Oxidative protein damage with carbohydrates and lipids in uremia: 'Carbonyl stress'

R. Inagi, Toshio Miyata

Research output: Contribution to journalReview articlepeer-review

50 Citations (Scopus)


Chronic uremia appears to be in a state of an increased oxidative stress. Under oxidative stress, proteins are modified directly by reactive oxygen species with the eventual formation of oxidised amino acids. Proteins are also modified indirectly with reactive carbonyl compounds formed by the autoxidation of carbohydrates and lipids, with the eventual formation of the advanced glycation/lipoxidation end products (AGEs/ALEs). AGEs, pentosidine and carboxymethyllysine (CML), and ALE, malondialdehyde (MDA)-lysine, are elevated in plasma and matrix proteins of uremic patients several times above normal subjects. Precursor carbonyl compounds derived from carbohydrates and lipids are indeed elevated in uremic circulation. Uremia thus appears to be in a state of carbonyl overload with potentially damaging proteins (carbonyl stress). Carbonyl stress might be relevant to long-term complications associated with chronic renal failure and dialysis, such as dialysis-related amyloidosis and atherosclerosis. Immunohistochemical studies identified carbonyl stress in long-lived amyloid deposits and vascular lesions. Proteins modified under carbonyl stress exhibit several biological activities, which might, at least in part, account for the development of joint and vascular complications in uremia.

Original languageEnglish
Pages (from-to)95-98
Number of pages4
JournalBlood Purification
Issue number2-3
Publication statusPublished - 1999 Sep 3
Externally publishedYes


  • Advanced glycation end products (AGEs)
  • Atherosclerosis
  • Dialysis-related amyloidosis
  • Non-enzymatic reaction
  • Oxidative stress
  • Uremic complication

ASJC Scopus subject areas

  • Hematology
  • Nephrology

Fingerprint Dive into the research topics of 'Oxidative protein damage with carbohydrates and lipids in uremia: 'Carbonyl stress''. Together they form a unique fingerprint.

Cite this