Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
DEMONSTRATION OF THE MOLECULAR SHAPE OF BP180, A 180-KDA BULLOUS PEMPHIGOID ANTIGEN AND ITS POTENTIAL FOR TRIMER FORMATION
Autore:
HIRAKO Y; USUKURA J; NISHIZAWA Y; OWARIBE K;
Indirizzi:
NAGOYA UNIV,GRAD SCH HUMAN INFORMAT,UNIT BIOSYST,CHIKUSA KU NAGOYA AICHI 46401 JAPAN NAGOYA UNIV,SCH SCI,DEPT BIOL MOLEC,CHIKUSA KU NAGOYA AICHI 46401 JAPAN NAGOYA UNIV,SCH MED,DEPT ANAT,CHIKUSA KU NAGOYA AICHI 46401 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 23, volume: 271, anno: 1996,
pagine: 13739 - 13745
SICI:
0021-9258(1996)271:23<13739:DOTMSO>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
BASEMENT-MEMBRANE ADHESION; IMMUNOELECTRON MICROSCOPY; INTEGRIN ALPHA-6-BETA-4; ANCHORING FILAMENTS; EPITHELIAL-CELLS; HEMIDESMOSOMES; COMPONENT; PROTEINS; AUTOANTIBODIES; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
Y. Hirako et al., "DEMONSTRATION OF THE MOLECULAR SHAPE OF BP180, A 180-KDA BULLOUS PEMPHIGOID ANTIGEN AND ITS POTENTIAL FOR TRIMER FORMATION", The Journal of biological chemistry, 271(23), 1996, pp. 13739-13745

Abstract

The 180-kDa bullous pemphigoid antigen (BP180) is a hemidesmosomal transmembrane glycoprotein comprising interrupted collagen domains in its extracellular part, BP180 is also termed type XVII collagen, But thequestion of whether it actually takes a collagen-like triple helical conformation in. vivo has remained unanswered, Using a monoclonal antibody, we found that a sub-population of BP180 localizes at the lateralsurfaces of corneal basal cells and cultured cells, in addition to the basal surface, This subpopulation of BP180 could be solubilized by 0.5% Triton X-100 and, among examined cell lines, was found to be most abundant in BMGE+H, a bovine mammary gland epithelial cell line, The Triton soluble fraction of BMGE+H cells was used for characterization, On sucrose gradient centrifugation, the soluble BP180 demonstrated a value of approximately 7 S, and chemical cross-linking experiments revealed a trimer form, The calculated frictional ratio, f/f(0) = 2.8, suggests an asymmetric configuration, For further characterization, we purified the soluble BP180 by immunoaffinity column chromatography usingan anti-BP180 monoclonal antibody, Rotary shadowing images of the purified BP180 showed a quaver-like molecule consisting of a globular head, a central rod, and a flexible tail, With regard to the primary structure and species comparisons, the central rod, 60-70 nm in length, probably corresponds to the largest collagenous region, forming a collagen-like triple helix, in human form, The globular head and the flexible tail seem to correspond to the cytoplasmic and the interrupted collagenous region, respectively, of the extracellular portions, In conclusion, the present demonstration of the entire configuration of BP180, with a collagen-like trimer in its extracellular part, suggests that BP180 is one of the major components of anchoring filaments.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 14:17:05