PMID- 10383420
OWN - NLM
STAT- MEDLINE
DCOM- 19990727
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 27
DP  - 1999 Jul 2
TI  - Cloning and recombinant expression of a novel mouse-secreted phospholipase A2.
PG  - 19152-60
AB  - Secreted phospholipases A2 (sPLA2s) form a class of structurally related enzymes 
      that are involved in a variety of physiological and pathological effects
      including inflammation and associated diseases, cell proliferation, cell
      adhesion, and cancer, and are now known to bind to specific membrane receptors.
      Here, we report the cloning and expression of a novel sPLA2 isolated from mouse
      thymus. Based on its structural features, this sPLA2 is most similar to the
      previously cloned mouse group IIA sPLA2 (mGIIA sPLA2). As for mGIIA sPLA2, the
      novel sPLA2 is made up of 125 amino acids with 14 cysteines, is basic (pI = 8.71)
      and its gene has been mapped to mouse chromosome 4. However, the novel sPLA2 has 
      only 48% identity with mGIIA and displays similar levels of identity with the
      other mouse group IIC and V sPLA2s, indicating that the novel sPLA2 is not an
      isoform of mGIIA sPLA2. This novel sPLA2 has thus been called mouse group IID
      (mGIID) sPLA2. In further contrast with mGIIA, which is found mainly in
      intestine, transcripts coding for mGIID sPLA2 are found in several tissues
      including pancreas, spleen, thymus, skin, lung, and ovary, suggesting distinct
      functions for the two enzymes. Recombinant expression of mGIID sPLA2 in
      Escherichia coli indicates that the cloned sPLA2 is an active enzyme that has
      much lower specific activity than mGIIA and displays a distinct specificity for
      binding to various phospholipid vesicles. Finally, recombinant mGIID sPLA2 did
      not bind to the mouse M-type sPLA2 receptor, while mGIIA was previously found to 
      bind to this receptor with high affinity.
FAU - Valentin, E
AU  - Valentin E
AD  - Institut de Pharmacologie Moleculaire et Cellulaire, CNRS, UPR 411, 660 route des
      Lucioles, Sophia Antipolis, 06560 Valbonne, France.
FAU - Koduri, R S
AU  - Koduri RS
FAU - Scimeca, J C
AU  - Scimeca JC
FAU - Carle, G
AU  - Carle G
FAU - Gelb, M H
AU  - Gelb MH
FAU - Lazdunski, M
AU  - Lazdunski M
FAU - Lambeau, G
AU  - Lambeau G
LA  - eng
SI  - GENBANK/AF124374
GR  - HL36235/HL/NHLBI 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.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Recombinant Proteins)
RN  - EC 3.1.1.32 (Phospholipases A)
RN  - EC 3.1.1.4 (Group II Phospholipases A2)
RN  - EC 3.1.1.4 (Phospholipases A2)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - CHO Cells
MH  - Calcium/metabolism
MH  - Cloning, Molecular
MH  - Cricetinae
MH  - Group II Phospholipases A2
MH  - Kinetics
MH  - Mice
MH  - Molecular Sequence Data
MH  - Open Reading Frames
MH  - Phospholipases A/*genetics/metabolism
MH  - Phospholipases A2
MH  - Recombinant Proteins/metabolism
MH  - Sequence Alignment
EDAT- 1999/06/26 00:00
MHDA- 1999/06/26 00:01
CRDT- 1999/06/26 00:00
PHST- 1999/06/26 00:00 [pubmed]
PHST- 1999/06/26 00:01 [medline]
PHST- 1999/06/26 00:00 [entrez]
AID - 10.1074/jbc.274.27.19152 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Jul 2;274(27):19152-60. doi: 10.1074/jbc.274.27.19152.