Glycoxidative modification of AA amyloid deposits in renal tissue | Zendy

Noriko Uesugi | Zendy; Noriyuki Sakata | Zendy; Ryoji Nagai | Zendy; Tadashi Jono | Zendy; Seikoh Horiuchi | Zendy; Shigeo Takebayashi | Zendy

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Glycoxidative modification of AA amyloid deposits in renal tissue

Author(s) -

Noriko Uesugi,

Noriyuki Sakata,

Ryoji Nagai,

Tadashi Jono,

Seikoh Horiuchi,

Shigeo Takebayashi

Publication year - 2000

Publication title -

nephrology dialysis transplantation

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.654

H-Index - 168

eISSN - 1460-2385

pISSN - 0931-0509

DOI - 10.1093/ndt/15.3.355

Subject(s) - amyloidosis , amyloid (mycology) , medicine , beta 2 microglobulin , al amyloidosis , laminin , pathology , glycation , diabetic nephropathy , kidney , endocrinology , diabetes mellitus , extracellular matrix , chemistry , biochemistry , immunology , immunoglobulin light chain , antibody

N(epsilon)-carboxymethyllysine (CML) is a product of the oxidative modification of glycated proteins, which damages proteins with ageing, diabetes, uraemia and Alzheimer's disease. In contrast, pyrraline is one of the advanced glycation end products, which is independent of oxidative processes. CML has been identified in beta-amyloid of Alzheimer's disease and beta(2)-microglobulin-associated amyloid. We investigated whether CML and pyrraline are formed in AA and AL amyloid of the kidney.

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