rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1994-10-13
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pubmed:abstractText |
Blood group antigens are structural variants in surface carbohydrate or amino acid polymorphisms on extracellular domains of membrane proteins. The red cell water channel-forming integral protein (Aquaporin CHIP) is a homotetramer with only one N-glycosylated subunit, however no CHIP-associated blood group antigens have yet been identified. Immunoblotting, monosaccharide composition analysis, and selective glycosidase digestions revealed that the CHIP-associated oligosaccharide contains ABH determinants and resembles a band 3-type glycan that cannot be cleaved from intact membranes by Peptide:N-glycosidase F. The molecular structure of the Colton antigens was previously unknown, but CHIP was selectively immunoprecipitated with anti-Coa or anti-Co(b). The DNA sequence from Colton-typed individuals predicted that residue 45 is alanine in the Co(a+b-) phenotype and valine in the Co(a-b+) phenotype. The nucleotide polymorphism corresponds to a PflMI endonuclease digestion site in the DNA from Co(a-b+) individuals. These studies have defined antigens within two blood group systems on CHIP: (a) an ABH-bearing polylactosaminoglycan attached to a poorly accessible site in the native membrane; and (b) the Colton antigen polymorphism which may permit the identification of rare individuals with defective water channel expression.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7521882-1280133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7521882-1373524,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/7521882-8362523
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ABO Blood-Group System,
http://linkedlifedata.com/resource/pubmed/chemical/AQP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporins,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Group Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9738
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
94
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1043-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7521882-Humans,
pubmed-meshheading:7521882-Blood Group Antigens,
pubmed-meshheading:7521882-Lymphocytes,
pubmed-meshheading:7521882-Monosaccharides,
pubmed-meshheading:7521882-Base Sequence,
pubmed-meshheading:7521882-ABO Blood-Group System,
pubmed-meshheading:7521882-Oligosaccharides,
pubmed-meshheading:7521882-Macromolecular Substances,
pubmed-meshheading:7521882-Phenotype,
pubmed-meshheading:7521882-Polymorphism, Genetic,
pubmed-meshheading:7521882-Cell Line,
pubmed-meshheading:7521882-Erythrocyte Membrane,
pubmed-meshheading:7521882-Molecular Sequence Data,
pubmed-meshheading:7521882-Carbohydrate Sequence,
pubmed-meshheading:7521882-Protein Structure, Secondary,
pubmed-meshheading:7521882-Ion Channels,
pubmed-meshheading:7521882-Restriction Mapping,
pubmed-meshheading:7521882-Carbohydrate Conformation,
pubmed-meshheading:7521882-Exons,
pubmed-meshheading:7521882-Aquaporins
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