TY - JOUR
T1 - A novel intracellular membrane-bound calcium-independent phospholipase A2
AU - Tanaka, Haruki
AU - Takeya, Ryu
AU - Sumimoto, Hideki
N1 - Funding Information:
We thank Professor Takashi Ito (Cancer Research Institute, Ka-nazawa University) for helpful discussion and encouragement. This work was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture of Japan and by Kyushu University Interdisciplinary Programs in Education and Projects in Research Development. Part of this study was performed in the Kyushu University Station for Collaborative Research.
PY - 2000/6/7
Y1 - 2000/6/7
N2 - We have cloned human cDNA encoding a novel protein of 782 amino acids that contains the lipase consensus sequence Gly-Xaa-Ser-Xaa-Gly and several stretches surrounding the motif, which are homologous to those of the catalytic domain of cytosolic calcium-independent phospholipase A2 (iPLA2). When expressed in COS-7 cells, the protein predominantly exists in the membrane fraction and exhibits a phospholipase A2 activity in a calcium-independent manner. The transcript of the membrane-bound iPLA2 gene is ubiquitously observed as a single band of approximately 3.3 kb on Northern blot, with the most abundant expression in the skeletal muscle and heart. By a search of the database, we have also identified its putative C. elegans homologue, which shows 47% identity with that of human in the iPLA2 catalytic region. Thus the novel type of iPLA2 is evolutionarily well conserved, suggestive of its biological significance. (C) 2000 Academic Press.
AB - We have cloned human cDNA encoding a novel protein of 782 amino acids that contains the lipase consensus sequence Gly-Xaa-Ser-Xaa-Gly and several stretches surrounding the motif, which are homologous to those of the catalytic domain of cytosolic calcium-independent phospholipase A2 (iPLA2). When expressed in COS-7 cells, the protein predominantly exists in the membrane fraction and exhibits a phospholipase A2 activity in a calcium-independent manner. The transcript of the membrane-bound iPLA2 gene is ubiquitously observed as a single band of approximately 3.3 kb on Northern blot, with the most abundant expression in the skeletal muscle and heart. By a search of the database, we have also identified its putative C. elegans homologue, which shows 47% identity with that of human in the iPLA2 catalytic region. Thus the novel type of iPLA2 is evolutionarily well conserved, suggestive of its biological significance. (C) 2000 Academic Press.
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U2 - 10.1006/bbrc.2000.2776
DO - 10.1006/bbrc.2000.2776
M3 - Article
C2 - 10833412
AN - SCOPUS:0034616686
VL - 272
SP - 320
EP - 326
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -