Studies on the insulinomimetic effects of benzylamine, exogenous substrate of semicarbazide-sensitive amine oxidase enzyme in streptozotocin induced diabetic rats
Semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 (SSAO) is believed to be a bifunctional membrane protein. It is localized extracellularly and preferentially oxidizes short chain primary amines to aldehydes, hydrogen peroxide and ammonia, but also functions as an adhesion molecule,...
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Published in: | Journal of Neural Transmission Vol. 114; no. 6; pp. 851 - 855 |
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Main Authors: | , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Austria
Springer Nature B.V
01-06-2007
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Subjects: | |
Online Access: | Get full text |
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Summary: | Semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 (SSAO) is believed to be a bifunctional membrane protein. It is localized extracellularly and preferentially oxidizes short chain primary amines to aldehydes, hydrogen peroxide and ammonia, but also functions as an adhesion molecule, which is involved in leukocyte migration. Serum SSAO activity is increased in diabetic patients and animals and the aldehydes formed in the enzyme reaction may contribute to vascular damage. However, administration of exogenous substrates has been shown to improve glucose tolerance and reduce hyperglycaemia in diabetic animals. Hydrogen peroxide and/or its vanadate complexes have been suggested responsible for these effects. Streptozotocin induced diabetic rats were treated with benzylamine (BZA) +/- vanadate (V) or insulin. In contrast to insulin, BZA + V treatment did not reduce HbA(1C) levels. However, it reduced the elevated serum SSAO activity, decreased the accumulation of advanced-glycation end products and increased the bioavailability of nitric oxide in diabetic animals, similarly to insulin. BZA alone did not affect any of these parameters. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0300-9564 1435-1463 |
DOI: | 10.1007/s00702-007-0700-1 |