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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
39
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pubmed:dateCreated |
1995-11-6
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pubmed:abstractText |
Rat T lymphocyte alloantigen 6.1 (RT6.1), which was synthesized as the fusion protein with a maltose-binding protein in Escherichia coli, displayed NAD(+)-dependent auto-ADP-ribosylation in addition to an enzyme activity of NAD+ glycohydrolase. Such ADP-ribosylation of RT6.1 was also observed in lymphocytes isolated from rat tissues as follows. When intact rat lymphocytes expressing RT6.1 mRNA were incubated with [alpha-32P]NAD+, its radioactivity was incorporated into a cell surface protein with the M(r) of 31,000. The radiolabeled 31-kDa protein was released from the cell surface by treatment of the cells with phosphatidylinositol-specific phospholipase C and immunoprecipitated with anti-RT6.1 antiserum. The radioactivity incorporated into the 31-kDa protein was recovered as 5'-[32P]AMP upon incubation with snake venom phosphodiesterase and also removed by NH2OH treatment. These results suggested that the NAD(+)-dependent modification of the 31-kDa protein was due to ADP-ribosylation of glycosylphosphatidylinositol-anchored RT6.1 at an arginine residue. When intact lymphocytes, in which RT6.1 had been once modified by [32P]ADP-ribosylation, were further incubated in the absence of NAD+, there was reduction of the radioactivity in the [32P]ADP-ribosylated RT6.1. The reduced radioactivity was recovered from the incubation medium as [32P]ADP-ribose. This reduction was effectively inhibited by the addition of ADP-ribose to the reaction mixture. Moreover, readdition of NAD+ caused the ADP-ribosylation of RT6.1 again. Thus, the ADP-ribosylation of RT6.1 appeared to proceed reversibly in intact rat lymphocytes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP Ribose Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Monophosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Art2b protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Isoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoinositide Phospholipase C,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphorus Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Snake Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/maltose transport system, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
22747-51
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:7559400-ADP Ribose Transferases,
pubmed-meshheading:7559400-ATP-Binding Cassette Transporters,
pubmed-meshheading:7559400-Adenosine Diphosphate Ribose,
pubmed-meshheading:7559400-Adenosine Monophosphate,
pubmed-meshheading:7559400-Animals,
pubmed-meshheading:7559400-Antigens, Differentiation, T-Lymphocyte,
pubmed-meshheading:7559400-Arginine,
pubmed-meshheading:7559400-Binding Sites,
pubmed-meshheading:7559400-Carrier Proteins,
pubmed-meshheading:7559400-Cells, Cultured,
pubmed-meshheading:7559400-Cloning, Molecular,
pubmed-meshheading:7559400-Escherichia coli,
pubmed-meshheading:7559400-Escherichia coli Proteins,
pubmed-meshheading:7559400-Gene Expression,
pubmed-meshheading:7559400-Glycosylphosphatidylinositols,
pubmed-meshheading:7559400-Histocompatibility Antigens,
pubmed-meshheading:7559400-Isoantigens,
pubmed-meshheading:7559400-Maltose,
pubmed-meshheading:7559400-Maltose-Binding Proteins,
pubmed-meshheading:7559400-Membrane Glycoproteins,
pubmed-meshheading:7559400-Monosaccharide Transport Proteins,
pubmed-meshheading:7559400-NAD,
pubmed-meshheading:7559400-Phosphatidylinositol Diacylglycerol-Lyase,
pubmed-meshheading:7559400-Phosphoinositide Phospholipase C,
pubmed-meshheading:7559400-Phosphoric Diester Hydrolases,
pubmed-meshheading:7559400-Phosphorus Radioisotopes,
pubmed-meshheading:7559400-RNA, Messenger,
pubmed-meshheading:7559400-Rats,
pubmed-meshheading:7559400-Recombinant Fusion Proteins,
pubmed-meshheading:7559400-Snake Venoms,
pubmed-meshheading:7559400-T-Lymphocytes
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pubmed:year |
1995
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pubmed:articleTitle |
NAD(+)-dependent ADP-ribosylation of T lymphocyte alloantigen RT6.1 reversibly proceeding in intact rat lymphocytes.
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pubmed:affiliation |
Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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