Glycomics investigation into insulin action.

Defects in glycosylation are becoming increasingly associated with a range of human diseases. In some cases, the disease is caused by the glycosylation defect, whereas in others, the aberrant glycosylation may be a consequence of the disease. The implementation of highly sensitive and rapid mass spe...

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Những tác giả chính: Parry, S, Hadaschik, D, Blancher, C, Kumaran, M, Bochkina, N, Morris, H, Richardson, S, Aitman, T, Gauguier, D, Siddle, K, Scott, J, Dell, A
Định dạng: Journal article
Ngôn ngữ:English
Được phát hành: 2006
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author Parry, S
Hadaschik, D
Blancher, C
Kumaran, M
Bochkina, N
Morris, H
Richardson, S
Aitman, T
Gauguier, D
Siddle, K
Scott, J
Dell, A
author_facet Parry, S
Hadaschik, D
Blancher, C
Kumaran, M
Bochkina, N
Morris, H
Richardson, S
Aitman, T
Gauguier, D
Siddle, K
Scott, J
Dell, A
author_sort Parry, S
collection OXFORD
description Defects in glycosylation are becoming increasingly associated with a range of human diseases. In some cases, the disease is caused by the glycosylation defect, whereas in others, the aberrant glycosylation may be a consequence of the disease. The implementation of highly sensitive and rapid mass spectrometric screening strategies for profiling the glycans present in model biological systems is revealing valuable insights into disease phenotypes. In addition, glycan screening is proving useful in the analysis of knock-out mice where it is possible to assess the role of glycosyltransferases and glycosidases and what function they have at the cellular and whole organism level. In this study, we analysed the effect of insulin on the glycosylation of 3T3-L1 cells and the effect of insulin resistance on glycosylation in a mouse model. Transcription profiling of 3T3-L1 cells treated with and without insulin revealed expression changes of several glycogenes. In contrast, mass spectrometric screening analysis of the glycans from these cells revealed very similar profiles suggesting that any changes in glycosylation were most likely on specific proteins rather than a global phenomenon. A fat-fed versus carbohydrate-fed mouse insulin resistant model was analysed to test the consequences of chronic insulin resistance. Muscle and liver N-glycosylation profiles from these mice are reported.
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spelling oxford-uuid:f486b51c-62f5-423f-a3e2-da7798ef4dec2022-03-27T12:20:28ZGlycomics investigation into insulin action.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f486b51c-62f5-423f-a3e2-da7798ef4decEnglishSymplectic Elements at Oxford2006Parry, SHadaschik, DBlancher, CKumaran, MBochkina, NMorris, HRichardson, SAitman, TGauguier, DSiddle, KScott, JDell, ADefects in glycosylation are becoming increasingly associated with a range of human diseases. In some cases, the disease is caused by the glycosylation defect, whereas in others, the aberrant glycosylation may be a consequence of the disease. The implementation of highly sensitive and rapid mass spectrometric screening strategies for profiling the glycans present in model biological systems is revealing valuable insights into disease phenotypes. In addition, glycan screening is proving useful in the analysis of knock-out mice where it is possible to assess the role of glycosyltransferases and glycosidases and what function they have at the cellular and whole organism level. In this study, we analysed the effect of insulin on the glycosylation of 3T3-L1 cells and the effect of insulin resistance on glycosylation in a mouse model. Transcription profiling of 3T3-L1 cells treated with and without insulin revealed expression changes of several glycogenes. In contrast, mass spectrometric screening analysis of the glycans from these cells revealed very similar profiles suggesting that any changes in glycosylation were most likely on specific proteins rather than a global phenomenon. A fat-fed versus carbohydrate-fed mouse insulin resistant model was analysed to test the consequences of chronic insulin resistance. Muscle and liver N-glycosylation profiles from these mice are reported.
spellingShingle Parry, S
Hadaschik, D
Blancher, C
Kumaran, M
Bochkina, N
Morris, H
Richardson, S
Aitman, T
Gauguier, D
Siddle, K
Scott, J
Dell, A
Glycomics investigation into insulin action.
title Glycomics investigation into insulin action.
title_full Glycomics investigation into insulin action.
title_fullStr Glycomics investigation into insulin action.
title_full_unstemmed Glycomics investigation into insulin action.
title_short Glycomics investigation into insulin action.
title_sort glycomics investigation into insulin action
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