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Journal ArticleDOI

Biological activity of a fragment of insulin

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TLDR
It is shown that a fragment of insulin produced by the action of the insulin-degrading enzyme has both independent biological effects and interactions with insulin, which supports a biologically important effect of insulin metabolism and insulin degradation products on insulin action on non-glucose pathways.
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This article is published in Biochemical and Biophysical Research Communications.The article was published on 2004-06-11. It has received 15 citations till now. The article focuses on the topics: Insulin receptor substrate & Insulin receptor.

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Citations
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Journal ArticleDOI

Macrophage-secreted factors induce adipocyte inflammation and insulin resistance.

TL;DR: Results indicate that macrophage-secreted factors induce inflammatory responses and reduce insulin responsiveness in adipocytes, and may contribute significantly to the systemic inflammation and insulin resistance associated with obesity.
Journal ArticleDOI

Development of a hybrid dextrin hydrogel encapsulating dextrin nanogel as protein delivery system.

TL;DR: The dextrin nanogel allowed the efficient incorporation of interleukin-10 and insulin in the oDex hydrogel, providing a sophisticated system of controlled release, and present promising properties as an injectable carrier of bioactive molecules.
Journal ArticleDOI

The role of copper(II) and zinc(II) in the degradation of human and murine IAPP by insulin-degrading enzyme

TL;DR: The role of the latter metal ions in the degradation of IAPP by insulin-degrading enzyme (IDE) has been investigated by a chromatographic and mass spectrometric combined method and IDE cleavage site preferences in the presence of metal ions are rationalized as metal ion-induced changes in substrate accessibility.
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AP/MALDI-MS complete characterization of the proteolytic fragments produced by the interaction of insulin degrading enzyme with bovine insulin.

TL;DR: A new experimental procedure by which an unambiguous as well as complete assignment of all the peptide fragments generated by the interaction of insulin with IDE is described, and Atmospheric pressure/matrix-assisted laser desorption ionization (AP/MALDI) mass spectra are reported.
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Formation of insulin fragments by insulin-degrading enzyme: the role of zinc(II) and cystine bridges

TL;DR: The role of zinc(II) and cystine bridges in the degradation of insulin by IDE are investigated by high-performance liquid chromatography-mass spectrometry (HPLC-MS), and the experimental conditions at which peculiar insulin fragments having biological activity are formed by the action of IDE are found and discussed.
References
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Journal ArticleDOI

Insulin-degrading enzyme regulates the levels of insulin, amyloid β-protein, and the β-amyloid precursor protein intracellular domain in vivo

TL;DR: In vivo findings suggest that IDE hypofunction may underlie or contribute to some forms of AD and DM2 and provide a mechanism for the recently recognized association among hyperinsulinemia, diabetes, and AD.
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Insulin Degradation: Progress and Potential

TL;DR: Insulin degradation is a regulated process that plays a role in controlling insulin action by removing and inactivating the hormone, and the possibility of a direct intracellular interaction of insulin with IDE that could modulate protein and fat metabolism is raised.
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A futile metabolic cycle activated in adipocytes by antidiabetic agents.

TL;DR: By inducing GyK, TZDs markedly stimulate glycerol incorporation into triglyceride and reduce FFA secretion from adipocytes, contributing to reduced FFA levels and perhaps insulin sensitization by antidiabetic therapies.
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Insulin degradation: mechanisms, products and significance

TL;DR: The roles of receptor binding and internalization in mediating insulin degradation have been clarified, the endosomal pathway for intracellular insulin degradation has been established and the importance of lysosomal degradation questioned.
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Amyloid-β peptide levels in brain are inversely correlated with insulysin activity levels in vivo

TL;DR: In vivo levels of brain Aβ40 and Aβ42 peptides were found to be increased significantly in an insulysin-deficient gene-trap mouse model, indicating that there is an inverse correlation between in vivo insuly sin activity levels and brain A β peptide levels and suggesting that modulation of insulySin activity may alter the risk for Alzheimer's disease.
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