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- W89287583 abstract "Summary It has been suggested that N ɛ -(carboxymethyl)lysine (CML), the major product of oxidative degradation of glycated proteins represents an integrative marker of oxidative stress in aging, arteriosclerosis and diabetes. Our previous immunohistochemical analysis using a CML-specific antiserum provided evidence for an age-and diabetes-dependent increase in CML-accumulation in the extracellular matrix. Intracellular accumulation of CML was found in macrophages and foam cells of arteriosclerotic plaques. In this study we immunohistochemically investigated the occurrence of CML in normal intestinal tissues. Furthermore, we analysed the immunolocalization of CML in chronically inflamed intestinal tissues (inflammation associated with M. Crohn or colitis ulcerosa) as a “model system” for a chronic inflammatory process. In these lesions we found widespread, intense, positive CML-staining in the macrophages. However, since in the normal intestinal wall we observed also positively labelled macrophages, it appears that exogenous CML uptake and phagocytosis in macrophages, e.g. from diet, may contribute to this staining. Furthermore, the formation of CML was studied in vitro to elucitate the origin of the unexpectedly high extent of intracellular CML. We found that CML was more rapidly formed from arachidonic acid than from glycated HSA. In summary, our observations provide strong evidence that CML-modified proteins may be formed by both, glycoxidation and lipid peroxidation, i.e., in situations of enhanced oxidative stress and that the CML-content of intestinal cells may result from phagocytosed AGE-modified proteins of endo-or exogenous origin." @default.
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- W89287583 date "2005-01-01" @default.
- W89287583 modified "2023-09-24" @default.
- W89287583 title "Immunolocalization of the Glycoxidation Product N ɛ -(carboxymethyl) Lysine in Normal and Inflamed Human Intestinal Tissues" @default.
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- W89287583 doi "https://doi.org/10.1533/9781845698447.7.316" @default.
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