PMID- 10224668
OWN - NLM
STAT- MEDLINE
DCOM- 19990608
LR  - 20190921
IS  - 1357-2725 (Print)
IS  - 1357-2725 (Linking)
VI  - 31
IP  - 3-4
DP  - 1999 Mar-Apr
TI  - Phospholipases and phagocytosis: the role of phospholipid-derived second
      messengers in phagocytosis.
PG  - 415-30
AB  - Phagocytosis, the process by which leukocytes recognize and destroy invading
      pathogens, is essential for host defense. The binding of foreign organisms to
      phagocytic leukocytes initiates a complex signaling cascade which ultimately
      results in the entrapment and destruction of the pathogen. The signal
      transduction pathway mediating phagocytosis is the subject of intense
      investigation and is known to include protein tyrosine kinases, GTP-binding
      proteins, protein kinase C (PKC), actin polymerization and membrane movement. A
      rapidly expanding body of evidence suggests that phospholipases play an integral 
      role in phagocytosis by generating essential second messengers. Here we review
      the data linking activation of phospholipase A2 (PLA2), phospholipase C (PLC)
      phospholipase D (PLD), and phosphoinositide 3-OH kinase (PI(3)K) to antibody
      (IgG)-mediated phagocytosis. Evidence is presented that (1) PLA2-derived
      arachidonic acid (AA) stimulates NADPH oxidase and membrane redistribution during
      phagocytosis, (2) the inositol-3,4,5-triphosphate (IP3) and diacylglycerol (DAG) 
      products of PLC activate NADPH oxidase and PKC, and (3) sequential activation of 
      PLD and phosphatidic acid phosphohydrolase may provide an alternative pathway for
      generation of DAG. Additionally, considerable evidence exists that wortmannin, a 
      PI(3)K inhibitor, depresses phagocytosis. This finding is discussed in the
      context of the extensive effects PI(3)K products have on endocytosis and
      exocytosis and the potential role of membrane redistribution in phagocytosis.
      Finally, a model is presented which integrates data obtained from a variety of
      phagocytic systems and illustrates potential interactions that may exist between 
      phospholipase-derived second messengers and signaling events required for
      phagocytosis.
FAU - Lennartz, M R
AU  - Lennartz MR
AD  - Department of Physiology and Cell Biology, Albany Medical College, NY 12208, USA.
      mlennartz@ccgateway.amc.edu
LA  - eng
GR  - GM 45983/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - Netherlands
TA  - Int J Biochem Cell Biol
JT  - The international journal of biochemistry & cell biology
JID - 9508482
RN  - 27YG812J1I (Arachidonic Acid)
RN  - EC 2.7.11.1 (3-Phosphoinositide-Dependent Protein Kinases)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.13 (Protein Kinase C)
RN  - EC 3.1.- (Phospholipases)
RN  - EC 3.1.1.32 (Phospholipases A)
RN  - EC 3.1.1.4 (Phospholipases A2)
RN  - EC 3.1.4.- (Type C Phospholipases)
RN  - EC 3.1.4.3 (phosphatidylcholine-specific phospholipase C)
RN  - EC 3.1.4.4 (Phospholipase D)
SB  - IM
MH  - 3-Phosphoinositide-Dependent Protein Kinases
MH  - Animals
MH  - Arachidonic Acid/physiology
MH  - Macrophages/metabolism
MH  - Models, Biological
MH  - Models, Chemical
MH  - Phagocytosis/*physiology
MH  - Phospholipase D/metabolism
MH  - Phospholipases/*physiology
MH  - Phospholipases A/metabolism
MH  - Phospholipases A2
MH  - Protein Kinase C/metabolism
MH  - Protein-Serine-Threonine Kinases/metabolism
MH  - Second Messenger Systems/*physiology
MH  - Type C Phospholipases/metabolism
RF  - 108
EDAT- 1999/05/04 00:00
MHDA- 1999/05/04 00:01
CRDT- 1999/05/04 00:00
PHST- 1999/05/04 00:00 [pubmed]
PHST- 1999/05/04 00:01 [medline]
PHST- 1999/05/04 00:00 [entrez]
AID - S1357-2725(98)00108-3 [pii]
AID - 10.1016/s1357-2725(98)00108-3 [doi]
PST - ppublish
SO  - Int J Biochem Cell Biol. 1999 Mar-Apr;31(3-4):415-30. doi:
      10.1016/s1357-2725(98)00108-3.