PMID- 10531313
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  - On the diversity of secreted phospholipases A(2). Cloning, tissue distribution,
      and functional expression of two novel mouse group II enzymes.
PG  - 31195-202
AB  - Over the last decade, an expanding diversity of secreted phospholipases A(2)
      (sPLA(2)s) has been identified in mammals. Here, we report the cloning in mice of
      three additional sPLA(2)s called mouse group IIE (mGIIE), IIF (mGIIF), and X
      (mGX) sPLA(2)s, thus giving rise to eight distinct sPLA(2)s in this species. Both
      mGIIE and mGIIF sPLA(2)s contain the typical cysteines of group II sPLA(2)s, but 
      have relatively low levels of identity (less than 51%) with other mouse sPLA(2)s,
      indicating that these enzymes are novel group II sPLA(2)s. However, a unique
      feature of mGIIF sPLA(2) is the presence of a C-terminal extension of 23 amino
      acids containing a single cysteine. mGX sPLA(2) has 72% identity with the
      previously cloned human group X (hGX) sPLA(2) and displays similar structural
      features, making it likely that mGX sPLA(2) is the ortholog of hGX sPLA(2). Genes
      for mGIIE and mGIIF sPLA(2)s are located on chromosome 4, and that of mGX sPLA(2)
      on chromosome 16. Northern and dot blot experiments with 22 tissues indicate that
      all eight mouse sPLA(2)s have different tissue distributions, suggesting specific
      functions for each. mGIIE sPLA(2) is highly expressed in uterus, and at lower
      levels in various other tissues. mGIIF sPLA(2) is strongly expressed during
      embryogenesis and in adult testis. mGX sPLA(2) is mostly expressed in adult
      testis and stomach. When the cDNAs for the eight mouse sPLA(2)s were transiently 
      transfected in COS cells, sPLA(2) activity was found to accumulate in cell
      medium, indicating that each enzyme is secreted and catalytically active. Using
      COS cell medium as a source of enzymes, pH rate profile and phospholipid
      headgroup specificity of the novel sPLA(2)s were analyzed and compared with the
      other mouse sPLA(2)s.
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 - Ghomashchi, F
AU  - Ghomashchi F
FAU - Gelb, M H
AU  - Gelb MH
FAU - Lazdunski, M
AU  - Lazdunski M
FAU - Lambeau, G
AU  - Lambeau G
LA  - eng
SI  - GENBANK/AF166097
SI  - GENBANK/AF166098
SI  - GENBANK/AF166099
SI  - GENBANK/AF166100
GR  - HL36235/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  - 0 (Phospholipids)
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 (Group X Phospholipases A2)
RN  - EC 3.1.1.4 (PLA2G10 protein, human)
RN  - EC 3.1.1.4 (Pla2g10 protein, mouse)
SB  - IM
EIN - J Biol Chem 2000 Jan 21;275(3):2246
MH  - Amino Acid Sequence
MH  - Animals
MH  - Bodily Secretions
MH  - Chromosome Mapping
MH  - Cloning, Molecular
MH  - Evolution, Molecular
MH  - *Genetic Variation
MH  - Group II Phospholipases A2
MH  - Group X Phospholipases A2
MH  - Hydrogen-Ion Concentration
MH  - Kinetics
MH  - Mice
MH  - Molecular Sequence Data
MH  - Phospholipases A/biosynthesis/classification/*genetics
MH  - Phospholipids/metabolism
MH  - Recombinant Proteins/biosynthesis
MH  - Sequence Homology, Amino Acid
MH  - Tissue Distribution
EDAT- 1999/10/26 09:00
MHDA- 2000/03/11 09:00
CRDT- 1999/10/26 09:00
PHST- 1999/10/26 09:00 [pubmed]
PHST- 2000/03/11 09:00 [medline]
PHST- 1999/10/26 09:00 [entrez]
AID - 10.1074/jbc.274.44.31195 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 29;274(44):31195-202. doi: 10.1074/jbc.274.44.31195.