Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1996-8-8
pubmed:databankReference
pubmed:abstractText
One of the hallmarks of mucosal-host defense is the clearance of inhaled Ags by alveolar macrophages (AM) through interactions of IgA Abs and IgA Fc receptors (Fc alpha R). AM constitutively expressed Fc alpha R at lower levels than freshly isolated and in vitro-differentiated monocytes as determined by immunofluorescence using four anti-Fc alpha R mAb. SDS-PAGE analysis of iodinated cell surface proteins revealed that Fc alpha R on AM has an Mr of 50 to 65 kDa, slightly lower than that on monocytes (55-75 kDa). Treatment of AM Fc alpha R by N-glycanase gave rise to a protein core of 28 KDa, smaller than the 32-kDa backbone of blood monocytes. AM Fc alpha R molecules were unaffected by phosphatidylinositol-phospholipase C treatment. Fc alpha R transcripts were analyzed by reverse transcription-PCR using primers in the 5' and 3' regions of a U937 Fc alpha R cDNA. Three transcripts were amplified, cloned, and sequenced from AM and/or monocyte mRNA, the full length Fc alpha R and two alternatively spliced products corresponding to deletions of 66 and 288 nucleotides in the portion coding for the extracellular domain; they were named Fc alpha R a.1, a.2, and a.3, respectively. These PCR products were transcribed and translated in vitro into three proteins (Mr 32, 30, and 22 kDa, respectively), in which the 32- and 30-kDa species were immunoprecipitated by an anti-Fc alpha R mAb. The predicted size of the protein encoded by the Fc alpha R a.2 transcript without the leader peptide is Mr approximately 27,400, a value that is consistent with the Mr of AM Fc alpha R backbone. These results indicate that AM express at their surfaces a protein product of an alternatively spliced Fc alpha R transcript, the Fc alpha R a.2 isoform, that might have physiologic relevance in IgA-mediated host defense at mucosal sites.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
156
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4442-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8666819-Alternative Splicing, pubmed-meshheading:8666819-Animals, pubmed-meshheading:8666819-Antibodies, Monoclonal, pubmed-meshheading:8666819-Antigens, CD, pubmed-meshheading:8666819-Base Sequence, pubmed-meshheading:8666819-DNA, Complementary, pubmed-meshheading:8666819-DNA Primers, pubmed-meshheading:8666819-Gene Expression, pubmed-meshheading:8666819-Humans, pubmed-meshheading:8666819-Immunity, Mucosal, pubmed-meshheading:8666819-Macrophages, Alveolar, pubmed-meshheading:8666819-Mice, pubmed-meshheading:8666819-Molecular Sequence Data, pubmed-meshheading:8666819-Monocytes, pubmed-meshheading:8666819-Polymerase Chain Reaction, pubmed-meshheading:8666819-Protein Biosynthesis, pubmed-meshheading:8666819-Receptors, Fc, pubmed-meshheading:8666819-Sequence Homology, Nucleic Acid, pubmed-meshheading:8666819-Transcription, Genetic
pubmed:year
1996
pubmed:articleTitle
Identification of Fc alpha receptor (CD89) isoforms generated by alternative splicing that are differentially expressed between blood monocytes and alveolar macrophages.
pubmed:affiliation
INSERM U25, Necker Hospital, Paris, France.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't