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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1990-2-9
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pubmed:abstractText |
In order to examine the role of phosphatidylinositol bisphosphate (PIP2) hydrolysis in B cell activation, we studied the effect of various classes of protein kinase C (PKC) activators on anti-Ig-mediated B cell stimulation. Anti-Ig-stimulated PIP2 hydrolysis, elevations in [Ca2+]i, and induction of DNA synthesis were inhibited by PMA (a phorbol ester) as previously reported. In contrast, indolactam (an alkaloid PKC activator) inhibited PIP2 hydrolysis and elevations in [Ca2+]i, but stimulated rather than inhibited cellular proliferation. In order to examine whether the binding avidity of the PKC activators to PKC played a role in determining their activity to stimulate or inhibit B cell activation, we studied two other PKC activators, bryostatin and mezerein. Again, both inhibited anti-Ig mediated PIP2 hydrolysis and elevations in [Ca2+]i, whereas only the former inhibited induction of DNA synthesis. These data suggest that a) high levels of PIP2 hydrolysis and elevations in [Ca2+]i are not essential for anti-Ig-mediated induction of B cell DNA synthesis and b) activation of PKC may induce both stimulatory and inhibitory pathways of B cell activation, and whether stimulation or inhibition of cell activation is observed may depend on the combined intensity of these two signals.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Anti-Idiotypic,
http://linkedlifedata.com/resource/pubmed/chemical/Bryostatins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Diterpenes,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin delta-Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Indoles,
http://linkedlifedata.com/resource/pubmed/chemical/Ionomycin,
http://linkedlifedata.com/resource/pubmed/chemical/Lactams,
http://linkedlifedata.com/resource/pubmed/chemical/Lactones,
http://linkedlifedata.com/resource/pubmed/chemical/Macrolides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 4,5-Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, B-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Terpenes,
http://linkedlifedata.com/resource/pubmed/chemical/bryostatin 1,
http://linkedlifedata.com/resource/pubmed/chemical/indolactam V,
http://linkedlifedata.com/resource/pubmed/chemical/mezerein
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
144
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
451-5
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2153169-Animals,
pubmed-meshheading:2153169-Antibodies, Anti-Idiotypic,
pubmed-meshheading:2153169-B-Lymphocytes,
pubmed-meshheading:2153169-Bryostatins,
pubmed-meshheading:2153169-Calcium,
pubmed-meshheading:2153169-Diterpenes,
pubmed-meshheading:2153169-Enzyme Activation,
pubmed-meshheading:2153169-Immunoglobulin delta-Chains,
pubmed-meshheading:2153169-Indoles,
pubmed-meshheading:2153169-Ionomycin,
pubmed-meshheading:2153169-Lactams,
pubmed-meshheading:2153169-Lactones,
pubmed-meshheading:2153169-Lymphocyte Activation,
pubmed-meshheading:2153169-Macrolides,
pubmed-meshheading:2153169-Mice,
pubmed-meshheading:2153169-Mice, Inbred DBA,
pubmed-meshheading:2153169-Phosphatidylinositol 4,5-Diphosphate,
pubmed-meshheading:2153169-Phosphatidylinositols,
pubmed-meshheading:2153169-Protein Kinase C,
pubmed-meshheading:2153169-Receptors, Antigen, B-Cell,
pubmed-meshheading:2153169-Signal Transduction,
pubmed-meshheading:2153169-Terpenes
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pubmed:year |
1990
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pubmed:articleTitle |
Protein kinase C activation in B cells by indolactam inhibits anti-Ig-mediated phosphatidylinositol bisphosphate hydrolysis but not B cell proliferation.
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pubmed:affiliation |
Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD 20814-4799.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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