Linked Life Data

8871630

Source:http://linkedlifedata.com/resource/pubmed/id/8871630

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1996-12-17
pubmed:abstractText
Post-translational modifications are important in regulating the functions of signal proteins. This is well established for intracellular proteins, but little is known in the case of extracellular domains of cell surface molecules. We recently described a cell surface protein, mono-ADP-ribosyltransferase (ADPRT), on cytotoxic T cells and showed that it mediates attachment of ADP-ribose to cell surface proteins. Concomitantly, cytolytic activity and cell proliferation are inhibited. Here we report that one of the principal proteins modified by this enzyme is lymphocyte function-associated molecule-1 (LFA-1). While both chains are ADP-ribosylated on the extracellular domain of the molecule, persistence of the modification differs between the chains. Label is released from the beta-chain by 1 h, yet remains for at least 6 h on the alpha-chain. Loss of label is suppressed by phosphodiesterase inhibitors such as ADP-ribose and p-nitrophenylthymidine 5'-monophosphate, pointing to the involvement of this class of enzyme. Modification of LFA-1 requires expression of the cell surface ADPRT and causes the loss of epitopes recognized by alpha- and beta-chain-specific Abs. Concomitantly, the generation of inositol phosphates induced by Ab cross-linking of LFA-1 is significantly inhibited. Consistent with this effect, anti-LFA-1-induced homotypic cell adhesion is also inhibited. These effects are not seen in cells from which the ADPRT was removed by phospholipase C. Moreover, cells lacking the cell surface ADPRT are not inhibited by NAD in the cell adhesion assay, but gain this property upon transfection with the ADPRT gene. It is concluded that the cell surface protein mono-ADPRT regulates LFA-1 functions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
157
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3341-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8871630-ADP Ribose Transferases, pubmed-meshheading:8871630-Animals, pubmed-meshheading:8871630-Antibodies, pubmed-meshheading:8871630-Arginine, pubmed-meshheading:8871630-Cell Adhesion, pubmed-meshheading:8871630-Cell Line, pubmed-meshheading:8871630-Cell Membrane, pubmed-meshheading:8871630-Epitopes, pubmed-meshheading:8871630-Hybridomas, pubmed-meshheading:8871630-Lymphocyte Function-Associated Antigen-1, pubmed-meshheading:8871630-Membrane Proteins, pubmed-meshheading:8871630-Mice, pubmed-meshheading:8871630-Mice, Inbred BALB C, pubmed-meshheading:8871630-Mice, Inbred C57BL, pubmed-meshheading:8871630-NAD, pubmed-meshheading:8871630-Phosphoric Diester Hydrolases, pubmed-meshheading:8871630-Poly(ADP-ribose) Polymerases, pubmed-meshheading:8871630-Protein Processing, Post-Translational, pubmed-meshheading:8871630-Signal Transduction, pubmed-meshheading:8871630-T-Lymphocytes, Cytotoxic, pubmed-meshheading:8871630-Transfection
pubmed:year
1996
pubmed:articleTitle
Cell surface ADP-ribosyltransferase regulates lymphocyte function-associated molecule-1 (LFA-1) function in T cells.
pubmed:affiliation
Department of Molecular Microbiology and Immunology, Norris Comprehensive Cancer Center, University of Southern California School of Medicine, Los Angeles 90033, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't