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Identification of caspase 3 motifs and critical aspartate residues in human phospholipase D1b and phospholipase D2a
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Wright, Michelle H., Farquhar, Michelle J., Aletrari, Mina-Olga, Ladds, Graham and Hodgkin, Matthew N. (2008) Identification of caspase 3 motifs and critical aspartate residues in human phospholipase D1b and phospholipase D2a. Biochemical and Biophysical Research Communications, Vol.369 (No.2). pp. 478-484. doi:10.1016/j.bbrc.2008.02.064 ISSN 0006-291X.
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Official URL: http://dx.doi.org/10.1016/j.bbrc.2008.02.064
Abstract
Stimulation of mammalian cells frequently initiates phospholipase D-catalyzed hydrolysis of phosphatidylcholine in the plasma membrane to yield phosphatidic acid (PA) a novel lipid messenger. PA plays a regulatory role in important cellular processes such as secretion, cellular shape change, and movement. A number of studies have highlighted that PLD-based signaling also plays a pro-mitogenic and pro-survival role in cells and therefore anti-apoptotic. We show that human PLD1b and PLD2a contain functional caspase 3 cleavage sites and identify the critical aspartate residues within PLD1b that affect its activation by phorbol esters and attenuate phosphatidylcholine hydrolysis during apoptosis. (C) 2008 Elsevier Inc. All rights reserved.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology Q Science > QP Physiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) > Biological Sciences ( -2010) | ||||
Library of Congress Subject Headings (LCSH): | Phospholipases, Apoptosis | ||||
Journal or Publication Title: | Biochemical and Biophysical Research Communications | ||||
Publisher: | Elsevier | ||||
ISSN: | 0006-291X | ||||
Official Date: | 2 May 2008 | ||||
Dates: |
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Volume: | Vol.369 | ||||
Number: | No.2 | ||||
Number of Pages: | 7 | ||||
Page Range: | pp. 478-484 | ||||
DOI: | 10.1016/j.bbrc.2008.02.064 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access | ||||
Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) |
Data sourced from Thomson Reuters' Web of Knowledge
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