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J. Biol. Chem., Vol. 278, Issue 49, 49438-49447, December 5, 2003

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Biochemical and Molecular Characterization of Two Phosphatidic Acid-selective Phospholipase A₁s, mPA-PLA₁ and mPA-PLA₁^*

Tatsufumi Hiramatsu, Hirofumi Sonoda, Yasukazu Takanezawa, Rei Morikawa, Mayuko Ishida¶||, Kohji Kasahara**, Yutaka Sanai, Ryo Taguchi¶||, Junken Aoki¶¶, and Hiroyuki Arai

From the Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan, the ^¶Faculty of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, Aichi 467-0027, Japan, the ^||Department of Metabolome Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan, the ^**Laboratory of Frontier Science, The Tokyo Metropolitan Institute of Medical Science, Tokyo Metropolitan Organization for Medical Research, 3-18-22, Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan, PRESTO, Japan Science and Technology Corporation, and the Department of Biochemical Cell Research, The Tokyo Metropolitan Institute of Medical Science, Tokyo Metropolitan Organization for Medical Research, 3-18-22, Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan

We have identified a novel phospholipase A₁, named mPA-PLA₁, which is specifically expressed in human testis and characterized it biochemically together with previously identified mPA-PLA₁. The sequence of mPAPLA₁ encodes a 460-amino acid protein containing a lipase domain with significant homology to the previously identified phosphatidic acid (PA)-selective PLA₁, mPA-PLA₁. mPA-PLA₁ contains a short lid and deleted 9 loop, which are characteristics of PLA₁ molecules in the lipase family, and is a member of a subfamily in the lipase family that includes mPA-PLA₁ and phosphatidylserine-specific PLA₁. Both mPA-PLA₁ and mPA-PLA₁ recombinant proteins exhibited PA-specific PLA₁ activity and were vanadate-sensitive. When mPAPLA₁-expressing cells were treated with bacterial phospholipase D, the cells produced lysophosphatidic acid (LPA). In both mPA-PLA₁ and -expressing cells, most of the PA generated by the phospholipase D (PLD) treatment was converted to LPA, whereas in control cells it was converted to diacylglycerol. When expressed in HeLa cells most mPA-PLA₁ protein was recovered from the cell supernatant. By contrast, mPA-PLA₁ was recovered almost exclusively from cells. Consistent with this observation, we found that mPA-PLA₁ has higher affinity to heparin than mPA-PLA₁. We also found that the membrane-associated mPA-PLA₁s were insoluble in solubilization by 1% Triton X-100 and were detected in Triton X-100-insoluble buoyant fractions of sucrose gradients. The present study raises the possibility that production of LPA by mPA-PLA₁ and - occurs on detergent-resistant membrane domains of the cells where they compete with lipid phosphate phosphatase for PA.

Received for publication, December 20, 2002 , and in revised form, September 2, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY197607 for human mPA-PLA₁.

^* This work was supported in part by research grants from the Ministry of Education, Science, Sports, and Culture of Japan, by special coordination funds from the Science and Technology Agency of the Japanese Government, and the Human Frontier Special Program. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to the results of this work.

^¶¶ To whom correspondence should be addressed. E-mail: jaoki{at}mol.f.u-tokyo.ac.jp.

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