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Titolo:
CLEAVAGE OF BP180, A 180-KDA BULLOUS PEMPHIGOID ANTIGEN, YIELDS A 120-KDA COLLAGENOUS EXTRACELLULAR POLYPEPTIDE
Autore:
HIRAKO Y; USUKURA J; UEMATSU J; HASHIMOTO T; KITAJIMA Y; OWARIBE K;
Indirizzi:
NAGOYA UNIV,GRAD SCH HUMAN INFORMAT,UNIT BIOSYST,CHIKUSA KU NAGOYA AICHI 46401 JAPAN NAGOYA UNIV,SCH SCI,DEPT BIOL MOL NAGOYA AICHI 46401 JAPAN SUZUKA UNIV MED SCI & TECHNOL SUZUKA 51002 JAPAN KURUME UNIV,SCH MED,DEPT DERMATOL FUKUOKA 830 JAPAN GIFU UNIV,SCH MED,DEPT DERMATOL GIFU 500 JAPAN NATL INST BASIC BIOL OKAZAKI AICHI 444 JAPAN NAGOYA UNIV,SCH MED,DEPT ANAT NAGOYA AICHI 46401 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 16, volume: 273, anno: 1998,
pagine: 9711 - 9717
SICI:
0021-9258(1998)273:16<9711:COBA1B>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
BENIGN EPIDERMOLYSIS-BULLOSA; ALPHA-6-BETA-4 INTEGRIN; BASEMENT-MEMBRANE; CELL-ADHESION; HEMIDESMOSOME FORMATION; PYLORIC ATRESIA; IDENTIFICATION; AUTOANTIBODIES; AUTOANTIGEN; DERMATOSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
Y. Hirako et al., "CLEAVAGE OF BP180, A 180-KDA BULLOUS PEMPHIGOID ANTIGEN, YIELDS A 120-KDA COLLAGENOUS EXTRACELLULAR POLYPEPTIDE", The Journal of biological chemistry, 273(16), 1998, pp. 9711-9717

Abstract

The hemidesmosome (HD) is a cell-to-substrate adhesion apparatus found in stratified and complex epithelia. One of the putative cell-matrixadhesion molecules present in the HD is the 18O-kDa bullous pemphigoid antigen (BP180), also termed type XVII collagen. In our previous study, using a monoclonal antibody (mAb) 1337, we have detected a 120-kDacollagenase-sensitive polypeptide in the HD fraction (Uematsu, J. andOwaribe, H. (1993) Cell Struct. Funct. 18, 588 (abstr.)). The presentstudy was undertaken to assess the relation of the 120-kDa polypeptide to this BP180. Immunofluorescence microscopy of bovine skin revealedthe basement membrane zone of skin to be stained clearly with mAb 1337, whereas the lateral surfaces of basal cells, which were decorated by typical antibodies against BP180, were not. The antibody did not detect HDs in cultured cells but rather in the culture medium. These results indicate a localization of mAb 1337 antigen distinct from BP180. However, the same polypeptide was also recognized by monoclonal antibodies to the extracellular but not the cytoplasmic part of BP180, and found to react with a polyclonal antibody against the non-collagenous 16A domain of BP180. Therefore, the polypeptide was identified as an extracellular fragment of BP180. mAb 1337 immunoprecipitated the 120-kDa fragment from the medium, but not the 180-kDa molecule of BP180 extracted from cultured cells, indicating that the antibody specifically recognizes the fragment. The mAb 1337 apparently recognizes a unique epitope that is exposed or formed by the cleavage. Hence, the staining pattern observed for bovine skin demonstrated the presence of the 120-kDaextracellular fragment. Rotary shadow electron microscopy of affinity-purified 120-kDa fragments demonstrated that they have the unique molecular shape consisting of a central rod and a flexible tail, without the globular head that is present in the BP180 molecule. From these results, we conclude that mAb 1337 shows unique epitope specificity, recognizing only the 120-kDa extracellular fragment of BP180, which is constitutively cleaved on the cell surface as a 120-kDa fragment both inin vivo and in vitro.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 14:01:16