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J. Biol. Chem., Vol. 280, Issue 32, 29128-29134, August 12, 2005

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A Novel Phospholipase C, PLC2, Is a Neuron-specific Isozyme^*

Masamichi Nakahara, Makoto Shimozawa, Yoshikazu Nakamura, Yasuhiro Irino, Mitsuhiro Morita, Yoshihisa Kudo, and Kiyoko Fukami¶

From the Laboratory of Genome and Biosignal and the Laboratory of Cellular Neurobiology, School of Life Science, Tokyo University of Pharmacy and Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392, Japan

Twelve phospholipase C (PLC) isozymes have been cloned so far, and they are divided into six classes, -, -, -, -, -, and -type, on the basis of structure and activation mechanisms. Here we report the identification of a novel PLC isozyme, PLC2. PLC2 is composed of conserved domains including pleckstrin homology, EF-hand, X and Y catalytic, and C2 domains and the isozyme-specific C-terminal region. PLC2 consists of 1164 amino acids with a molecular mass of 125 kDa. The PLC activity of PLC2 was more sensitive to calcium concentration than the PLC activity of the PLC-type enzyme, which is thought to be the most calcium-sensitive PLC. Immunofluorescence analysis showed that PLC2 was localized predominantly to the plasma membrane at resting state via the pleckstrin homology domain. This observation was supported by Western blot analysis of cytosol and membrane fractions. In addition, expression of PLC2 was detected after birth and showed a restricted distribution in the brain; it was particularly abundant in the hippocampus, cerebral cortex, and olfactory bulb. The pattern was similar to that of the neuronal marker microtubule-associated protein 2 by Western blot. Furthermore, in situ hybridization showed positive signals for PLC2 in pyramidal cells of the hippocampus. Finally, we found that PLC2 was expressed abundantly in neuron-containing primary culture but not in astrocyte-enriched culture. These results indicate that PLC2 is a neuron-specific isozyme that may be important for the formation and/or maintenance of the neuronal network in the postnatal brain.

Received for publication, April 8, 2005 , and in revised form, May 17, 2005.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY966876.

^* This work was supported by a grant-in-aid for general scientific research and a High-Tech Research Center Project for Private Universities matching fund subsidy (2002–2006) from the Japan Ministry of Education, Culture, Sports, Science and Technology. This study was also supported by the Naito Foundation and the Uehara Memorial Foundation. 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.

^¶ To whom correspondence should be addressed. Tel.: 81-426-76-7214; Fax: 81-426-76-7249; E-mail: kfukami{at}ls.toyaku.ac.jp.

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