Linked Life Data

10838164

Source:http://linkedlifedata.com/resource/pubmed/id/10838164

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-7-20
pubmed:abstractText
Numerous studies show that PLD is activated in cells by calcium and by protein kinase C (PKC). We found that human PLD1 and PLD2 expressed in Sf9 cells can be activated by calcium-mobilizing agonists and by co-expression with PKCalpha. The calcium-mobilizing agonists A23187 and CryIC toxin triggered large increases in phosphatidylethanol (PtdEth) production in Sf9 cells over-expressing PLD1 and PLD2, but not in vector controls. PLD activation by these agonists was largely dependent on extracellular calcium. Membrane assays demonstrated significant PLD1 and PLD2 activity in the absence of divalent cations, which could be enhanced by low levels of calcium either in the presence or absence of magnesium. PLD1 but not PLD2 activity was slightly enhanced by magnesium. Treatment of Sf9 cells expressing PLD1 and PLD2 with PMA resulted in little PtdEth production. However, a significant and comparable formation of PtdEth occurred when PLD1 or PLD2 were co-expressed with PKCalpha, but not PKCdelta, and was further augmented by PMA. In contrast to PLD1, co-expressing PLD2 with PKCalpha or PKCdelta further enhanced A23187-induced PtdEth production. Immunoprecipitation experiments demonstrated that PLD1 and PLD2 associated with the PKC isoforms in Sf9 cells. Furthermore, in membrane reconstitution assays, both PLD1 and PLD2 could be stimulated by calmodulin and PKCalpha-enriched cytosol. The results indicate that PLD2 as well as PLD1 is subject to agonist-induced activation in intact cells and can be regulated by calcium and PKC.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins, http://linkedlifedata.com/resource/pubmed/chemical/Calcimycin, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Recombinant, http://linkedlifedata.com/resource/pubmed/chemical/Endotoxins, http://linkedlifedata.com/resource/pubmed/chemical/Hemolysin Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C, http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate, http://linkedlifedata.com/resource/pubmed/chemical/insecticidal crystal protein..., http://linkedlifedata.com/resource/pubmed/chemical/phospholipase D1, http://linkedlifedata.com/resource/pubmed/chemical/phospholipase D2
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
1497
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
103-14
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Regulation of human PLD1 and PLD2 by calcium and protein kinase C.
pubmed:affiliation
Program in Cell Biology, Department of Pediatrics, National Jewish Medical and Research Center, 1400 Jackson St., Denver, CO 80206, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't