Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1992-7-29
pubmed:abstractText
The bovine interferon-alpha receptor (BoIFN-alpha R) mediates the activity of bovine IFN-alpha s and IFN-beta. In addition, human IFN-alpha s have uniformly high biological activity on bovine cells. A 32P-labeled derivative of human recombinant IFN-alpha A (HuIFN-alpha A-P1) binds well and can form a characteristic 130-kDa complex on bovine cells, but not on hamster cells. We have, therefore, analyzed the binding and covalent crosslinking of [32P]HuIFN-alpha A-P1 to a panel of bovine-hamster somatic cell hybrids. Binding to several bovine-hamster hybrid cell lines was strong (about 30-50% of that seen with bovine MDBK cells) and specific. The binding correlated uniquely with bovine syntenic group U10. In several of the hybrid lines, the ability of human IFN-alpha B to enhance the expression of endogenous MHC class I molecules correlated with the binding results. We thus conclude that the bovine IFN-alpha R structural gene (locus designation IFNAR) localizes to syntenic group U10. This group includes a number of other genes whose homologs map to human Chromosome (Chr) 21.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0938-8990
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
237-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Somatic cell mapping of the bovine interferon-alpha receptor.
pubmed:affiliation
Department of Molecular Genetics and Microbiology, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway 08854-5635.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't