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Cited by 398

The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.

beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis.

Open access
Miyata, T, Oda, O, Inagi, R, Iida, Y, Araki, N, Yamada, N, Horiuchi, S, Taniguchi, N, Maeda, K, Kinoshita, T·1993·Journal of Clinical Investigation

Abstract

beta 2-Microglobulin (beta 2M) is a major constituent of amyloid fibrils in hemodialysis-associated amyloidosis, a complication of long-term hemodialysis patients. Amyloid fibril proteins were isolated from connective tissues forming carpal tunnels in hemodialysis patients with carpal tunnel syndrome. Two-dimensional polyacrylamide gel electrophoresis and Western blotting demonstrated that most of the beta 2M forming amyloid fibrils exhibited a more acidic pI value than normal beta 2M. This acidic beta 2M was also found in a small fraction of beta 2M in sera and urine from these patients, whereas heterogeneity was not observed in healthy individuals. We purified acidic and normal beta 2M from the urine of long-term hemodialysis patients and compared their physicochemical and immunochemical properties. Acidic beta 2M, but not normal beta 2M, was brown in color and fluoresced, both of which are characteristics of advanced glycation end products (AGEs) of the Maillard reaction. Immunochemical studies showed that acidic beta 2M reacted with anti-AGE antibody and also with an antibody against an Amadori product, an early product of the Maillard reaction, but normal beta 2M did not react with either antibody. Incubating normal beta 2M with glucose in vitro resulted in a shift to a more acidic pI, generation of fluorescence, and immunoreactivity to the anti-AGE antibody. The beta 2M forming amyloid fibrils also reacted with anti-AGE antibody. These data provided evidence that AGE-modified beta 2M is a dominant constituent of the amyloid deposits in hemodialysis-associated amyloidosis.

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Metadata

Authors
Miyata, T., Oda, O., Inagi, R., Iida, Y., Araki, N., Yamada, N., Horiuchi, S., Taniguchi, N., Maeda, K., & Kinoshita, T.
Venue
Journal of Clinical Investigation
Published
1993-09-01
Volume
92
Issue
3
Pages
1243-1252
ISSN
0021-9738 (ISSN-L)
OpenAlex
W2026782054
Cited by
398
References
33
FWCI
17.53
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis. https://app.cochat.ai/papers/10.1172/jci116696
The paper
Miyata, T., Oda, O., Inagi, R., Iida, Y., Araki, N., Yamada, N., Horiuchi, S., Taniguchi, N., Maeda, K., & Kinoshita, T. (1993). beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis. Journal of Clinical Investigation. https://doi.org/10.1172/jci116696

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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