Journal of Leukocyte Biology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published online as doi:10.1189/jlb.0107033 on April 12, 2007

Published online before print April 12, 2007
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
jlb.0107033v1
82/2/272    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gomez-Cambronero, J.
Right arrow Articles by Knapek, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gomez-Cambronero, J.
Right arrow Articles by Knapek, K.
Related Collections
Right arrowRelated Article
(Journal of Leukocyte Biology. 2007;82:272-281.)
© 2007 by Society for Leukocyte Biology

Understanding phospholipase D (PLD) using leukocytes: PLD involvement in cell adhesion and chemotaxis

Julian Gomez-Cambronero1, Mauricio Di Fulvio and Katie Knapek

Cell Biology and Physiology, Wright State University, School of Medicine, Dayton, Ohio, USA

1 Correspondence: Cell Biology and Physiology, Wright State University School of Medicine, 3640 Colonel Glenn Highway, Dayton, OH 45435, USA. E-mail: julian.cambronero{at}wright.edu

ABSTRACT

Phospholipase D (PLD) is an enzyme that catalyzes the conversion of membrane phosphatidylcholine to choline and phosphatidic acid (PA; a second messenger). PLD is expressed in nearly all types of leukocytes and has been associated with phagocytosis, degranulation, microbial killing, and leukocyte maturation. With the application of recently developed molecular tools (i.e., expression vectors, silencing RNA, and specific antibodies), the demonstration of a key role for PLD in those and related cellular actions has contributed to a better awareness of its importance. A case in point is the recent findings that RNA interference-mediated depletion of PLD results in impaired leukocyte adhesion and chemotaxis toward a gradient of chemokines, implying that PLD is necessary for leukocyte movement. We forecast that based on results such as those, leukocytes may prove to be useful tools to unravel still-unresolved mechanistic issues in the complex biology of PLD. Three such issues are considered here: first, whether the cellular actions of PLD are mediated entirely by PA (the product of its enzymatic reaction) or whether PLD by itself interacts with other protein signaling molecules; second, the current difficulty of defining a "PA consensus site" in the various intracellular protein targets of PA; and third, the resolution of specific PLD location (upstream or downstream) in a particular effector signaling cascade. There are reasons to expect that leukocytes and their leukemic cell line counterparts will continue yielding invaluable information to cell biologists to resolve standing molecular and functional issues concerning PLD.

Key Words: signal transduction • differentiation


Related Article

Pivotal Advance: Endogenous pathway to SIRS, sepsis, and related conditions
Amy H. Tang, Gregory J. Brunn, Marilia Cascalho, and Jeffrey L. Platt
J. Leukoc. Biol. 2007 82: 282-285. [Abstract] [Full Text] [PDF]





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2007 by the Society for Leukocyte Biology.