Immunochemical evidence for the presence of advanced glycation end products in human lens proteins and its positive correlation with aging

J Biol Chem. 1992 May 25;267(15):10211-4.

Abstract

Prolonged incubation of protein with reducing sugar proceeds through a series of reactions involving early stage products to the advanced glycation end products with fluorescence, brown color, and cross-linking. Known collectively as the Maillard reaction, these changes have been suggested as factors in diabetic complications and the aging process. The early stage products have been demonstrated in vivo, but evidence for the presence in vivo of the advanced glycation end products has been limited. We sought to provide immunochemical evidence by the preparation and use of polyclonal and monoclonal antibodies to these end products (Horiuchi, S., Araki, N., and Morino, Y. (1991) J. Biol. Chem. 266, 7329-7332) as probes to identify and quantitate such compounds in human lens crystallins. Neither of the antibodies reacted with extracts from infant lenses, but fractions from adult lenses showed a significant reactivity, correlating with lens age. Our findings provide the first immunochemical evidence that human lens crystallins contain advanced glycation end products and that these products increase with tissue age.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adult
  • Aged
  • Aged, 80 and over
  • Aging / metabolism*
  • Antibodies, Monoclonal
  • Blotting, Western
  • Child, Preschool
  • Crystallins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme-Linked Immunosorbent Assay
  • Glucose / metabolism*
  • Humans
  • Immunochemistry
  • Infant
  • Maillard Reaction
  • Middle Aged

Substances

  • Antibodies, Monoclonal
  • Crystallins
  • Glucose