Linked Life Data

2136857

Source:http://linkedlifedata.com/resource/pubmed/id/2136857

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-2-21
pubmed:abstractText
The contribution of N-linked carbohydrates to human interferon-gamma receptor (hIFN-gamma-R) structure and function was investigated in four tumor cell lines of various tissue origin. Western and ligand blotting of native and deglycosylated, affinity-purified hIFN-gamma-R of the monocytic cell line U937 and the lymphoid cell line Raji revealed that the different sizes of hIFN-gamma-R from U937 (103 kDa) and Raji (90 kDa) cells are reduced upon either metabolic inhibition or enzymatic deglycosylation of N-linked carbohydrates to a common size of the receptor molecule with an apparent molecular mass of 73 kDa for both cell lines, indicating that heterogeneity in hIFN-gamma-R size is largely due to differential glycosylation. In all cell lines investigated, inhibition of N-linked glycosylation or modulation of carbohydrate processing did not prevent receptor transport to the cell membrane, but blocked hIFN-gamma binding capacity of membrane-expressed receptor molecules, as revealed by specific binding of hIFN-gamma-R-specific monoclonal antibody and specific binding of 125I-labeled hIFN-gamma. These data suggest that a lack of complex-type N-linked carbohydrates is associated with a complete loss of receptor function, i.e. high affinity binding capacity. Recovery of hIFN-gamma binding of deglycosylated receptors was achieved upon affinity purification and adsorption to nitrocellulose membranes, indicating that the carbohydrate side chains themselves do not directly contribute to the ligand binding epitope but seem to be essential for appropriate conformation of the receptor protein in the cell membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1710-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:2136857-Alkaloids, pubmed-meshheading:2136857-Blotting, Western, pubmed-meshheading:2136857-Cell Line, pubmed-meshheading:2136857-Cell Membrane, pubmed-meshheading:2136857-Chromatography, Affinity, pubmed-meshheading:2136857-Glycoside Hydrolases, pubmed-meshheading:2136857-Glycosylation, pubmed-meshheading:2136857-Humans, pubmed-meshheading:2136857-Interferon-gamma, pubmed-meshheading:2136857-Kinetics, pubmed-meshheading:2136857-Ligands, pubmed-meshheading:2136857-Lymphocytes, pubmed-meshheading:2136857-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, pubmed-meshheading:2136857-Membrane Glycoproteins, pubmed-meshheading:2136857-Molecular Weight, pubmed-meshheading:2136857-Monocytes, pubmed-meshheading:2136857-Precipitin Tests, pubmed-meshheading:2136857-Receptors, Immunologic, pubmed-meshheading:2136857-Receptors, Interferon, pubmed-meshheading:2136857-Structure-Activity Relationship, pubmed-meshheading:2136857-Swainsonine, pubmed-meshheading:2136857-Tunicamycin
pubmed:year
1990
pubmed:articleTitle
Glycosylation of the human interferon-gamma receptor. N-linked carbohydrates contribute to structural heterogeneity and are required for ligand binding.
pubmed:affiliation
Clinical Research Group, Biological Regulation of Host-Tumor-Interaction, Max-Planck-Society, Medical Clinic, University of Göttingen, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't