Downregulation of Phospholipase C δ3 by cAMP and Calcium

Four different isoforms of mammalian phospholipase C δ (PLCδ) have been described. PLCδ1, the best-understood isoform, is activated by an atypical GTP-binding protein. It has been suggested that it is a calcium signal amplifier. However, very less is known about other subtypes, including PLCδ3. Ther...

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Published inBiochemical and biophysical research communications Vol. 286; no. 2; pp. 274 - 280
Main Authors Lin, Fu-Gong, Cheng, Hwei-Fang, Lee, I-Fang, Kao, Hsiao-Jung, Loh, Shih-Hurng, Lee, Wei-Hwa
Format Journal Article
LanguageEnglish
Published Elsevier Inc 17.08.2001
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Summary:Four different isoforms of mammalian phospholipase C δ (PLCδ) have been described. PLCδ1, the best-understood isoform, is activated by an atypical GTP-binding protein. It has been suggested that it is a calcium signal amplifier. However, very less is known about other subtypes, including PLCδ3. Therefore, in the present study, we examined the expression of PLCδ3 in different human tissues. Moreover, the cellular underlying regulation for PLCδ3 was studied in different cell lines. Our study showed that the mRNA and protein levels differed significantly among human tissues. The human PLCδ3 gene was composed of 15 exons and 1 putative cAMP response element in the 5′-end promoter region. PLCδ3 mRNA expression was downregulated by cAMP and calcium in both the human normal embryonic lung tissue diploid WI38 cell line and the glioblastoma/astrocytoma U373 cell line. However, mRNA expression showed no impact by PKC activators or inhibitors. This study shows the human PLCδ3 expression pattern and is the first report that PLCδ3 gene expression is downregulation by cAMP and calcium.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2001.5371