Cell Biology of Extracellular Matrix by Elizabeth D. Hay (auth.), Elizabeth D. Hay (eds.)

By Elizabeth D. Hay (auth.), Elizabeth D. Hay (eds.)

At a contemporary assembly to debate the domain names of cellphone biology, I placed forth a case for the extracellular matrix, even if my argument ran the chance of falling on deaf ears. finally, the matrix is EXTRAcellular, outdoor the cells. during this e-book, notwithstanding, the authors make a compelling case for the relevance of the matrix to mobile matters. not just are quite a few mobilephone forms, together with many epithelia, particularly stuck up within the enterprise of producing matrix elements, but in addition such a lot of them comprise matrix molecules in exoskeletons which are hooked up to the plasmalemma and that manage or differently effect the affairs of the cyto­ plasm. the assumption of this e-book is to offer the extracellular matrix to telephone biolo­ gists of all degrees. The authors are lively and busy investigators, well-known specialists of their fields, yet all have been captivated with the possibility of writing for this viewers. The chapters are usually not "review" articles within the ordinary feel, nor are they rehashes of symposium talks; they have been written in particular for this ebook and so they current the "state of the artwork" in attractive kind, with considerable references to extra technical or historic stories. The booklet is wealthy in electron micro­ graphs and diagrams and for lots of of the latter, in addition to for the layout of the canopy, we're indebted to Sylvia J. Keene, clinical illustrator for the dept of Anatomy at Harvard clinical Scrool. We additionally owe designated due to Susan G.

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3. Type III Collagen Type III collagen has a tissue distribution similar to type I, except for bone, tendon, and cornea, in which it is either absent or present only in very small amounts. , 1971; Chung and Miller, 1974; Epstein, 1974). Immunocytochemical staining experiments with specific antibodiessuggestthat type III is theprincipalcomponentofthe small (50 nm wide), argyrophilic collagen fibers that characterize reticular connective tissues. Type III collagen is most easily obtained by limited pepsin digestion of reticular connective tissue, followed by salt fractionation to separate it from other collagens, chiefly type I.

Nusgens, D. , and Lapiere, C. , 1971, Collagen made of extended a-chains, procollagen, in genetically defective dermatosparaxic calves, Eur. ]. Biochem. 23:533-543. Levene, C. , 1959, Alterations in state of molecular aggregation of collagen induced in chick embryos by /3-aminopropionitrile (lathyrus factor),]. Exp. Med. 110:771-790. Linsenmayer, T. , 1974, Temporal and spatial transitions in collagen types during embryonic chick limb development. II. Comparison of the embryonic cartilage collagen molecule with that from adult cartilage, Dev.

Fessler, L. , Morris, N. , and Fessler, J. , 1975, Procollagen: Biological scission of amino and carboxyl extension peptides, Proc. Nat!. Acad. Sci. USA 72:4905-4909. Fietzek, P. , and Kuhn, K, 1975, Information contained in the amino acid sequence of the a 1{I)-chain of collagen and its consequences upon the formation of the triple helix, of fibrils and crosslinks, Mol. Cell. Biochem. 8:141-157. , and Miller, E. , 1979, Collagen in the Physiology and Pathology of Connective Tissue, Gustav Fischer Verlag, New York.

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