forming collagens—especially... 

Since fibril assembly can be regarded in part as a spontaneous self-assembly process, the limitation of fibril size could be ascribed to a physical equilibrium between soluble procollagen molecules and the growing insoluble fibril. Fibril-forming collagens are synthesized as precursor... 

Dreisewerd, K., Rohlfing, A., Spottke, B., Urbanke, C., and Henkel, W. (2004). Characterization of whole fibril-forming collagen proteins of types I, III, and V from foetal calf skin by infrared matrix-assisted laser desorption ionization mass spectrometry. Anal. Chem. 76, 3482-3491. 

Kadler, K. Extracellular matrix I. Fibril-forming collagens. Protein Profile 1 519-638, 1994. 

At least nine of the collagens - types I, HI, IV, V, VI, VIII, XII, XIII, and XIV - have been found in the vessel walP. The ratio of the various collagen molecules in a normal and in an arteriosclerotic vessel wall is different . The fibril-forming collagens type I,... 

All the fibril-forming collagen t) es (t) e I, II, III, V, XI, XXIV, and XXVII collagens) are cross-linked through a mechanism based on the reactions of aldehydes derived from some lysine (or hydroxylysine) side chains. Histidine might also participate in the formation of a trivalent cross-link by reacting with an aldimine bond formed between a lysine aldehyde and hydroxylysine residue. 

The collagen present in the avian comeal stroma is a striated collagen, but with a smaller and more uniform diameter (25 /im) than most fibril-forming collagens, and this is thought to be necessary for comeal transparency. Linsenmayer et al. (1993) proposed that this is achieved by a coassembly of... 

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