Kinetin inhibits protein oxidation and glycoxidation in vitro

Biochem Biophys Res Commun. 2000 Oct 5;276(3):1265-70. doi: 10.1006/bbrc.2000.3616.

Abstract

We tested the ability of N(6)-furfuryladenine (kinetin) to protect against oxidative and glycoxidative protein damage generated in vitro by sugars and by an iron/ascorbate system. At 50 microM, kinetin was more efficient (82% inhibition) than adenine (49% inhibition) to inhibit the bovine serum albumin (BSA)-pentosidine formation in slow and fast glycation/glycoxidation models. Kinetin also inhibited the formation of BSA-carbonyls after oxidation significantly more than adenine did. However both compounds inhibited the advanced glycation end product (AGE) formation to the same extent (59-68% inhibition). At 200 microM, kinetin but not adenine, limited the aggregation of BSA during glycation. These data suggest that kinetin is a strong inhibitor of oxidative and glycoxidative protein-damage generated in vitro.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenine / analogs & derivatives*
  • Adenine / pharmacology*
  • Animals
  • Arabinose / pharmacology
  • Arginine / analogs & derivatives*
  • Arginine / metabolism
  • Cattle
  • Glycation End Products, Advanced / metabolism*
  • Glyoxal / pharmacology
  • Kinetin
  • Lysine / analogs & derivatives*
  • Lysine / metabolism
  • Oxidants / antagonists & inhibitors*
  • Oxidants / metabolism
  • Oxidation-Reduction / drug effects
  • Protein Denaturation / drug effects
  • Reactive Oxygen Species / metabolism
  • Ribose / pharmacology
  • Serum Albumin / chemistry*
  • Serum Albumin / metabolism*
  • Time Factors

Substances

  • Glycation End Products, Advanced
  • Oxidants
  • Reactive Oxygen Species
  • Serum Albumin
  • Glyoxal
  • Ribose
  • Arginine
  • Arabinose
  • pentosidine
  • Adenine
  • Lysine
  • Kinetin