By Eugene J. Kucharz M.D., Ph.D. (auth.)
This publication describes each demeanour during which collagen is occupied with common anddisease-altered states of a number of the organs and platforms. within the first a part of the e-book the biochemical facets of collagens are reviewed, together with their constitution, heterogeneity, syntheses, and degradation. the most half specializes in the involvement of collagen in bone, cartilage, tendon, muscle, middle, vessels, lungs, liver, pores and skin, eye, ear, tooth, periodontal tissues, kidneys and reproductive, hemopoietic,and worried platforms. The effect of radiation and food on collagen, the position of collagen in neoplasms, the hormonal regulate of its metabolism, immunobiology and the pharmacology of collagen also are defined. an important function of the ebook is the great evaluate of the scientific facets of collagen, from these recognized intimately to these in simple terms hypothesized together with hereditary problems affecting collagen and so-called collagen ailments. every one bankruptcy reviewsknown or attainable mechanisms of collagen involvement and alterations in indices of collagen which are measured in scientific perform to watch those phenomena. the truth that collagen is concerned into the pathophysiology of virtually all organs and physique structures implies that physicians in just about all branches of medication will locate this e-book of significant curiosity.
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Extra resources for The Collagens: Biochemistry and Pathophysiology
Example text
It is a homotrimer of a 1 (X), with a molecular weight of 59000 Da (Schmid and Linsenmayer 1987). The molecule consists of two noncollagenous domains, NC1 and NC2, located at both ends of the collagenous domain of 460 amino acid residues. The NC1 domain is located at the carboxyterminal end of the molecule and is substantially larger than the NC2 domain; it contains 170 amino acid residues. The helical domain of the molecule has two types of interruptions in the Gly-X-Y sequence. Four positions have a Gly-X-Gly sequence, and three others have a Gly-X-Y separated from the next triplet by two additional amino acid residues.
It is possible that type V collagen in vivo contributes to fibrillogenesis of type I collagen. This suggestion arose during immunolocalization studies of type V collagen in the cornea (see Chap. 17). 1\vo possible models of fibers containing types I and V collagens have been suggested. The molecules of both types can be intimately mixed throughout the whole cross-section of a fiber, or type V collagen could be restricted to the central part of the fiber (Linsenmayer et al. 1983, 1984, 1985; Fitch et al.
The gene COUAl was found at q21-q25 bands of chromosome 17 (Huerre et al. 1982; Solomon et al. 1984; Retief et al. 1985). The gene COUA2 is located on chromosome 7 approximately within bands q21-q22 (Henderson et al. 1983; Solomon et al. 1983; Junien et al. 1983; Myers and Emanuel 1987). 2 (Strom et al. 1984; Huerre-Jeanpierre et al. 1986; Arheden et al. 1989; Vikkula and Peltonen 1989). 3-q31 (Emanuel et al. 1985). The genes coding both chains of the basement membrane collagen, type IV, are found on chromosome 13.