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Cloning and identification of the human LPAAT-zeta gene, a novel member of the lysophosphatidic acid acyltransferase family.

作者信息

Li Dan, Yu Long, Wu Hai, Shan Yuxi, Guo Jinhu, Dang Yongjun, Wei Youheng, Zhao Shouyuan

机构信息

State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University, 200433, Shanghai, P.R. China.

Institute of Genetics, Fudan University, 220 Handan Road, 200433, Shanghai, P.R. China.

出版信息

J Hum Genet. 2003;48(8):438-442. doi: 10.1007/s10038-003-0045-z. Epub 2003 Aug 19.

DOI:10.1007/s10038-003-0045-z
PMID:12938015
Abstract

Lysophosphatidic acid (LPA) is a naturally occurring component of phospholipid and plays a critical role in the regulation of many physiological and pathophysiological processes including cell growth, survival, and pro-angiogenesis. LPA is converted to phosphatidic acid by the action of lysophosphatidic acid acyltransferase (LPAAT). Five members of the LPAAT gene family have been detected in humans to date. Here, we report the identification of a novel LPAAT member, which is designated as LPAAT-zeta. LPAAT-zeta was predicted to encode a protein consisting of 456 amino acid residues with a signal peptide sequence and the acyltransferase domain. Northern blot analysis showed that LPAAT-zeta was ubiquitously expressed in all 16 human tissues examined, with levels in the skeletal muscle, heart, and testis being relatively high and in the lung being relatively low. The human LPAAT-zeta gene consisted of 13 exons and is positioned at chromosome 8p11.21.

摘要

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A conserved histidine is essential for glycerolipid acyltransferase catalysis.一个保守的组氨酸对于甘油脂酰基转移酶催化作用至关重要。
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