Processing Advanced Glycation End Product-Modified Albumin by the Renal Proximal Tubule and the Early Pathogenesis of Diabetic Nephropathy
| Autor: | Miriam F. Weiss, Aylin M. Ozdemir, Vincent M. Monnier, Ulrich Hopfer, Penny Erhard |
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| Rok vydání: | 2005 |
| Předmět: |
Glycation End Products
Advanced medicine.medical_specialty Glomerulus (kidney) General Biochemistry Genetics and Molecular Biology Nephropathy Kidney Tubules Proximal Pathogenesis Diabetic nephropathy chemistry.chemical_compound History and Philosophy of Science Glycation Diabetes mellitus Internal medicine Acetylglucosaminidase medicine Albuminuria Humans Diabetic Nephropathies Cells Cultured Serum Albumin General Neuroscience Albumin Serum Albumin Bovine medicine.disease Culture Media Diabetes Mellitus Type 1 medicine.anatomical_structure Endocrinology chemistry Advanced glycation end-product Fluorescein-5-isothiocyanate |
| Zdroj: | Annals of the New York Academy of Sciences. 1043:625-636 |
| ISSN: | 0077-8923 |
| DOI: | 10.1196/annals.1338.071 |
| Popis: | Diabetes is characterized by increased quantities of circulating proteins modified by advanced glycation end products (AGEs). Proteins filtered at the glomerulus and presented to the renal proximal tubule are likely to be highly modified by AGEs. The proximal tubule binds, takes up, and catabolizes AGE-modified albumin by pathways different from those of unmodified albumin. These differences were examined in polarized, electrically resistant proximal tubular cells grown in monolayer culture. In patients with type 1 diabetes, urinary excretion of a lysosomal enzyme predicted the development of nephropathy. |
| Databáze: | OpenAIRE |
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