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Platelet-localized ST6Gal1 does not impact IgG sialylation.
Glendenning, Leandre M; Zhou, Julie Y; Kukan, Emily N; Gao, Chao; Cummings, Richard D; Joshi, Smita; Whiteheart, Sidney W; Cobb, Brian A.
Afiliación
  • Glendenning LM; Department of Pathology, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106-7288, USA.
  • Zhou JY; Department of Pathology, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106-7288, USA.
  • Kukan EN; Department of Pathology, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106-7288, USA.
  • Gao C; Harvard Medical School Center for Glycoscience, National Center for Functional Glycomics, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA.
  • Cummings RD; Harvard Medical School Center for Glycoscience, National Center for Functional Glycomics, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA.
  • Joshi S; Department of Molecular and Cellular Biochemistry, University of Kentucky, 741 S Limestone Street, Lexington, KY 40536-0509, USA.
  • Whiteheart SW; Department of Molecular and Cellular Biochemistry, University of Kentucky, 741 S Limestone Street, Lexington, KY 40536-0509, USA.
  • Cobb BA; Department of Pathology, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106-7288, USA.
Glycobiology ; 33(11): 943-953, 2023 Dec 25.
Article en En | MEDLINE | ID: mdl-37379323
The IgG antibody class forms an important basis of the humoral immune response, conferring reciprocal protection from both pathogens and autoimmunity. IgG function is determined by the IgG subclass, as defined by the heavy chain, as well as the glycan composition at N297, the conserved site of N-glycosylation within the Fc domain. For example, lack of core fucose promotes increased antibody-dependent cellular cytotoxicity, whereas α2,6-linked sialylation by the enzyme ST6Gal1 helps to drive immune quiescence. Despite the immunological significance of these carbohydrates, little is known about how IgG glycan composition is regulated. We previously reported that mice with ST6Gal1-deficient B cells have unaltered IgG sialylation. Likewise, ST6Gal1 released into the plasma by hepatocytes does not significantly impact overall IgG sialylation. Since IgG and ST6Gal1 have independently been shown to exist in platelet granules, it was possible that platelet granules could serve as a B cell-extrinsic site for IgG sialylation. To address this hypothesis, we used a platelet factor 4 (Pf4)-Cre mouse to delete ST6Gal1 in megakaryocytes and platelets alone or in combination with an albumin-Cre mouse to also remove it from hepatocytes and the plasma. The resulting mouse strains were viable and had no overt pathological phenotype. We also found that despite targeted ablation of ST6Gal1, no change in IgG sialylation was apparent. Together with our prior findings, we can conclude that in mice, neither B cells, the plasma, nor platelets have a substantial role in homeostatic IgG sialylation.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Inmunoglobulina G / Factores Inmunológicos Límite: Animals Idioma: En Revista: Glycobiology Asunto de la revista: BIOQUIMICA Año: 2023 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: Inmunoglobulina G / Factores Inmunológicos Límite: Animals Idioma: En Revista: Glycobiology Asunto de la revista: BIOQUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido