PMID- 10196188
OWN - NLM
STAT- MEDLINE
DCOM- 19990517
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 16
DP  - 1999 Apr 16
TI  - An alternative splicing form of phosphatidylserine-specific phospholipase A1 that
      exhibits lysophosphatidylserine-specific lysophospholipase activity in humans.
PG  - 11053-9
AB  - Phosphatidylserine-specific phospholipase A1 (PS-PLA1), which acts specifically
      on phosphatidylserine (PS) and 1-acyl-2-lysophosphatidylserine (lyso-PS) to
      hydrolyze fatty acids at the sn-1 position of these phospholipids, was first
      identified in rat platelets (Sato, T., Aoki, J., Nagai, Y., Dohmae, N., Takio,
      K., Doi, T., Arai, H., and Inoue, K. (1997) J. Biol. Chem. 272, 2192-2198). In
      this study we isolated and sequenced cDNA clones encoding human PS-PLA1, which
      showed 80% homology with rat PS-PLA1 at the amino acid level. In addition to an
      mRNA encoding a 456-amino acid product (PS-PLA1), an mRNA with four extra bases
      inserted at the boundary of the exon-intron junction was detected in human
      tissues and various human cell lines. This mRNA is most probably produced via an 
      alternative use of the 5'-splicing site (two consensus sequences for RNA splicing
      occur at the boundary of the exon-intron junction) and encodes a 376-amino acid
      product (PS-PLA1DeltaC) that lacks two-thirds of the C-terminal domain of
      PS-PLA1. Unlike PS-PLA1, PS-PLA1DeltaC hydrolyzed exclusively lyso-PS but not PS 
      appreciably. Any other phospholipids such as phosphatidylcholine (PC),
      phosphatidylethanolamine (PE), phosphatidic acid (PA), and their lyso derivatives
      were not hydrolyzed at all. These data demonstrated that PS-PLA1DeltaC exhibits
      lyso-PS-specific lysophospholipase activity and that the C-terminal domain of
      PS-PLA1 is responsible for recognizing diacylphospholipids. In addition, human
      PS-PLA1 gene was mapped to chromosome 3q13.13-13.2 and was unexpectedly identical
      to the nmd gene, which is highly expressed in nonmetastatic melanoma cell lines
      but poorly expressed in metastatic cell lines (van Groningen, J. J., Bloemers, H.
      P., and Swart, G. W. (1995) Cancer Res. 55, 6237-6243).
FAU - Nagai, Y
AU  - Nagai Y
AD  - Department of Health Chemistry, Graduate School of Pharmaceutical Sciences, The
      University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
FAU - Aoki, J
AU  - Aoki J
FAU - Sato, T
AU  - Sato T
FAU - Amano, K
AU  - Amano K
FAU - Matsuda, Y
AU  - Matsuda Y
FAU - Arai, H
AU  - Arai H
FAU - Inoue, K
AU  - Inoue K
LA  - eng
SI  - GENBANK/AF035268
SI  - GENBANK/AF035269
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (Isoenzymes)
RN  - 0 (Lysophospholipids)
RN  - 0 (Phosphatidylserines)
RN  - 0 (lysophosphatidylserine)
RN  - EC 3.1.1.32 (Phospholipases A)
RN  - EC 3.1.1.32 (Phospholipases A1)
RN  - EC 3.1.1.5 (Lysophospholipase)
SB  - IM
MH  - *Alternative Splicing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cell Line
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Humans
MH  - Isoenzymes/*genetics/metabolism
MH  - Lysophospholipase/*metabolism
MH  - Lysophospholipids/*metabolism
MH  - Molecular Sequence Data
MH  - Phosphatidylserines/*metabolism
MH  - Phospholipases A/*genetics/metabolism
MH  - Phospholipases A1
MH  - Rats
EDAT- 1999/04/10 00:00
MHDA- 1999/04/10 00:01
CRDT- 1999/04/10 00:00
PHST- 1999/04/10 00:00 [pubmed]
PHST- 1999/04/10 00:01 [medline]
PHST- 1999/04/10 00:00 [entrez]
AID - 10.1074/jbc.274.16.11053 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 16;274(16):11053-9. doi: 10.1074/jbc.274.16.11053.