Molecular identity and cellular distribution of advanced glycation endproduct receptors: relationship of p60 to OST-48 and p90 to 80K-H membrane proteins
| Autor: | Yong Ming Li, Helen Vlassara, Jenny Li, Deben Banerjee, Alan W. Stitt, Tomoko Mitsuhashi, Cijiang He, Nobuyoshi Shimizu, Donald Wojciechowicz |
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| Rok vydání: | 1996 |
| Předmět: |
Glycation End Products
Advanced Male Molecular Sequence Data Receptor for Advanced Glycation End Products Biology Cell Line Rats Sprague-Dawley Cell membrane Mice Transferases Glycation Calcium-binding protein medicine Animals Humans Amino Acid Sequence Receptors Immunologic Fluorescent Antibody Technique Indirect Myristoylated Alanine-Rich C Kinase Substrate Receptor Multidisciplinary Sequence Homology Amino Acid Endoplasmic reticulum Calcium-Binding Proteins Cell Membrane Intracellular Signaling Peptides and Proteins Membrane Proteins Phosphoproteins Rats medicine.anatomical_structure Hexosyltransferases Membrane protein Biochemistry Oligosaccharyltransferase complex Microsome Endoplasmic Reticulum Rough Sequence Alignment Glucosidases Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 93:11047-11052 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.93.20.11047 |
| Popis: | Advanced glycation endproducts (AGEs) are derivatives of nonenzymatic reactions between sugars and protein or lipids, and together with AGE-specific receptors are involved in numerous pathogenic processes associated with aging and hyperglycemia. Two of the known AGE-binding proteins isolated from rat liver membranes, p60 and p90, have been partially sequenced. We now report that the N-terminal sequence of p60 exhibits 95% identity to OST-48, a 48-kDa member of the oligosaccharyltransferase complex found in microsomal membranes, while sequence analysis of p90 revealed 73% and 85% identity to the N-terminal and internal sequences, respectively, of human 80K-H, a 80- to 87-kDa protein substrate for protein kinase C. AGE-ligand and Western analyses of purified oligosaccharyltransferase complex, enriched rough endoplasmic reticulum, smooth endoplasmic reticulum, and plasma membranes from rat liver or RAW 264.7 macrophages yielded a single protein of approximately 50 kDa recognized by both anti-p60 and anti-OST-48 antibodies, and also exhibited AGE-specific binding. Immunoprecipitated OST-48 from rat rough endoplasmic reticulum fractions exhibited both AGE binding and immunoreactivity to an anti-p60 antibody. Immune IgG raised to recombinant OST-48 and 80K-H inhibited binding of AGE-bovine serum albumin to cell membranes in a dose-dependent manner. Immunostaining and flow cytometry demonstrated the surface expression of OST-48 and 80K-H on numerous cell types and tissues, including mononuclear, endothelial, renal, and brain neuronal and glial cells. We conclude that the AGE receptor components p60 and p90 are identical to OST-48, and 80K-H, respectively, and that they together contribute to the processing of AGEs from extra- and intracellular compartments and in the cellular responses associated with these pathogenic substances. |
| Databáze: | OpenAIRE |
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