PMID- 11380253
OWN - NLM
STAT- MEDLINE
DCOM- 20010816
LR  - 20201208
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 40
IP  - 22
DP  - 2001 Jun 5
TI  - Phospholipases stimulate secretion in RBL mast cells.
PG  - 6589-97
AB  - Roles for glycerophospholipids in exocytosis have been proposed, but remain 
      controversial. Phospholipases are stimulated following the activation of the 
      high-affinity receptor for immunoglobulin E (IgE) in mast cells. To study the 
      biochemical sequelae that lead to degranulation, broken cell systems were 
      employed. We demonstrate that the addition of three distinct types of exogenous 
      phospholipases (i.e., bcPLC, scPLD, and tfPLA(2)), all of which hydrolyze 
      phosphatidylcholine (PC), trigger degranulation in permeabilized RBL-2H3 cells, a 
      mucosal mast cell line. Production of bioactive lipids by these phospholipases 
      promotes release of granule contents through the plasma membrane and acts 
      downstream of PKC, PIP(2), and Rho subfamily GTPases in regulated secretion. 
      These exogenous phospholipase-induced degranulation pathways circumvent specific 
      factors activated following stimulation of the IgE receptor as well as in ATP- 
      and GTP-dependent intracellular pathways. Taken together, these results suggest 
      that regulated secretion may be achieved in vitro in the absence of cytosolic 
      factors via phospholipase activation and that products of PC hydrolysis can 
      promote exocytosis in mast cells.
FAU - Cohen, J S
AU  - Cohen JS
AD  - Department of Molecular Medicine, Veterinary Medical Center, and Field of 
      Biochemistry, Molecular and Cellular Biology, Cornell University, Ithaca, New 
      York 14853-6401, USA.
FAU - Brown, H A
AU  - Brown HA
LA  - eng
GR  - GM58516/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Bacterial Proteins)
RN  - 0 (Bacterial Toxins)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Membrane Proteins)
RN  - 0 (Naphthalenes)
RN  - 0 (toxB protein, Clostridium difficile)
RN  - EC 3.1.4.- (Type C Phospholipases)
RN  - EC 3.1.4.4 (Phospholipase D)
RN  - I16QD7X297 (Neomycin)
RN  - I271P23G24 (calphostin C)
SB  - IM
MH  - Animals
MH  - Bacillus cereus/enzymology
MH  - *Bacterial Proteins
MH  - Bacterial Toxins/pharmacology
MH  - Biological Transport
MH  - Cell Degranulation/drug effects
MH  - Cell Membrane/immunology/metabolism
MH  - Clostridioides difficile/physiology
MH  - Cytoplasmic Granules/enzymology/metabolism
MH  - Enzyme Inhibitors/pharmacology
MH  - Immunohistochemistry
MH  - Leukemia, Basophilic, Acute/enzymology/metabolism
MH  - Mast Cells/*enzymology/*metabolism
MH  - Membrane Proteins/immunology/metabolism
MH  - Naphthalenes/pharmacology
MH  - Neomycin/pharmacology
MH  - Phospholipase D/antagonists & inhibitors/*metabolism
MH  - Rats
MH  - Streptomyces/enzymology
MH  - Tumor Cells, Cultured/enzymology/metabolism
MH  - Type C Phospholipases/antagonists & inhibitors/*metabolism
EDAT- 2001/05/31 10:00
MHDA- 2001/08/17 10:01
CRDT- 2001/05/31 10:00
PHST- 2001/05/31 10:00 [pubmed]
PHST- 2001/08/17 10:01 [medline]
PHST- 2001/05/31 10:00 [entrez]
AID - bi0103011 [pii]
AID - 10.1021/bi0103011 [doi]
PST - ppublish
SO  - Biochemistry. 2001 Jun 5;40(22):6589-97. doi: 10.1021/bi0103011.