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Am J Physiol Lung Cell Mol Physiol 288: L1171-L1178, 2005. First published February 25, 2005; doi:10.1152/ajplung.00237.2004
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Expression and localization of diacylglycerol kinase isozymes and enzymatic features in rat lung

Yuji Katagiri,1,2 Tsukasa Ito,1 Sachiko Saino-Saito,1 Yasukazu Hozumi,1 Akira Suwabe,3 Kazuhisa Otake,2 Makoto Sata,2 Hisatake Kondo,4 Fumio Sakane,5 Hideo Kanoh,5 Isao Kubota,2 and Kaoru Goto1

1Department of Anatomy and Cell Biology and 2First Department of Internal Medicine, Yamagata University School of Medicine, Yamagata; 3Department of Laboratory Medicine, Iwate Medical University School of Medicine, Morioka; 4Department of Cell Biology, Division of Histology, Tohoku University Graduate School of Medical Science, Sendai; and 5Department of Biochemistry, Sapporo Medical University School of Medicine, Sapporo, Japan

Submitted 25 June 2004 ; accepted in final form 17 February 2005

Diacylglycerol kinase (DGK) catalyzes phosphorylation of diacylglycerol to generate phosphatidic acid, and both molecules are known to serve as second messengers as well as important intermediates for the synthesis of various lipids. In this study, we investigated the spatiotemporal expression patterns of DGK isozymes together with the developmental changes of the mRNA expression and enzymatic property in rat lung. Northern blot and RT-PCR analyses showed that mRNAs for DGK{alpha}, -{epsilon}, and -{zeta} were detected in the lung. By immunohistochemical examination, DGK{alpha} and -{zeta} were shown to be coexpressed in alveolar type II cells and macrophages. Interestingly, these isozymes were localized at distinct subcellular locations, i.e., DGK{alpha} in the cytoplasm and DGK{zeta} in the nucleus, suggesting different roles for these isozymes. In the developing lung, the expression for DGK{alpha} and -{zeta} was transiently elevated on embryonic day 21 (E21) to levels approximately two- to threefold higher than on postnatal day 0 (P0). On the other hand, the expression for DGK{epsilon} was inversely elevated approximately twofold on P0 compared with that on E21. These unique changes in the expression pattern during the perinatal period suggest that each isozyme may play a distinct role in the adaptation of the lung to air or oxygen breathing at birth.

phosphoinositide; spatiotemporal expression patterns



Address for reprint requests and other correspondence: K. Goto, Dept. of Anatomy and Cell Biology, Yamagata Univ. School of Medicine, Iida-Nishi 2-2-2, Yamagata 990-9585, Japan (E-mail: kgoto{at}med.id.yamagata-u.ac.jp)







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