Abstract
Type IV collagen is a heterotrimer composed of 3 a chains; these molecules form tetramers by overlap at the amino terminus (7S domain) which further aggregate by end-to-end interaction involving the non-collagenous carboxyl termini (NC1 domains). Collagen is a major component of basement membranes. There are six a chains of type IV collagen whose genes have been cloned. The most predominent heterotrimer is composed of two a-1 and one a-2 chains. It can be prepared by extraction of a mouse sarcoma (EHS tumor) (Wisdom, Gunwar, Hudson, Noelken and Hudson, 1992). Molecular forms of the other type IV collagen chains, a3(IV), a4(IV), a5(IV), a6(IV), have not been isolated (Hudson, Reeders and Tryggwason, 1993; Zhou, Ding, Zhao and Reeders, 1994) and the clones for the a3(IV), a4(IV), a5(IV) and a6(IV) have been reported (Zhou et al., 1994). There is evidence that the latter are also distributed in several types of basement membranes including the kidney glomerulus, the alveolus, the choroid plexus and lens capsule (Ninomiya, Kagawa, Iyama, Naito, Kishiro, Seyer, Sugimoto, Oohashi and Sado, 1995). Lens capsule collagen may be obtained in purified forms. It contains all the types of chains except a6(IV).
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Monboisse, J.C. et al. (1998). The Interaction of Human Neutrophils with Type IV Collagen Involves an Inhibitory Signal Transduction Pathway. In: Maragoudakis, M.E. (eds) Angiogenesis. NATO ASI Series, vol 298. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9185-3_22
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