The liver is the main site for metabolism of circulating advanced glycation end products (Q77530330)

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6 December 2019

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title

The liver is the main site for metabolism of circulating advanced glycation end products (English)

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6 December 2019

author name string

Seikoh Horiuchi

series ordinal

1

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6 December 2019

publication date

1 January 2002

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6 December 2019

published in

Journal of Hepatology

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6 December 2019

volume

36

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6 December 2019

page(s)

123-125

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6 December 2019

issue

1

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N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins

6 December 2019

cites work

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N (epsilon)-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction

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7 January 2021

N epsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins

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Ultrastructure of nonenzymatically glycated mesangial matrix in diabetic nephropathy.

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

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Advanced Maillard reaction end products are associated with Alzheimer disease pathology

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7 January 2021

Advanced glycation end products contribute to amyloidosis in Alzheimer disease

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Lipid advanced glycosylation: pathway for lipid oxidation in vivo

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Markedly elevated levels of plasma advanced glycation end products in patients with liver cirrhosis - amelioration by liver transplantation.

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Increased accumulation of the glycoxidation product N(epsilon)-(carboxymethyl)lysine in human tissues in diabetes and aging.

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Renal fate of circulating advanced glycated end products (AGE): evidence for reabsorption and catabolism of AGE-peptides by renal proximal tubular cells

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7 January 2021

Two novel rat liver membrane proteins that bind advanced glycosylation endproducts: relationship to macrophage receptor for glucose-modified proteins

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7 January 2021

Advanced glycation end products are eliminated by scavenger-receptor-mediated endocytosis in hepatic sinusoidal Kupffer and endothelial cells

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Molecular identity and cellular distribution of advanced glycation endproduct receptors: relationship of p60 to OST-48 and p90 to 80K-H membrane proteins.

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The role of galectin-3 in endocytosis of advanced glycation end products and modified low density lipoproteins

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7 January 2021

Macrophage scavenger receptor mediates the endocytic uptake and degradation of advanced glycation end products of the Maillard reaction

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7 January 2021

A role for macrophage scavenger receptors in atherosclerosis and susceptibility to infection

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7 January 2021

Cd36, a member of the class b scavenger receptor family, as a receptor for advanced glycation end products

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7 January 2021

Scavenger receptor class B type I-mediated reverse cholesterol transport is inhibited by advanced glycation end products

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7 January 2021

Identification of scavenger receptor SR-BI as a high density lipoprotein receptor

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7 January 2021

Endocytic uptake of advanced glycation end products by mouse liver sinusoidal endothelial cells is mediated by a scavenger receptor distinct from the macrophage scavenger receptor class A.

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7 January 2021

Oxidized or acetylated low density lipoproteins are rapidly cleared by the liver in mice with disruption of the scavenger receptor class A type I/II gene

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7 January 2021

Uptake and catabolism of modified LDL in scavenger-receptor class A type I/II knock-out mice.

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7 January 2021

N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression

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7 January 2021

Glycolaldehyde, a reactive intermediate for advanced glycation end products, plays an important role in the generation of an active ligand for the macrophage scavenger receptor

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7 January 2021

In-vitro carboxymethylation of low density lipoprotein alters its metabolism via the high-affinity receptor

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7 January 2021

Formation of plasma advanced glycosylation end products (AGEs) has no influence on plasma viscosity

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7 January 2021

10.1016/S0168-8278(01)00293-8

Identifiers

DOI

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6 December 2019

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