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Titolo:
Properties of the collagen type XVII ectodomain - Evidence for N- to C-terminal triple helix folding
Autore:
Areida, SK; Reinhardt, DP; Muller, PK; Fietzek, PP; Kowitz, J; Marinkovich, MP; Notbohm, H;
Indirizzi:
Med Univ Lubeck, Inst Mol Sci Med, D-23538 Lubeck, Germany Med Univ Lubeck Lubeck Germany D-23538 Sci Med, D-23538 Lubeck, Germany Vet Affairs Palo Alto Hlth Care Syst, Dermatol Serv, Palo Alto, CA 94304 USA Vet Affairs Palo Alto Hlth Care Syst Palo Alto CA USA 94304 CA 94304 USA Stanford Univ, Sch Med, Program Epithelial Biol, Stanford, CA 94305 USA Stanford Univ Stanford CA USA 94305 ithelial Biol, Stanford, CA 94305 USA Univ Rostock, Orthopad Klin, D-18057 Rostock, Germany Univ Rostock Rostock Germany D-18057 opad Klin, D-18057 Rostock, Germany
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 2, volume: 276, anno: 2001,
pagine: 1594 - 1601
SICI:
0021-9258(20010112)276:2<1594:POTCTX>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
BULLOUS PEMPHIGOID ANTIGEN; MOLECULAR RECOGNITION; CYTOPLASMIC DOMAIN; BP180 ECTODOMAIN; TRIMER FORMATION; PROCOLLAGEN; HEMIDESMOSOMES; PROTEIN; CELLS; CLEAVAGE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Notbohm, H Med Univ Lubeck, Inst Mol Sci Med, Ratzeburger Allee 160, D-23538 Lubeck, Germany Med Univ Lubeck Ratzeburger Allee 160 Lubeck Germany D-23538 y
Citazione:
S.K. Areida et al., "Properties of the collagen type XVII ectodomain - Evidence for N- to C-terminal triple helix folding", J BIOL CHEM, 276(2), 2001, pp. 1594-1601

Abstract

Collagen XVII is a transmembrane component of hemidesmosomal cells with important functions in epithelial-basement membrane interactions. Here we report on properties of the extracellular ectodomain of collagen XVII, which harbors multiple collagenous stretches. We have recombinantly produced subdomains of the collagen XVII ectodomain in a mammalian expression system. rColXVII-A spans the entire ectodomain from delta NC16a to NC1, rColXVII-B is similar but lacks the NC1 domain, a small N-terminal polypeptide rColXVII-Cencompasses domains delta NC16a to C15, and a small C-terminal polypeptiderColXVII-D comprises domains NC6 to NC1, Amino acid analysis of rColXVII-Aand -C demonstrated prolyl and lysyl hydroxylation with ratios for hydroxyproline/proline of 0.4 and for hydroxylysine/lysine of 0,5, A small proportion of the hydroxylysyl residues in rColXVII-C (similar to3.3%) was glycosylated. Limited pepsin and trypsin degradation assays and analyses of circular dichroism spectra clearly demonstrated a triple-helical conformation forrColXVII-A, -B, and -C, whereas the C-terminal rColXVII-D did not adopt a triple-helical fold. These results were further substantiated by electron microscope analyses, which revealed extended molecules for rColXVII-A and -C, whereas rColXVII-D appeared globular, Thermal denaturation experiments revealed melting temperatures of 41 degreesC (rCol/XVII-A), 39 degreesC (rColXVII-B), and 35 degreesC (rColXVII-C), In summary, our data suggest that triple helix formation in the ectodomain of ColXVII occurs with an N- to C-terminal directionality.

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Documento generato il 25/11/20 alle ore 06:43:12