Cytochemistry of circulating lymphocytes in diabetes mellitus with and without retinopathy and in newly diagnosed type I (insulin dependent) diabetes

Solerte, Sebastiano Bruno; Invernizzi, Rosangela; Fioravanti, Marisa; Schianca, Giampiero Carnevale; Bozzetti, Anna; Girino, Margherita; Bertolino, Giampiera; Ferrari, Ettore

doi:10.1016/s0065-1281(86)80067-8

Acta Histochemica

1986

DOI: 10.1016/s0065-1281(86)80067-8

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Cytochemistry of circulating lymphocytes in diabetes mellitus with and without retinopathy and in newly diagnosed type I (insulin dependent) diabetes

Sebastiano Bruno Solerte

Rosangela Invernizzi

Marisa Fioravanti

et al.

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Cited by 4 publications

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“…Esterase has been identified in normal human lens (Swanson and Truesdale, 1974), and partially purified into two fractions (Kamei, 1996). The activity of esterase was decreased in diabetic patients and in experimental diabetic rats (Agarwal et al, 1985;Aoyagi et al, 1985;Mayfield et al, 1985;Solerte et al, 1986). The activity of esterase was decreased in diabetic patients and in experimental diabetic rats (Agarwal et al, 1985;Aoyagi et al, 1985;Mayfield et al, 1985;Solerte et al, 1986).…”

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confidence: 99%

The Molecular Chaperone, α-Crystallin, Protects against Loss of Antigenicity and Activity of Esterase Caused by Sugars, Sugar Phosphate and a Steroid

Zhang

Harding²

2003

Biological Chemistry

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Previously we showed that glycation-induced inactivation and loss of antigenicity of enzymes occur simultaneously. Alpha-crystallin, a major structural protein of the mammalian lens, prevents the aggregation of other proteins and protects enzyme function against post-translational modification in vitro. However, it is not known whether alpha-crystallin can also protect against loss of antigenicity of enzymes. Esterase activity in the lens is decreased in senile cataract and diabetes. We investigated the loss of antigenicity of esterase caused by different insults and the ability of alpha-crystallin to protect. Inactivation of carboxylesterase by sugars, fructose 6-phosphate (F6P) and a steroid, prednisolone-21-hemisuccinate (P-21-H), was measured spectrophotometrically in the presence and absence of alpha-crystallin, while loss of antigenicity was monitored simultaneously using an immunoprecipitation method. The esterase was progressively inactivated by fructose, F6P, ribose, and P-21-H. Bovine alpha-crystallin fully protected against inactivation of esterase by all four compounds, and also protected against loss of antigenicity of the esterase by fructose, ribose and P-21-H at a molar ratio of 1:1. The results indicated that alpha-crystallin, under our experimental conditions, clearly exhibited the ability to prevent loss of antigenicity and inactivation of esterase. The protective effect of alpha-crystallin against loss of antigenicity indicates a novel aspect of its chaperoning function.

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mentioning

confidence: 99%

The Molecular Chaperone, α-Crystallin, Protects against Loss of Antigenicity and Activity of Esterase Caused by Sugars, Sugar Phosphate and a Steroid

Zhang

Harding²

2003

Biological Chemistry

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Immunological aspects of diabetes mellitus: Prospects for pharmacological modification

Itoh¹

1989

Pharmacology & Therapeutics

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Carnosine protects against the inactivation of esterase induced by glycation and a steroid

Zhang

Harding

2005

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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Carnosine, an endogenous histidine-containing dipeptide, protects protein from oxidation and glycation, which may contribute to a potential treatment for some conformational diseases including cataract. Glycation, the non-enzymic reaction of sugars with proteins, promotes cross-linking and further aggregation. Prolonged use of glucocorticoids is a risk factor for cataract, as is diabetes. Esterase activity in the lens is decreased in senile cataract and diabetes. Previously, we reported that glycation and a steroid inactivate esterase. Here we tested the inactivation of esterase with fructose, fructose 6-phosphate (F6P) and ribose as model glycation reactions and prednisolone-21-hemisuccinate (P-21-H) as a model steroid and investigated the ability of carnosine to protect esterase against inactivation. The activity of esterase was measured by a spectrophotometric assay using p-nitrophenyl acetate as the substrate. The modified esterase was examined electrophoretically. The esterase was progressively inactivated by F6P, fructose, ribose and P-21-H. P-21-H was more effective than the sugars. Carnosine significantly inhibited the inactivation of esterase induced by all four compounds. Carnosine decreased the extent of the cross-linking. These results provide further evidence for carnosine's role as an anti-glycation compound. It is also proposed that carnosine may be an anti-steroid agent.

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Cytochemistry of circulating lymphocytes in diabetes mellitus with and without retinopathy and in newly diagnosed type I (insulin dependent) diabetes

Cited by 4 publications

References 26 publications

The Molecular Chaperone, α-Crystallin, Protects against Loss of Antigenicity and Activity of Esterase Caused by Sugars, Sugar Phosphate and a Steroid

The Molecular Chaperone, α-Crystallin, Protects against Loss of Antigenicity and Activity of Esterase Caused by Sugars, Sugar Phosphate and a Steroid

Immunological aspects of diabetes mellitus: Prospects for pharmacological modification

Carnosine protects against the inactivation of esterase induced by glycation and a steroid

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