PMID- 10531350
OWN - NLM
STAT- MEDLINE
DCOM- 19991216
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 44
DP  - 1999 Oct 29
TI  - Low molecular weight group IIA and group V phospholipase A(2) enzymes have
      different intracellular locations in mouse bone marrow-derived mast cells.
PG  - 31476-84
AB  - The subcellular location of the enzymes of eicosanoid biosynthesis is critical
      for their co-ordinate action in the generation of leukotrienes and
      prostaglandins. This activity is thought to occur predominantly at a perinuclear 
      location. Whereas the subcellular locations of cytosolic phospholipase (PL) A(2) 
      and each of the pathway enzymes of eicosanoid generation have been defined, the
      distribution of the low molecular weight species of PLA(2) has remained elusive
      because of the lack of antibodies that distinguish among homologous family
      members. We have prepared affinity-purified rabbit antipeptide IgG antibodies
      that distinguish mouse group IIA PLA(2) and group V PLA(2). Immunofluorescence
      staining and immunogold electron microscopy reveal different subcellular
      locations for the enzymes. Group IIA(2) PLA(2) is present in the secretory
      granules of mouse bone marrow-derived mast cells, consistent with its putative
      role in facilitating secretory granule exocytosis and its consequent
      extracellular action. In contrast, group V PLA(2) is associated with various
      membranous organelles including the Golgi apparatus, nuclear envelope, and plasma
      membrane. The perinuclear location of group V PLA(2) is consistent with a
      putative interaction with translocated cytosolic PLA(2) in supplying arachidonic 
      acid for generation of eicosanoid products, while the location in Golgi cisternae
      may also reflect its action as a secreted enzyme. The spatial segregation of
      group IIA PLA(2) and group V PLA(2) implies that these enzymes are not
      functionally redundant.
FAU - Bingham, C O 3rd
AU  - Bingham CO 3rd
AD  - Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115, USA.
FAU - Fijneman, R J
AU  - Fijneman RJ
FAU - Friend, D S
AU  - Friend DS
FAU - Goddeau, R P
AU  - Goddeau RP
FAU - Rogers, R A
AU  - Rogers RA
FAU - Austen, K F
AU  - Austen KF
FAU - Arm, J P
AU  - Arm JP
LA  - eng
SI  - GENBANK/AF162712
SI  - GENBANK/AF162713
GR  - AI22531/AI/NIAID NIH HHS/United States
GR  - AI31599/AI/NIAID NIH HHS/United States
GR  - HL36110/HL/NHLBI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - EC 3.1.1.32 (Phospholipases A)
RN  - EC 3.1.1.4 (Group II Phospholipases A2)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Bone Marrow Cells/*enzymology/ultrastructure
MH  - Cell Compartmentation
MH  - Cloning, Molecular
MH  - Fluorescent Antibody Technique
MH  - Group II Phospholipases A2
MH  - Mast Cells/*enzymology/ultrastructure
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C57BL
MH  - Molecular Sequence Data
MH  - Phospholipases A/genetics/*isolation & purification
MH  - Sequence Homology, Amino Acid
EDAT- 1999/10/26 09:00
MHDA- 2001/03/28 10:01
CRDT- 1999/10/26 09:00
PHST- 1999/10/26 09:00 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1999/10/26 09:00 [entrez]
AID - 10.1074/jbc.274.44.31476 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 29;274(44):31476-84. doi: 10.1074/jbc.274.44.31476.