Nonenzymatic glycosylation of immunoglobulin G impairs complement fixation

JPEN J Parenter Enteral Nutr. 1991 Jan-Feb;15(1):60-4. doi: 10.1177/014860719101500160.

Abstract

Transient hyperglycemia in patients receiving total parenteral nutrition may be associated with impaired immune function. The effects of short-term hyperglycemia on one aspect of antimicrobial immune function, ie, the ability of IgG to fix complement, were investigated. Aliquots of anti-human albumin, anti-horse ferritin, and anti-alkaline phosphatase were incubated for 0, 8, 16, 24, 48, and 96 hr with either 0 or 240 mg of glucose per deciliter of buffer. All samples were analyzed for the degree of glycation using a thiobarbituric acid assay, and for complement fixation ability using a microcomplement fixation assay. Significant increases in glycation over control samples were observed after only 16 hr (31 vs 15 mmol 5-hydroxymethylfurfural/mol IgG, p less than 0.01). Complement fixation was significantly altered after 48 hr of incubation (76 +/- 5% vs 90 +/- 8% total serum complement fixed by albumin/anti-albumin complex, p less than 0.03) when four of the 84 (4.7%) IgG lysine residues were glycated. It is demonstrated that a significant reduction in complement fixation by immunoglobulin occurs with elevated glucose concentrations and that this may play a clinically significant role in transiently hyperglycemic patients.

MeSH terms

  • Alkaline Phosphatase / immunology
  • Animals
  • Complement Fixation Tests*
  • Ferritins / immunology
  • Glycosylation
  • Humans
  • Hyperglycemia / immunology*
  • Immune Sera / immunology
  • Immune Sera / metabolism
  • Immunoglobulin G / immunology
  • Immunoglobulin G / metabolism*
  • Serum Albumin / immunology

Substances

  • Immune Sera
  • Immunoglobulin G
  • Serum Albumin
  • Ferritins
  • Alkaline Phosphatase