Chemical modification of muscle protein in diabetes
| Autor: | Suzanne R. Thorpe, Nadja Alt, N. L. Alderson, James A. Carson, Ryoji Nagai, Thomas Henle, John W. Baynes, Yuping Wang |
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| Rok vydání: | 2004 |
| Předmět: |
Glycation End Products
Advanced medicine.medical_specialty Lysine Biophysics Muscle Proteins macromolecular substances Biochemistry Streptozocin Diabetes Mellitus Experimental Rats Sprague-Dawley Lipid peroxidation chemistry.chemical_compound symbols.namesake Glycation Internal medicine Diabetes mellitus medicine Animals Muscle Skeletal Molecular Biology Skin medicine.disease Rats Maillard reaction Endocrinology chemistry symbols Advanced glycation end-product Collagen Lipid Peroxidation Myofibril Cysteine |
| Zdroj: | Archives of Biochemistry and Biophysics. 425:200-206 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/j.abb.2004.03.012 |
| Popis: | Levels of glycation (fructose-lysine, FL) and advanced glycoxidation and lipoxidation end-products (AGE/ALEs) were measured in total skeletal (gastrocnemius) muscle and myofibril protein and compared to levels of the same compounds in insoluble skin collagen of control and diabetic rats. Levels of FL in total muscle and myofibril protein were 3-5% the level of FL in skin collagen. The AGE/ALEs, N(epsilon)-(carboxymethyl)lysine (CML) and N(epsilon)-(carboxyethyl)lysine, were also significantly lower in total muscle and myofibril protein, approximately 25% of levels in skin collagen. The newly described sulfhydryl AGE/ALE, S-(carboxymethyl)cysteine (CMC), was also measured in muscle; levels of CMC were comparable to those of CML and increased similarly in response to diabetes. Although FL and AGE/ALEs increased in muscle protein in diabetes, the relative increase was less than that seen in skin collagen. These data indicate that muscle protein is partially protected against the increase in both glycation and AGE/ALE formation in diabetes. |
| Databáze: | OpenAIRE |
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