Sandbox Reserved 381: Difference between revisions

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== OGT ~~mediated~~ Disease ==

== OGT Mediated Disease ==

Faulty regulation of O-GlcNAc midifications has been suggested to be involved in neurodegenerative diseases, diabetes mellitus and cancer. Biochemical details of these processes are still unclear.<ref>PMID:16051707</ref> Proteins modified by O-GlcNAc have been directly shown to have a role in the pathology of human diseases. For instance, the Ser/The kinase AKT,PI(3)K,insulin receptor substrate 1, glycogen synthase and endothelial nitric oxide synthase,all of which are enzymes that have a crucial role in insulin signalling,are reversibly modified by OGT. A recent study showed thate recruitment of OGT to the plasma membrane specifically prevents the phosphorylation of AKT and possibly other proteins, thereby terminating insulin signalling.<ref>PMID:18288188</ref> This adds evidence to the view that increasing the level of O-GlcNAc modifications correlates with the development of insulin resistance, which is a characteristic of type II diabetes.<ref>PMID:16317114</ref><ref>PMID:16781888</ref> Some indications suggest that O-GlcNAc modifications have a role in Alzheimer disease. Higher levels of O-GlcNAc can be detected in the brain tissue and several proteins involved in neuronal signalling are modified with O-GlcNAc. Among them are the B-anyloid precursor protein, clathrin-assembly proteins and neurofilaments. In the brains of patients with Alzheimer disease, hyperphosphorylated Tau protein was modified by O-GlcNAc to a lesser extent than in healthy individuals.<ref>PMID:17940659</ref> Studies have shown that some oncogenes and tumour suppressors are targets of O-glycosylation, including the SV40 T antigen and c-MYC.<ref>PMID:14533811</ref> Tumour cells have an altered glucose metabolism that is expected to produce changes in O-GlcNAc levels and to affect different signalling pathways.

Sandbox Reserved 381: Difference between revisions

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Revision as of 18:26, 25 November 2011 view source Sheri Marcum (talk \| contribs) 81 edits No edit summary ← Older edit		Revision as of 18:28, 25 November 2011 view source Sheri Marcum (talk \| contribs) 81 edits →OGT mediated Disease Newer edit →
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	== OGT ~~mediated~~ Disease ==		== OGT Mediated Disease ==
	Faulty regulation of O-GlcNAc midifications has been suggested to be involved in neurodegenerative diseases, diabetes mellitus and cancer. Biochemical details of these processes are still unclear.<ref>PMID:16051707</ref> Proteins modified by O-GlcNAc have been directly shown to have a role in the pathology of human diseases. For instance, the Ser/The kinase AKT,PI(3)K,insulin receptor substrate 1, glycogen synthase and endothelial nitric oxide synthase,all of which are enzymes that have a crucial role in insulin signalling,are reversibly modified by OGT. A recent study showed thate recruitment of OGT to the plasma membrane specifically prevents the phosphorylation of AKT and possibly other proteins, thereby terminating insulin signalling.<ref>PMID:18288188</ref> This adds evidence to the view that increasing the level of O-GlcNAc modifications correlates with the development of insulin resistance, which is a characteristic of type II diabetes.<ref>PMID:16317114</ref><ref>PMID:16781888</ref> Some indications suggest that O-GlcNAc modifications have a role in Alzheimer disease. Higher levels of O-GlcNAc can be detected in the brain tissue and several proteins involved in neuronal signalling are modified with O-GlcNAc. Among them are the B-anyloid precursor protein, clathrin-assembly proteins and neurofilaments. In the brains of patients with Alzheimer disease, hyperphosphorylated Tau protein was modified by O-GlcNAc to a lesser extent than in healthy individuals.<ref>PMID:17940659</ref> Studies have shown that some oncogenes and tumour suppressors are targets of O-glycosylation, including the SV40 T antigen and c-MYC.<ref>PMID:14533811</ref> Tumour cells have an altered glucose metabolism that is expected to produce changes in O-GlcNAc levels and to affect different signalling pathways.		Faulty regulation of O-GlcNAc midifications has been suggested to be involved in neurodegenerative diseases, diabetes mellitus and cancer. Biochemical details of these processes are still unclear.<ref>PMID:16051707</ref> Proteins modified by O-GlcNAc have been directly shown to have a role in the pathology of human diseases. For instance, the Ser/The kinase AKT,PI(3)K,insulin receptor substrate 1, glycogen synthase and endothelial nitric oxide synthase,all of which are enzymes that have a crucial role in insulin signalling,are reversibly modified by OGT. A recent study showed thate recruitment of OGT to the plasma membrane specifically prevents the phosphorylation of AKT and possibly other proteins, thereby terminating insulin signalling.<ref>PMID:18288188</ref> This adds evidence to the view that increasing the level of O-GlcNAc modifications correlates with the development of insulin resistance, which is a characteristic of type II diabetes.<ref>PMID:16317114</ref><ref>PMID:16781888</ref> Some indications suggest that O-GlcNAc modifications have a role in Alzheimer disease. Higher levels of O-GlcNAc can be detected in the brain tissue and several proteins involved in neuronal signalling are modified with O-GlcNAc. Among them are the B-anyloid precursor protein, clathrin-assembly proteins and neurofilaments. In the brains of patients with Alzheimer disease, hyperphosphorylated Tau protein was modified by O-GlcNAc to a lesser extent than in healthy individuals.<ref>PMID:17940659</ref> Studies have shown that some oncogenes and tumour suppressors are targets of O-glycosylation, including the SV40 T antigen and c-MYC.<ref>PMID:14533811</ref> Tumour cells have an altered glucose metabolism that is expected to produce changes in O-GlcNAc levels and to affect different signalling pathways.