Binding sites for carrier-immobilized carbohydrates in the kidney: Implication for the pathogenesis of Henoch-Schonlein purpura and/or IgA nephropathy

Anna Šedivá, Karel Smetana, Josef Stejskal, Jiřina Bartůňková, Fu-Tong Liu, Nicolai V. Bovin, Hans Joachim Gabius

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Background. Henoch-Schonlein purpura is a common vasculitis of childhood affecting the skin, joints, gastrointestinal tract, and kidney. The mesangial deposition of IgA1 is the most critical factor for the prognosis of patients with this disease. The aberrant glycosylation of the IgA1 subclass with the absence of terminally located galactose and presence of only α-N-acetylgalactosamine in O-linked oligosaccharides in the hinge region of IgA1 represents a prominent difference from the normal IgA1. These alterations prompt the supposition that the sugar part may guide IgA deposition by recognition of endogenous lectins on the mesangium. Methods. Owing to the limited knowledge about the expression of carbohydrate-binding sites in the human kidney we initiated the study of this aspect with a class of tools which are suitable to map the lectinome of cells. Employing biolinylated neoglycoconjugates, glycosaminoglycans, and sulphated polysaccharides we monitored the presence of accessible carbohydrate-binding sites in control kidneys represented by tumour-free areas or kidneys with Grawitz tumour and in biopsies from patients with Henoch-Schonlein purpura-associated IgA nephropathy. Results. Using frozen sections, no expression of any tested carbohydrate-binding site(s) was observed in the endothelial and the mesangial cells in glomeruli of the control kidneys as well as in the biopsies from Henoch-Schonlein purpura IgA nephropathic kidneys, in contrast to the tubules. The N-acetylgalactosamine-binding sites were expressed only in the inner layer of Bowman's capsule of 20% of glomeruli of the control kidney from one patient with Grawitz tumour and one biopsy from a patient with Henoch-Schonlein purpura-associated IgA nephropathy. However, the macrophages in the glomeruli of patients with IgA nephropathy and interstitial macrophages from both studied groups, i.e. without and with IgA nephropathy harbour capacity to recognize carrier-immobilized α-acetylgalactosamine. Access to this binding site for the neoligand conjugate can be blocked by the monoclonal antibody MEM-18 recognizing CD14 antigen. Conclusion. The possibility for a participation of macrophage deposition of IgA1 in mesangium via a lectin mechanism involving this binding capacity warrants further studies.

Original languageEnglish (US)
Pages (from-to)2885-2891
Number of pages7
JournalNephrology Dialysis Transplantation
Volume14
Issue number12
StatePublished - 1999

Keywords

  • α-N-acetylgalactosamine
  • CD14
  • Henoch-Schonlein purpura
  • IgA nephropathy
  • Lectin macrophage

ASJC Scopus subject areas

  • Nephrology
  • Transplantation

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    Šedivá, A., Smetana, K., Stejskal, J., Bartůňková, J., Liu, F-T., Bovin, N. V., & Gabius, H. J. (1999). Binding sites for carrier-immobilized carbohydrates in the kidney: Implication for the pathogenesis of Henoch-Schonlein purpura and/or IgA nephropathy. Nephrology Dialysis Transplantation, 14(12), 2885-2891.