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Interactions between the matricellular protein BM-40 and fibrillar collagens type I, II and III

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Introduction 5 Table 1: Genetically distinct collagen types (continued from page 3). Type Chain(s) Molecular forms Main Distribution Key Features XVII α1(XVII) (?) Bullous pemphigoid antigen, expressed at dermal-epidermal junction Triple helix is interrupted in several places. Transmembrane collagen with an hydrophobic domain XVIII α1(XVIII) (?) Expressed in highly vascularised tissues Triple helix is interrupted in several places XIX α1(XIX) (?) Expressed in very small amounts by cultured skin fibroblasts and tumour cells A fibril-associated collagen with an interrupted triple helix (FACIT) with five triple helical subdomains XX α1(XX) (?) Minor component of several connective tissues, such as sternal cartilage, cornea and tendon and embryonic tissue as corneal epithelium A fibril-associated collagen with an interrupted triple helix (FACIT) XXI α1(XXI) (?) Expressed in tissues with a muscle phenotype (heart, skeletal muscle, smooth muscle and placenta) A fibril-associated collagen with an interrupted triple helix (FACIT) XXII α1(XXII) Hair follicle Unspecified XXIII α1(XXIII) [α1(XXIII)] 3 (?) Cornea, overexpressed in adenocarcinoma cells; cellular localization Transmembrane collagen with an hydrophobic domain XXIV α1(XXIV) (?) Cartilage, retina, cornea, skin Fibrillar collagen close to collagens type V and XI XXV α1(XXV) (?) Overexpressed in neurons Transmembrane collagen with an hydrophobic domain XXVI α1(XXVI) (?) Specifically expressed in testis and ovary Unspecified, maybe related to collagen type XIII and XXV XXVII α1(XXVII) (?) Cartilage, eye, ear, lung and colon Fibrillar collagen Collagen structure The basic conformation of the triple helix has been deduced at the end of the sixties from X-ray diffraction studies on collagen in tendon. The comparison between the chemical and the crystallographic data has shown that each of the three polypeptide chains in the molecule forms an extended left-handed polyproline II helix, which is stabilized by the high imino acid content. The three chains are then supercoiled around a common axis in a right-handed manner to form the triple helix which is stabilized by hydrogen bonds between the chains (Fig. 1) (Rich A. et al., 1961; Ramachandran G.N., 1967; Fraser R.B.D. et al., 1973).

Anteprima della Tesi di Camilla Giudici

Anteprima della tesi: Interactions between the matricellular protein BM-40 and fibrillar collagens type I, II and III, Pagina 5

Tesi di Dottorato

Dipartimento: Dipartimento di Biochimica

Autore: Camilla Giudici Contatta »

Composta da 94 pagine.

 

Questa tesi ha raggiunto 290 click dal 12/10/2004.

 

Consultata integralmente una volta.

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