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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1992-3-24
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pubmed:abstractText |
Nonglycosylated murine and human granulocyte-macrophage colony-stimulating factor have a molecular mass of approximately 14.5 kDa predicted from the primary amino acid sequence. The expression of both proteins in COS cells leads to a heterogeneous population of molecules that differ in the degree of glycosylation. Both human and murine molecules contain two N-linked glycosylation sites that are situated in nonhomologous locations along the linear sequence. Despite this difference both proteins show a similar size distribution among the glycosylation variants. These studies analyze the effects of introducing in the murine protein novel N-linked glycosylation sites corresponding to those sites found in the human molecule. A panel of molecules composed of various combinations of human N-linked glycosylation sites in either the presence or the absence of murine N-linked glycosylation was compared. Substitution of a proper human N-linked glycosylation consensus sequence at Asn 24 did not result in N-linked glycosylation, nor was there any considerable effect on bioactivity. Replacement of the N-linked glycosylation consensus sequence at Asn 34 results in glycosylation similar to that found in the human molecule and causes a significant decrease in bioactivity. These data suggest that the position of N-linked glycosylation is critical for maximal bioactivity in a particular species and that the changes in position of these sites in different species probably occurred during evolution in response to changes in their receptors.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
|
pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
293
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
349-55
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1536571-Amino Acid Sequence,
pubmed-meshheading:1536571-Animals,
pubmed-meshheading:1536571-Asparagine,
pubmed-meshheading:1536571-Carbohydrate Conformation,
pubmed-meshheading:1536571-Cell Line,
pubmed-meshheading:1536571-Genetic Vectors,
pubmed-meshheading:1536571-Glycosylation,
pubmed-meshheading:1536571-Granulocyte-Macrophage Colony-Stimulating Factor,
pubmed-meshheading:1536571-Humans,
pubmed-meshheading:1536571-Mice,
pubmed-meshheading:1536571-Molecular Sequence Data,
pubmed-meshheading:1536571-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1536571-Transfection
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pubmed:year |
1992
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pubmed:articleTitle |
Evaluation of human N-linked glycosylation sites in murine granulocyte-macrophage colony-stimulating factor.
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pubmed:affiliation |
Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia 19104.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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