| N-glycans in cell survival and death: cross-talk between glycosyltransferases. | |
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MedLine Citation:
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PMID: 22326428 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Asparagine-linked (N-linked) protein glycosylation is one of the most important protein modifications. N-glycans with "high mannose", "hybrid", or "complex" type sugar chains participate in a multitude of cellular processes. These include cell-cell/cell-matrix/receptor-ligand interaction, cell signaling/growth and differentiation, to name a few. Many diseases such as disorders of blood clotting, congenital disorder of glycosylation, diseases of blood vessels, cancer, neo-vascularization, i.e., angiogenesis essential for breast and other solid tumor progression and metastasis are associated with N-glycan expression. Biosynthesis of N-glycans requires multiple steps and multiple cellular compartments. Following transcription and translation the proteins migrate to the endoplasmic reticulum (ER) lumen to acquire glycan chain(s) with a defined glycoform, i.e., a tetradecasaccharide. These are further modified, i.e., edited in ER lumen and in Golgi prior to moving to their respective destinations. The tetradecasaccharide is pre-assembled on a poly-isoprenoid lipid called dolichol, and becomes an essential component of the supply chain. Therefore, dolichol cycle synthesizing the lipid-linked oligosaccharide (LLO) is a hallmark for all N-linked glycoproteins. It is expected that there is a great deal of cross-talk between the participating glycosyltransferases and any missed step would express defective N-glycans that could have fatal consequences. The positive impact of the structurally altered N-glycans could lead to discovery of an N-glycan signature for a disease and/or help developing glycotherapeutic treating cancer or other human diseases. The purpose of this review is to identify the gaps of N-glycan biology and help developing appropriate technology for biomedical applications. This article is part of a Special Issue entitled Glycoproteomics. |
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Authors:
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Dipak K Banerjee |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review Date: 2012-02-03 |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1820 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 2012 Sep |
Date Detail:
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Created Date: 2012-06-25 Completed Date: 2013-03-07 Revised Date: 2013-04-16 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: Netherlands |
Other Details:
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Languages: eng Pagination: 1338-46 Citation Subset: IM |
Copyright Information:
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Copyright © 2012 Elsevier B.V. All rights reserved. |
Affiliation:
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Department of Biochemistry, School of Medicine, University of Puerto Rico, Medical Sciences Campus, San Juan, PR 00936-5067. dipak.banerjee@upr.edu |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Death Cell Proliferation Cell Survival Glycoproteins / biosynthesis, metabolism* Glycosyltransferases / metabolism*, physiology Humans Metabolic Networks and Pathways / physiology Polysaccharides / metabolism*, physiology* |
| Grant Support | |
ID/Acronym/Agency:
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U54-CA096297/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Glycoproteins; 0/Polysaccharides; EC 2.4.-/Glycosyltransferases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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