Source:http://linkedlifedata.com/resource/pubmed/id/16821040
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
2006-12-15
|
pubmed:abstractText |
Aluminum (Al(3+)) has been recognized as a main toxic factor in crop production in acid lands. Phosphatidic acid (PA) is emerging as an important lipid signaling molecule and has been implicated in various stress-signaling pathways in plants. In this paper, we focus on how PA generation is affected by Al(3+) using Coffea arabica suspension cells. We pre-labeled cells with [(32)P]orthophosphate ((32)Pi) and assayed for (32)P-PA formation in response to Al(3+). Treating cells for 15 min with either AlCl(3) or Al(NO(3))(3) inhibited the formation of PA. In order to test how Al(3+) affected PA signaling, we used the peptide mastoparan-7 (mas-7), which is known as a very potent stimulator of PA formation. The Al(3+) inhibited mas-7 induction of PA response, both before and after Al(3+) incubation. The PA involved in signaling is generated by two distinct phospholipid signaling pathways, via phospholipase D (PLD; EC: 3.1.4.4) or via Phospholipase C (PLC; EC: 3.1.4.3), and diacylglycerol kinase (DGK; EC 2.7.1.107). By labeling with (32)Pi for short periods of time, we found that PA formation was inhibited almost 30% when the cells were incubated with AlCl(3) suggesting the involvement of the PLC/DGK pathway. Incubation of cells with PLC inhibitor, U73122, affected PA formation, like AlCl(3) did. PLD in vivo activation by mas-7 was reduced by Al(3+). These results suggest that PA formation was prevented through the inhibition of the PLC activity, and it provides the first evidence for the role of Al toxicity on PA production.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aluminum Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Chlorides,
http://linkedlifedata.com/resource/pubmed/chemical/Diacylglycerol Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Wasp Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/aluminum chloride,
http://linkedlifedata.com/resource/pubmed/chemical/mastoparan
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0032-0935
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
225
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
393-401
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:16821040-Aluminum Compounds,
pubmed-meshheading:16821040-Cells, Cultured,
pubmed-meshheading:16821040-Chlorides,
pubmed-meshheading:16821040-Coffea,
pubmed-meshheading:16821040-Diacylglycerol Kinase,
pubmed-meshheading:16821040-Peptides,
pubmed-meshheading:16821040-Phosphatidic Acids,
pubmed-meshheading:16821040-Phospholipase D,
pubmed-meshheading:16821040-Signal Transduction,
pubmed-meshheading:16821040-Type C Phospholipases,
pubmed-meshheading:16821040-Wasp Venoms
|
pubmed:year |
2007
|
pubmed:articleTitle |
Aluminum inhibits phosphatidic acid formation by blocking the phospholipase C pathway.
|
pubmed:affiliation |
Centro de Investigación Científica de Yucatán, Unidad de Bioquímica y Biología Molecular de Plantas, Calle 43, 130 Col Chuburná de Hidalgo, Mérida Yucatán, México.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|