PMID- 10506173
OWN - NLM
STAT- MEDLINE
DCOM- 19991109
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 41
DP  - 1999 Oct 8
TI  - Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that is
      involved in the regulation of mitochondrial lipid biosynthesis.
PG  - 29172-80
AB  - In this study, we isolated cDNA encoding lysophosphatidic acid (LPA) phosphatase 
      (LPAP). The amino acid sequence deduced from the cDNA encoding LPAP had 421
      residues including a putative signal peptide and was homologous to acid
      phosphatase, especially at the active site. Human LPAP had 28.5% amino acid
      identity to human prostatic acid phosphatase. Northern blot analysis showed a
      ubiquitous expression of LPAP, which was marked in kidney, heart, small
      intestine, muscle, and liver. Human chromosome map obtained by fluorescence in
      situ hybridazation showed that the gene for LPAP was localized to chromosome 1
      q21. The mutant in which histidine was replaced with alanine at the active site
      and the putative signal peptide-deleted LPAP had no LPA phosphatase activity. In 
      addition, the putative signal peptide-deleted LPAP showed no mitochondrial
      localization. The site of intracellular localization of endogenous LPAP was also 
      mitochondria in MDCK cells and differentiated C2C12 cells. The LPAP homologous
      phosphatase, human prostatic acid phosphatase, also has LPA phosphatase activity.
      LPAP-stable transfected NIH 3T3 cells showed less phosphatidic acid,
      phosphatidylglycerol, and cardiolipin. These results suggested that LPAP
      regulates lipid metabolism in mitochondria via the hydrolysis of LPA to
      monoacylglycerol.
FAU - Hiroyama, M
AU  - Hiroyama M
AD  - Department of Biochemistry, Institute of Medical Science, University of Tokyo,
      4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
FAU - Takenawa, T
AU  - Takenawa T
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Lipids)
RN  - 0 (Lysophospholipids)
RN  - 0 (Protein Sorting Signals)
RN  - 0 (RNA, Messenger)
RN  - EC 3.1.3.- (lysophosphatidic acid phosphatase)
RN  - EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - Brain/enzymology
MH  - Cell Line
MH  - Chromosomes, Human, Pair 1/genetics
MH  - Cloning, Molecular
MH  - Humans
MH  - In Situ Hybridization, Fluorescence
MH  - Lipids/*biosynthesis
MH  - Lysophospholipids/metabolism
MH  - Male
MH  - Mitochondria/*enzymology
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Phosphoric Monoester Hydrolases/chemistry/*genetics
MH  - Protein Sorting Signals/genetics
MH  - RNA, Messenger/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Tumor Cells, Cultured
EDAT- 1999/10/03 00:00
MHDA- 1999/10/03 00:01
CRDT- 1999/10/03 00:00
PHST- 1999/10/03 00:00 [pubmed]
PHST- 1999/10/03 00:01 [medline]
PHST- 1999/10/03 00:00 [entrez]
AID - 10.1074/jbc.274.41.29172 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 8;274(41):29172-80. doi: 10.1074/jbc.274.41.29172.