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Titolo:
Transient translocation of hemidesmosomal bullous pemphigoid antigen 1 from cytosol to membrane fractions by 12-O-tetradecanoylphorbol-13-acetate treatment and Ca2+-switch in a human carcinoma cell line
Autore:
Matsuoka, Y; Yamada, T; Seishima, M; Hirako, Y; Owaribe, K; Kitajima, Y;
Indirizzi:
Gifu Univ, Sch Med, Dept Dermatol, Gifu 5008705, Japan Gifu Univ Gifu Japan 5008705 Sch Med, Dept Dermatol, Gifu 5008705, Japan Nagoya Univ, Sch Informat & Sci, Dept Nat Sci Informat, Nagoya, Aichi 4668550, Japan Nagoya Univ Nagoya Aichi Japan 4668550 rmat, Nagoya, Aichi 4668550, Japan
Titolo Testata:
JOURNAL OF DERMATOLOGICAL SCIENCE
fascicolo: 3, volume: 27, anno: 2001,
pagine: 206 - 214
SICI:
0923-1811(200111)27:3<206:TTOHBP>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSMEMBRANE PROTEIN BP180; BETA-4 INTEGRIN SUBUNIT; BASEMENT-MEMBRANE; EPITHELIAL-CELLS; PLASMA-MEMBRANE; KINASE-C; KERATINOCYTES; CONTACT; ADHESION; DOMAIN;
Keywords:
bullous pemphigoid; hemidesmosome; keratinocyte; protein kinase C;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Kitajima, Y Gifu Univ, Sch Med, Dept Dermatol, 40 Tsukasamachi, Gifu 5008705, Japan Gifu Univ 40 Tsukasamachi Gifu Japan 5008705 u 5008705, Japan
Citazione:
Y. Matsuoka et al., "Transient translocation of hemidesmosomal bullous pemphigoid antigen 1 from cytosol to membrane fractions by 12-O-tetradecanoylphorbol-13-acetate treatment and Ca2+-switch in a human carcinoma cell line", J DERMA SCI, 27(3), 2001, pp. 206-214

Abstract

We previously showed that 12-O-tetradecanoylphorbol-13-acetate (TPA) and Ca2+-switch from low (0.07 mM) to normal (1.87 mM) concentration in culture medium., which were also linked to activation of protein kinase C (PKC), lead to phosphorylation of 180 kDa-bullous pemphigoid antigen (BPAG) 2, but not of 230 kDa-BPAG1, and possibly to its disassembly from hemidesmosomes ina human squamous cell carcinoma cell line (DJM-1). In this study. we examined the effects of TPA and Ca2+-switch on intracellular localization of BPAG1 by immuno-blotting and immuno-fluorescence microscopy with monoclonal antibodies to the antigen after sub-cellular fractionation. In DJM-1 cells cultured in low Call medium, BPAG1 was detected as phosphate buffered saline-soluble (cytosolic), Triton X-100 soluble (roughly membrane-associated) andTriton X-100 insoluble (cytoskeleton-bound) forms, whereas in normal Ca2+-grown cells only as cytosolic and cytoskeleton-bound forms. In normal Ca2+-cultured cells, TPA (50 nM) caused a complete translocation of BPAG1 from cytosol to membrane fractions within 10 min, that was inhibited by pretreatment with H7 (a selective PKC inhibitor) at 40 muM. After 30 min and 4 h of TPA-treatment, BPAG I was exclusively detected in cytoskeleton fractions. Morphologically, immuno-fluorescence microscopy showed that treatment causeda marked reduction of BPAG1 from the cytoplasm and generated a linear pattern at cell-cell contacts. suggesting translocation of BPAG I from the cytosol to the plasma membrane. In contrast, the Ca2+-switch from low to normalcaused a prominent increase of BPAG1. both in cytosolic and membrane-associated forms after 4 h. that was inhibited both with H7 and cycloheximide (an inhibitor of protein synthesis) at 70 muM. suggesting a role for PKC and BPAG1 synthesis in these Ca2+-induced effects. These results suggest that TPA and Ca2+-switch induced BPAG1 translocation to membrane fractions possibly mediated by PKC-activation. Furthermore, whereas TPA affects the redistribution of BPAG1 among their pools without inducing their synthesis, Ca2+-switch induces both membrane translocation and synthesis of BPAG1, suggesting involvement of signaling other than PKC pathways in control of BPAG1 synthesis. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/10/20 alle ore 07:02:08