Semiquantitative Analysis of Apolipoprotein A-I Modified by Advanced Glycation End Products in Diabetes Mellitus

Author:

Kurosaki Yoshifumi,Tsukushi Tomoaki1,Munekata Shinichi1,Akahoshi Tohru2,Moriya Tatsumi3,Ogawa Zensuke

Affiliation:

1. Department of Clinical Laboratory; Kitasato University Hospital; Sagamihara; Japan

2. Department of General Medicine; School of Medicine; Kitasato University; Sagamihara; Japan

3. Department of Endocrinology; Diabetes & Metabolism; School of Medicine; Kitasato University; Sagamihara; Japan

Publisher

Wiley

Subject

Microbiology (medical),Biochemistry, medical,Medical Laboratory Technology,Clinical Biochemistry,Public Health, Environmental and Occupational Health,Hematology,Immunology and Allergy

Reference24 articles.

1. Correlation of glucose regulation and hemoglobin A1c in diabetes mellitus;Koening;N Eng J Med,1976

2. The role of glycation in aging and diabetes mellitus;Boekel;Mol Biol Rep,1991

3. Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha- acetylarginine, N alpha-acetylcysteine, and N alpha acetyllysine, and bovine serum albumin;Lo;J Biol Chem,1994

4. In vivo glucosylated LpA-I subfraction;Bruno;Arterioscler Thromb Vasc Biol,1997

5. High glucose stimulates macrophage SR-BI expression and induces a switch in its activity from cholesterol efflux to cholesterol influx;Gantman;Biochem Biophys Res Commun,2010

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