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Titolo:
Molecular mapping of the major epitopes of BP180 recognized by herpes gestationis autoantibodies
Autore:
Lin, MS; Gharia, M; Fu, CL; Olague-Marchan, N; Hacker, M; Harman, KE; Bhogal, BS; Black, MM; Diaz, LA; Giudice, GJ;
Indirizzi:
Med Coll Wisconsin, Dept Dermatol, Milwaukee, WI 53226 USA Med Coll Wisconsin Milwaukee WI USA 53226 rmatol, Milwaukee, WI 53226 USA Med Coll Wisconsin, Dept Biochem, Milwaukee, WI 53226 USA Med Coll Wisconsin Milwaukee WI USA 53226 iochem, Milwaukee, WI 53226 USA VA Med Ctr, Milwaukee, WI USA VA Med Ctr Milwaukee WI USAVA Med Ctr, Milwaukee, WI USA St Thomas Hosp, St Johns Inst Dermatol, London SE1 7EH, England St Thomas Hosp London England SE1 7EH Dermatol, London SE1 7EH, England
Titolo Testata:
CLINICAL IMMUNOLOGY
fascicolo: 3, volume: 92, anno: 1999,
pagine: 285 - 292
SICI:
1521-6616(199909)92:3<285:MMOTME>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
PEMPHIGOID AUTOANTIBODIES; NC16A DOMAIN; ANTI-BP180 AUTOANTIBODIES; HG-FACTOR; B-CELL; ANTIGEN; ECTODOMAIN; REACT; IMMUNOPATHOLOGY; PROTEIN;
Keywords:
autoimmunity; keratinocyte; bullous disease; hemidesmosome;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Lin, MS Med Coll Wisconsin, Dept Dermatol, Milwaukee, WI 53226 USA Med Coll Wisconsin Milwaukee WI USA 53226 Milwaukee, WI 53226 USA
Citazione:
M.S. Lin et al., "Molecular mapping of the major epitopes of BP180 recognized by herpes gestationis autoantibodies", CLIN IMMUNO, 92(3), 1999, pp. 285-292

Abstract

Herpes gestationis (HG) is an autoantibody-mediated subepidermal bullous dermatosis associated with pregnancy. The primary target of HG autoantibodies is BP180, a 180-kDa hemidesmosomal glycoprotein. We previously showed that autoantibodies and autoimmune T lymphocytes from HG patients recognize the MCW-1 antigenic site (AA 507-520), which is located in the membrane-proximal noncollagenous domain (NC16A) of BP180. Here, we analyzed the sera of 37 HG; patients to further define the sites on BP180 that are targeted by autoantibodies. All of the HG sera, but none of the control sera, were immunoreactive with sec180e, a 120-kDa recombinant protein encompassing the entire BP180 extracellular domain. HG sera depleted of reactivity to NC16A no longer reacted with sec180e, indicating that the major HG-associated epitopeson BP180 are restricted to the NC16A domain. The vast majority of the HG sera (34 of 37) reacted with a 7 amino acid peptide corresponding to the N-terminal half of MCW-1 (MCW-1A). Eleven HG sera (including the 3 that failedto react with MCW-1A) recognized one or more of three antigenic sites located within a 15 amino acid stretch immediately downstream of MCW-1A. In summary, we have identified four major HG-associated epitopes clustered withina 22 amino acid region of the BP180 ectodomain. These findings support thehypothesis that an autoimmune response to the BP180 NC16A domain is a crucial step in the pathogenesis of HG. (C) 1999 Academic Press.

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Documento generato il 10/07/20 alle ore 00:19:06