Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-4
|
| pubmed:dateCreated |
1998-11-25
|
| pubmed:abstractText |
Glycoproteins are proteins that carry N- and O-glycosidically-linked carbohydrate chains of complex structures and functions. N-glycan chains are assembled in the endoplasmic reticulum and the Golgi by a controlled sequence of glycosyltransferase and glycosidase processing reactions involving dolichol intermediates. The assembly of O-glycans occurs in the Golgi and does not involve dolichol. For most reactions, families of glycosyltransferases exist; the expression of the individual enzymes within a family is often subject to complex regulation. The biosynthesis of N- and O-glycan is controlled at the level of gene expression, mRNA, enzyme protein activity and localization, and through substrate and cofactor concentrations at the site of synthesis. This complex regulation results in many hundreds of structures, the range of which varies in different species, cell types, tissue types, states of development and differentiation. In diseased cells, the relative proportions of these structures are often characteristically different from normal, and may be useful for the assessment of the stage of the disease and for diagnosis. Knowledge of disease-specific glycoprotein structures and their functions may be used therapeutically, in immunotherapy, in blocking cell adhesion or interfering with other binding or biological processes. Recently, some of the mechanisms underlying glycoprotein alterations in disease have been elucidated. This opens the possibility of an active interference in the disease process. The functions of glycans in diseased cells will become more clear with the tools of molecular biology and transgenic animal models.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0001-5180
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
161
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
36-78
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:9780351-Animals,
pubmed-meshheading:9780351-Communicable Diseases,
pubmed-meshheading:9780351-Congenital Disorders of Glycosylation,
pubmed-meshheading:9780351-Dolichol,
pubmed-meshheading:9780351-Endoplasmic Reticulum,
pubmed-meshheading:9780351-Female,
pubmed-meshheading:9780351-Glycoproteins,
pubmed-meshheading:9780351-Glycosyltransferases,
pubmed-meshheading:9780351-Golgi Apparatus,
pubmed-meshheading:9780351-Humans,
pubmed-meshheading:9780351-Inflammatory Bowel Diseases,
pubmed-meshheading:9780351-Leukocyte-Adhesion Deficiency Syndrome,
pubmed-meshheading:9780351-Male,
pubmed-meshheading:9780351-Mice,
pubmed-meshheading:9780351-Neoplasms,
pubmed-meshheading:9780351-Phenotype,
pubmed-meshheading:9780351-Polysaccharides,
pubmed-meshheading:9780351-Transplantation, Heterologous,
pubmed-meshheading:9780351-Vascular Diseases
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Glycoproteins and their relationship to human disease.
|
| pubmed:affiliation |
Biochemistry Department, University of Toronto, and The Terrence Donnelly Heart Centre, St. Michael's Hospital, Toronto, Canada. Inka.JSBach@sympatico.ca
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
|