The liver cell histones of diabetic patients contain glycation endproducts (AGEs) which may be lipofuscin components

Jobst, K; Lakatos, Ágnes

doi:10.1016/s0009-8981(96)06419-4

Cited by 15 publications

(11 citation statements)

References 4 publications

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“…However, more intense accumulation in STZ-induced diabetic rats compared with age-matched control rats was seen for CEL and fluorolink in hepatocytes; 2A2-positive AGE antigen in splenic macrophages; CML, CEL, and fluorolink in renal glomerular endothelial and mesangial cells; CML and CEL in testicular Leydig cells; and CML, fluorolink, and 2A2-positive AGE antigen in erythrocytes. These results suggest that marked accumulation of AGE in these tissues and cells is responsible for the characteristic histopathologic changes of diabetes mellitus, in agreement with findings reported previously (Jobst and Lakatos, 1996;Orth et al, 1979;Paz and Homonnai, 1979;Vlassara et al, 1994;Wautier et al, 1994).…”

Section: Ling Et Alsupporting

confidence: 93%

“…In the present study, AGE accumulated in hepatocytes, accompanied by accumulation of lipofuscin pigments. In the liver of diabetic patients, histones contain AGE, which might be lipofuscin pigments (Jobst and Lakatos, 1996). Studies reported that STZ-induced diabetic rats are infertile, presumably because of decreased testicular Leydig cell function and altered Leydig cell components (Paz and Homonnai, 1979;Orth et al, 1979).…”

Section: Ling Et Almentioning

confidence: 99%

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Immunohistochemical Distribution and Quantitative Biochemical Detection of Advanced Glycation End Products in Fetal to Adult Rats and in Rats with Streptozotocin-Induced Diabetes

Xia

Nagai

Sakashita

et al. 2001

Laboratory Investigation

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SUMMARY:We used immunohistochemical methods and four monoclonal antibodies for specific molecular structures of advanced glycation end products (AGE)-6D12, KNH-30, 1F6, and 2A2-to examine localization of AGE in fetal, young, and adult rats, and rats with streptozotocin-induced diabetes. 6D12 recognized N ⑀ -(carboxymethyl)lysine (CML); KNH-30, N ⑀ -(carboxyethyl)lysine (CEL); and 1F6, fluorolink. The epitope of 2A2 is as yet unknown. Immunoreactivities for these monoclonal antibodies were found in various organs and tissues in postnatal and adult rats, and accumulation increased with aging. In the fetuses, AGE structures were detected at 10 fetal days, and their accumulation increased during ontogeny. Reversed-phase high-performance liquid chromatography revealed CML in fetuses at 13 fetal days and in lungs of 28-week-old rats. In various organs and tissues of fetal, young, and adult rats, CML, CEL, 2A2-positive AGE, and fluorolink accumulated, in that order, which suggests that the accumulation of CML, a nonfluorescent/noncross-linked AGE, occurs earlier than accumulation of fluorolink, a fluorescent/cross-linked AGE. In diabetic rats, hepatocytes, splenic macrophages, renal glomerular endothelial and mesangial cells, testicular Leydig cells, and erythrocytes showed excessive accumulation of AGE, leading to the pathologic changes characteristic of diabetes mellitus. For the induction of these changes, persistent hyperglycemia and hyperketonemia might be important for acceleration of intracellular AGE accumulation in diabetic rats. Thus, AGE accumulation in tissues and cells occurs not only during aging and in diabetes mellitus but also from an early stage of ontogeny. (Lab Invest 2001, 81:845-861).

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Section: Ling Et Alsupporting

confidence: 93%

Section: Ling Et Almentioning

confidence: 99%

Immunohistochemical Distribution and Quantitative Biochemical Detection of Advanced Glycation End Products in Fetal to Adult Rats and in Rats with Streptozotocin-Induced Diabetes

Xia

Nagai

Sakashita

et al. 2001

Laboratory Investigation

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“…Interference with ascorbate uptake by hyperglycemia would result in increased production of melanins such as lipofuscins due to polymerization of catecholamine metabolites (Dillon & Root-Bernstein, 2000;Root-Bernstein & Dillon, 1997;Hegedus, 2000;Kameyam et al, 1996;Hegedus & Nayak, 1994;Pawelek & Lerner, 1978). It is suspected that lipofuscins may be a key component in glycation endproducts (AGEs) (Jobst & Lakatos, 1996), which have been associated with diabetic pathologies (Hammes et al, 1991). Indeed, many oxidative intermediates in the conversion of catcholamines into melanins are known to be cytopathic (Kameyam et al, 1996;Hegedus & Nayak, 1994;Pawelek & Lerner, 1978).…”

Section: Clinical Consequences Of the Hypothesismentioning

confidence: 99%

Are Diabetic Neuropathy, Retinopathy and Nephropathy Caused by Hyperglycemic Exclusion of Dehydroascorbate Uptake by Glucose Transporters?

Root‐Bernstein

Busik

Henry

2002

Journal of Theoretical Biology

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“…Amadori-and AGE-modified histones were detected in liver cells of diabetic patients [29,30] whereas a number of Amadori-modified plasma proteins (viz. immunoglobulin heavy-chain constant regions) have been identified in type 2 diabetic patients [28].…”

Section: Glycated Lysine-rich Proteins and Their Involvement In Age-rmentioning

confidence: 99%

Glycated Lysine Residues: A Marker for Non-Enzymatic Protein Glycation in Age-Related Diseases

2011

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Abstract.Nonenzymatic glycosylation or glycation of macromolecules, especially proteins leading to their oxidation, play an important role in diseases. Glycation of proteins primarily results in the formation of an early stage and stable Amadori-lysine product which undergo further irreversible chemical reactions to form advanced glycation endproducts (AGEs). This review focuses these products in lysine rich proteins such as collagen and human serum albumin for their role in aging and age-related diseases. Antigenic characteristics of glycated lysine residues in proteins together with the presence of serum autoantibodies to the glycated lysine products and lysine-rich proteins in diabetes and arthritis patients indicates that these modified lysine residues may be a novel biomarker for protein glycation in aging and age-related diseases.

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The liver cell histones of diabetic patients contain glycation endproducts (AGEs) which may be lipofuscin components

Cited by 15 publications

References 4 publications

Immunohistochemical Distribution and Quantitative Biochemical Detection of Advanced Glycation End Products in Fetal to Adult Rats and in Rats with Streptozotocin-Induced Diabetes

Immunohistochemical Distribution and Quantitative Biochemical Detection of Advanced Glycation End Products in Fetal to Adult Rats and in Rats with Streptozotocin-Induced Diabetes

Are Diabetic Neuropathy, Retinopathy and Nephropathy Caused by Hyperglycemic Exclusion of Dehydroascorbate Uptake by Glucose Transporters?

Glycated Lysine Residues: A Marker for Non-Enzymatic Protein Glycation in Age-Related Diseases

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