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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1989-8-18
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pubmed:abstractText |
Utilizing a solid phase binding assay, we have demonstrated that rIL-2 binds with high affinity to the human urinary glycoprotein uromodulin. This binding is specifically inhibited by the saccharides diacetylchitobiose and Man(alpha 1-3)(Man(alpha 1-6]Man-O-methyl and by the high mannose glycopeptides Man5GlcNAc2-R and Man6GlcNAc2-R, but not by Man9GlcNAc2-R. rIL-2 also binds OVA, a glycoprotein which contains approximately 50% high mannose chains at a single glycosylation site, and to yeast mannan. This binding is inhibited by the same battery of saccharides which inhibit the binding to uromodulin. The conclusion that rIL-2 is a lectin is further supported by the observation that the sequence of IL-2 shares 27% homology with a 33-residue sequence of the carbohydrate-binding domain of human mannose-binding protein. The potential physiologic relevance of the carbohydrate binding activity is further elucidated by studies which show that 1) binding of soluble rIL-2 to immobilized uromodulin is enhanced at a pH of 4 to5 in the presence of divalent cations, and 2) neither uromodulin nor the high mannose glycopeptide Man5GlcNAc2Asn blocks the binding of rIL-2 to the IL-2R. Thus the carbohydrate-binding site of rIL-2 is distinct from the cell surface receptor-binding site, and might function preferentially in acidic microenvironments.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Mucoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/UMOD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Uromodulin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
143
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
939-44
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:2787353-Amino Acid Sequence,
pubmed-meshheading:2787353-Binding, Competitive,
pubmed-meshheading:2787353-Carbohydrate Sequence,
pubmed-meshheading:2787353-Carrier Proteins,
pubmed-meshheading:2787353-Female,
pubmed-meshheading:2787353-Glycopeptides,
pubmed-meshheading:2787353-Humans,
pubmed-meshheading:2787353-Hydrogen-Ion Concentration,
pubmed-meshheading:2787353-Interleukin-2,
pubmed-meshheading:2787353-Lectins,
pubmed-meshheading:2787353-Mannose,
pubmed-meshheading:2787353-Mannose-Binding Lectins,
pubmed-meshheading:2787353-Molecular Sequence Data,
pubmed-meshheading:2787353-Mucoproteins,
pubmed-meshheading:2787353-Oligosaccharides,
pubmed-meshheading:2787353-Pregnancy,
pubmed-meshheading:2787353-Receptors, Interleukin-2,
pubmed-meshheading:2787353-Recombinant Proteins,
pubmed-meshheading:2787353-Uromodulin
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pubmed:year |
1989
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pubmed:articleTitle |
IL-2, a lectin with specificity for high mannose glycopeptides.
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pubmed:affiliation |
Department of Biochemistry, University of Maine, Orono 04469.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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