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S Horiuchi

Researcher at Kumamoto University

Publications -  19
Citations -  1376

S Horiuchi is an academic researcher from Kumamoto University. The author has contributed to research in topics: Receptor & Serum albumin. The author has an hindex of 15, co-authored 19 publications receiving 1351 citations.

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Immunochemical approach to characterize advanced glycation end products of the Maillard reaction. Evidence for the presence of a common structure.

TL;DR: The results strongly suggest the presence of a common structure in AGE preparations, regardless of whether AGE products are generated from proteins, amino acids, or monoaminocarboxylic acids.
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Lysophosphatidylcholine plays an essential role in the mitogenic effect of oxidized low density lipoprotein on murine macrophages.

TL;DR: Results suggest that lyso-PC may play an essential role in the mitogenic activity of Ox-LDL and that the growth-stimulating effect of acetyl-LD lysophosphatidylcholine on murine resident macrophages was negligibly weak.
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Endocytic uptake of nonenzymatically glycosylated proteins is mediated by a scavenger receptor for aldehyde-modified proteins.

TL;DR: Endocytic uptake of AGE-proteins by macrophages appeared to be mediated by a scavenger receptor for aldehyde-modified proteins, providing evidence for the biological importance of the scavengers receptor in eliminating senescent macromolecules from the circulation.
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Advanced glycation endproduct-modified superoxide dismutase-1 (SOD1)-positive inclusions are common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutations and transgenic mice expressing human SOD1 with a G85R mutation.

TL;DR: The results suggest that a portion of the S OD1 composing both type of inclusions, probably toxic mutant SOD1, is modified by the AGEs, and that the formation of the A GE-modified SOD 1 is one of the mechanisms responsible for the aggregation involving no significant oxidative mechanisms.
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Characterization of a membrane-associated receptor from rat sinusoidal liver cells that binds formaldehyde-treated serum albumin.

TL;DR: Kinetic studies of binding of 125I-labeled formaldehyde-treated serum albumin with the membranes of sinusoidal liver cells demonstrated the presence of specific, high-affinity, saturable membrane-bound receptors with an apparent Kd = 8 micrograms of f-Alb/ml and the optimal pH at around 8.0.