Study of the antidiabetic action of cinnamon extract on cell culture of 3T3-Li adipocytes

Insulin binds to the extracellular -subunit of the insulin receptor, and induces a conformational change in the kinase domain of the trans membrane β-subunit resulting in activation of insulin receptor tyrosine kinase, an essential step for the downstream insulin signalling events. In type 2 dia...

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Main Author: Sarmidi, Mohamad Roji
Format: Monograph
Language:English
Published: Universiti Teknologi Malaysia 2005
Subjects:
Online Access:http://eprints.utm.my/2797/
http://eprints.utm.my/2797/1/75091.pdf
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author Sarmidi, Mohamad Roji
author_facet Sarmidi, Mohamad Roji
author_sort Sarmidi, Mohamad Roji
building UTeM Institutional Repository
collection Online Access
description Insulin binds to the extracellular -subunit of the insulin receptor, and induces a conformational change in the kinase domain of the trans membrane β-subunit resulting in activation of insulin receptor tyrosine kinase, an essential step for the downstream insulin signalling events. In type 2 diabetes, part of the insulin resistance is due to inability of insulin to activate the receptor kinase activity. The activity of cinnamtannin B1 on phosphorylation of insulin receptor was analyzed using western blot technique. Cnnnamtannin B 1 stimulated phosphorylation of insulin receptor β-subunit. There was no phosphorylation of insulin receptor observed in 3T3-L1 preadipocytes. The activity of cinnamtannin B1 in stimulating phosphorylation was inhibited by wortmannin and cytochalasin B. In contrast, sodium orthovanadate stimulated phosphorylation of insulin receptor.
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publishDate 2005
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spelling utm-27972010-06-01T03:05:14Z http://eprints.utm.my/2797/ Study of the antidiabetic action of cinnamon extract on cell culture of 3T3-Li adipocytes Sarmidi, Mohamad Roji TP Chemical technology Insulin binds to the extracellular -subunit of the insulin receptor, and induces a conformational change in the kinase domain of the trans membrane β-subunit resulting in activation of insulin receptor tyrosine kinase, an essential step for the downstream insulin signalling events. In type 2 diabetes, part of the insulin resistance is due to inability of insulin to activate the receptor kinase activity. The activity of cinnamtannin B1 on phosphorylation of insulin receptor was analyzed using western blot technique. Cnnnamtannin B 1 stimulated phosphorylation of insulin receptor β-subunit. There was no phosphorylation of insulin receptor observed in 3T3-L1 preadipocytes. The activity of cinnamtannin B1 in stimulating phosphorylation was inhibited by wortmannin and cytochalasin B. In contrast, sodium orthovanadate stimulated phosphorylation of insulin receptor. Universiti Teknologi Malaysia 2005-03-31 Monograph NonPeerReviewed application/pdf en http://eprints.utm.my/2797/1/75091.pdf Sarmidi, Mohamad Roji (2005) Study of the antidiabetic action of cinnamon extract on cell culture of 3T3-Li adipocytes. Project Report. Universiti Teknologi Malaysia. (Unpublished)
spellingShingle TP Chemical technology
Sarmidi, Mohamad Roji
Study of the antidiabetic action of cinnamon extract on cell culture of 3T3-Li adipocytes
title Study of the antidiabetic action of cinnamon extract on cell culture of 3T3-Li adipocytes
title_full Study of the antidiabetic action of cinnamon extract on cell culture of 3T3-Li adipocytes
title_fullStr Study of the antidiabetic action of cinnamon extract on cell culture of 3T3-Li adipocytes
title_full_unstemmed Study of the antidiabetic action of cinnamon extract on cell culture of 3T3-Li adipocytes
title_short Study of the antidiabetic action of cinnamon extract on cell culture of 3T3-Li adipocytes
title_sort study of the antidiabetic action of cinnamon extract on cell culture of 3t3-li adipocytes
topic TP Chemical technology
url http://eprints.utm.my/2797/
http://eprints.utm.my/2797/1/75091.pdf