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DAF in diabetic patients is subject to glycation/inactivation at its active site residues.
Flückiger, Rudolf; Cocuzzi, Enzo; Nagaraj, Ram H; Shoham, Menachem; Kern, Timothy S; Medof, M Edward.
Afiliación
  • Flückiger R; Harvard Medical School, Boston, MA, USA.
  • Cocuzzi E; Institute of Pathology, Case Western Reserve University, Cleveland, OH, USA.
  • Nagaraj RH; Department of Ophthalmology, Case Western Reserve University, Cleveland, OH, USA.
  • Shoham M; Department of Biochemistry, Case Western Reserve University, Cleveland, OH, USA.
  • Kern TS; Department of Medicine, Case Western Reserve University, Cleveland, OH, USA; Center for Diabetes Research, Case Western Reserve University, Cleveland, OH, USA.
  • Medof ME; Institute of Pathology, Case Western Reserve University, Cleveland, OH, USA; Department of Ophthalmology, Case Western Reserve University, Cleveland, OH, USA; Department of Medicine, Case Western Reserve University, Cleveland, OH, USA. Electronic address: mxm16@case.edu.
Mol Immunol ; 93: 246-252, 2018 01.
Article en En | MEDLINE | ID: mdl-28886871
Decay accelerating factor (DAF or CD55) is a cell associated C3 and C5 convertase regulator originally described in terms of protection of self-cells from systemic complement but now known to modulate adaptive T cell responses. It is expressed on all cell types. We investigated whether nonenzymatic glycation could impair its function and potentially be relevant to complications of diabetes mellitus and other conditions that result in nonenzymatic glycation including cancer, Alzheimer's disease, and aging. Immunoblots of affinity-purified DAF from erythrocytes of patients with diabetes showed pentosidine, glyoxal-AGEs, carboxymethyllysine, and argpyrimidine. HPLC/MS analyses of glucose modified DAF localized the sites of AGE modifications to K125 adjacent to K126, K127 at the junction of CCPs2-3 and spatially near R96, and R100, all identified as being critical for DAF's function. Functional analyses of glucose or ribose treated DAF protein showed profound loss of its regulatory activity. The data argue that de-regulated activation of systemic complement and de-regulated activation of T cells and leukocytes could result from non-enzymatic glycation of DAF.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Productos Finales de Glicación Avanzada / Antígenos CD55 / Diabetes Mellitus Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Mol Immunol Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Productos Finales de Glicación Avanzada / Antígenos CD55 / Diabetes Mellitus Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Mol Immunol Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido