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Autoantibodies to the amino-terminal fragment of beta-fodrin expressed in glandular epithelial cells in patients with Sjögren's syndrome

Kuwana, M ; Okano, T ; Ogawa, Y ; Kaburaki, J ; Kawakami, Y

The Journal of immunology (1950), 2001-11, Vol.167 (9), p.5449-5456 [Periódico revisado por pares]

United States

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  • Título:
    Autoantibodies to the amino-terminal fragment of beta-fodrin expressed in glandular epithelial cells in patients with Sjögren's syndrome
  • Autor: Kuwana, M ; Okano, T ; Ogawa, Y ; Kaburaki, J ; Kawakami, Y
  • Assuntos: Autoantibodies - analysis ; Carrier Proteins - genetics ; Carrier Proteins - immunology ; Caspase 3 ; Caspase 8 ; Caspase 9 ; Caspases - metabolism ; DNA, Complementary - isolation & purification ; Epithelial Cells - immunology ; Graft vs Host Disease - immunology ; Granzymes ; Humans ; Lacrimal Apparatus - immunology ; Microfilament Proteins - genetics ; Microfilament Proteins - immunology ; Peptide Fragments - immunology ; Serine Endopeptidases - metabolism ; Sjogren's Syndrome - immunology
  • É parte de: The Journal of immunology (1950), 2001-11, Vol.167 (9), p.5449-5456
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
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  • Descrição: Sjögrens's syndrome (SS) is an autoimmune disease characterized by destruction of lacrimal and salivary glands, but the mechanisms underlying the disease process are unclear. By immunoscreening a HepG2 cDNA library with serum from an SS patient we isolated a cDNA encoding amino-terminal 616 aa of beta-fodrin, a membrane skeleton protein associated with ion channels and pumps. Serum Ab to the amino-terminal fragment of beta-fodrin was frequently detected in SS patients compared with rheumatic disease patients without SS or healthy controls (70 vs 12 or 4%; p < 0.00001). All the anti-beta-fodrin-positive sera recognized the amino-terminal fragment with no homology to alpha-fodrin. Anti-beta-fodrin Abs in patients' sera as well as mouse polyclonal sera raised against the amino-terminal beta-fodrin fragment did not react with intact beta-fodrin, but recognized the 65-kDa amino-terminal fragment generated through cleavage by caspase-3 or granzyme B. When expression of intact and fragmented beta-fodrin in lacrimal glands was assessed by immunohistochemistry, the antigenic amino-terminal fragment was distributed diffusely in acinar epithelial cell cytoplasm, whereas the carboxyl-terminal fragment and/or intact beta-fodrin were localized in peripheral cytoplasm, especially at the basal membrane, in SS patients. In contrast, intact beta-fodrin was detected primarily at the apical membrane of epithelia, and the amino-terminal fragment was scarcely detected in control patients with chronic graft-vs-host disease. These findings suggest that cleavage and altered distribution of beta-fodrin in glandular epithelial cells may induce impaired secretory function and perpetuate an autoimmune response to beta-fodrin, leading to autoantibody production and glandular destruction in SS.
  • Editor: United States
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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