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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1992-11-25
pubmed:abstractText
C33 Ag was originally identified by mAb inhibitory to syncytium formation induced by human T cell leukemia virus type 1. The Ag was shown to be a highly heterogeneous glycoprotein consisting of a 28-kDa protein and N-linked oligosaccharides ranging from 10 to 50 kDa. In the present study, cDNA clones were isolated from a human T cell cDNA expression library in Escherichia coli by using mAb C33. The identity of cDNA was verified by immunostaining and immunoprecipitation of transfected NIH3T3 cells with mAb. The cDNA contained an open reading frame of a 267-amino acid sequence which was a type III integral membrane protein of 29.6 kDa with four putative transmembrane domains and three putative N-glycosylation sites. The C33 gene was found to belong to a newly defined family of genes for membrane proteins, such as CD9, CD37, CD53, CD63, and TAPA-1, and was identical to R2, a cDNA recently isolated because of its strong up-regulation after T cell activation. Availability of mAb for C33 Ag enabled us to define its distribution in human leukocytes. C33 Ag was expressed in CD4+ T cells, CD19+ B cells, CD14+ monocytes, and CD16+ granulocytes. Its expression was low in CD8+ T cells and mostly negative in CD16+ NK cells. PHA stimulation enhanced the expression of C33 Ag in CD4+ T cells by about 5-fold and in CD8+ T cells by about 20-fold. PHA stimulation also induced the dramatic size changes in the N-linked sugars previously shown to accompany human T cell leukemia virus type 1-induced transformation of CD4+ T cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
149
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2879-86
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:1401919-Amino Acid Sequence, pubmed-meshheading:1401919-Antibodies, Monoclonal, pubmed-meshheading:1401919-Antigens, CD, pubmed-meshheading:1401919-Antigens, CD82, pubmed-meshheading:1401919-Antigens, Differentiation, pubmed-meshheading:1401919-Antigens, Surface, pubmed-meshheading:1401919-Base Sequence, pubmed-meshheading:1401919-Blotting, Northern, pubmed-meshheading:1401919-Cell Line, pubmed-meshheading:1401919-Cloning, Molecular, pubmed-meshheading:1401919-Flow Cytometry, pubmed-meshheading:1401919-Gene Library, pubmed-meshheading:1401919-Giant Cells, pubmed-meshheading:1401919-Glycosylation, pubmed-meshheading:1401919-Human T-lymphotropic virus 1, pubmed-meshheading:1401919-Humans, pubmed-meshheading:1401919-Lymphocyte Activation, pubmed-meshheading:1401919-Membrane Glycoproteins, pubmed-meshheading:1401919-Molecular Sequence Data, pubmed-meshheading:1401919-Open Reading Frames, pubmed-meshheading:1401919-Proto-Oncogene Proteins, pubmed-meshheading:1401919-RNA, Messenger, pubmed-meshheading:1401919-T-Lymphocytes, pubmed-meshheading:1401919-Tetradecanoylphorbol Acetate, pubmed-meshheading:1401919-Transfection, pubmed-meshheading:1401919-Up-Regulation
pubmed:year
1992
pubmed:articleTitle
C33 antigen recognized by monoclonal antibodies inhibitory to human T cell leukemia virus type 1-induced syncytium formation is a member of a new family of transmembrane proteins including CD9, CD37, CD53, and CD63.
pubmed:affiliation
Shionogi Institute for Medical Science, Osaka, Japan.
pubmed:publicationType
Journal Article