Linked Life Data

8144881

Source:http://linkedlifedata.com/resource/pubmed/id/8144881

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1994-5-4
pubmed:abstractText
Triggering of the Ig receptor (IgR) induces the activation in multiple intracellular signal transduction reactions including protein tyrosine phosphorylation, activation of phospholipase C, increased inositoltriphosphate, increased diacylglycerol, intracellular Ca2+ mobilization, and activation of protein kinase C. The IgR-complex, composed of mu-chain, L chain, Ig-alpha (MB-1), and Ig-beta (B29) proteins, is a functional unit both for expression of IgR and for signal transduction into cells, possibly by physical association with the down-stream functional molecules. An important functional motif ((D or E)-X7-(D or E)-Y-X3-L-X7-Y-X2-(L or I)) in the cytoplasmic domain of MB-1 molecule was shown to bind with several phosphoprotein components including src-type tyrosine kinases and phosphatidylinositol-3 kinase. To further study the functional components, we analyzed the phosphoprotein molecules coprecipitated with MB-1 protein. We found that a 52-kDa protein is coprecipitated with MB-1 protein and is inducibly phosphorylated by the stimulation with PMA. A rat mAb, prepared by immunizing the 52-kDa protein purified from SDS-PAGE, could detect the similar 52-kDa phosphoprotein (p52) expressed on the cell surface. In comparison with the 52-kDa protein in the immunoprecipitate of MB-1, the p52 migrated to the same position on 2-D gel electrophoresis (nonequilibrium pH gradient gel electrophoresis/SDS-PAGE). An in vitro kinase reaction analysis demonstrated that the p52 is tightly associated with the tyrosine kinase molecule(s), one of which is an 80-kDa protein containing an apparent autophosphorylation activity. These molecules would provide the informations of the down-stream molecules in the cascade reactions of the IgR-mediated signal transduction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
152
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2742-52
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8144881-Amino Acid Sequence, pubmed-meshheading:8144881-Animals, pubmed-meshheading:8144881-Antibodies, Monoclonal, pubmed-meshheading:8144881-Antigens, CD, pubmed-meshheading:8144881-Antigens, CD79, pubmed-meshheading:8144881-Membrane Glycoproteins, pubmed-meshheading:8144881-Mice, pubmed-meshheading:8144881-Mice, Inbred BALB C, pubmed-meshheading:8144881-Molecular Sequence Data, pubmed-meshheading:8144881-Molecular Weight, pubmed-meshheading:8144881-Phosphoproteins, pubmed-meshheading:8144881-Phosphorylation, pubmed-meshheading:8144881-Precipitin Tests, pubmed-meshheading:8144881-Protein-Tyrosine Kinases, pubmed-meshheading:8144881-Rats, pubmed-meshheading:8144881-Rats, Wistar, pubmed-meshheading:8144881-Receptors, Antigen, B-Cell, pubmed-meshheading:8144881-Tetradecanoylphorbol Acetate
pubmed:year
1994
pubmed:articleTitle
Identification of a 52-kDa molecule (p52) coprecipitated with the Ig receptor-related MB-1 protein that is inducibly phosphorylated by the stimulation with phorbol myristate acetate.
pubmed:affiliation
Department of Immunology, School of Life Science, Faculty of Medicine, Tottori University, Yonago, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't