PLC-¦Ä1-Lf, a novel N-terminal extended phospholipase C-¦Ä1
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- 作者：Na Young Kim ; Sang Jung Ahn ; Moo-Sang Kim ; Jung Soo Seo ; Bo Seong Kim ; Hye Jin Bak ; Jin Young Lee ; Myoung-Ae Park ; Ju Hyeon Park ; Hyung Ho Lee ; Joon Ki Chung
- 关键词：RT-PCR ; reverse transcription polymerase chain reaction ; SDS&ndash ; PAGE ; sodium dodecyl sulfate polyacrylamide gel electrophoresis ; cDNA ; DNA complementary to RNA
- 刊名：Gene
- 出版年：2013
- 出版时间：10 October, 2013
- 年：2013
- 卷：528
- 期：2
- 页码：170-177
- 全文大小：1380 K
文摘
Phospholipase C-¦Ä (PLC-¦Ä), a key enzyme in phosphoinositide turnover, is involved in a variety of physiological functions. The widely expressed PLC-¦Ä1 isoform is the best characterized and the most well understood phospholipase family member. However, the functional and molecular mechanisms of PLC-¦Ä1 remain obscure. Here, we identified that the N-terminal region of mouse PLC-¦Ä1 gene has two variants, a novel alternative splicing form, named as long form (mPLC-¦Ä1-Lf) and the previously reported short form (mPLC-¦Ä1-Sf), having exon 2 and exon 1, respectively, while both the gene variants share exons 3-16 for RNA transcription. Furthermore, the expression, identification and enzymatic characterization of the two types of PLC-¦Ä1 genes were compared. Expression of mPLC-¦Ä1-Lf was found to be tissue specific, whereas mPLC-¦Ä1-Sf was widely distributed. The recombinant mPLC-¦Ä1-Sf protein exhibited higher activity than recombinant mPLC-¦Ä1-Lf protein. Although, the general catalytic and regulatory properties of mPLC-¦Ä1-Lf are similar to those of PLC-¦Ä1-Sf isozyme, the mPLC-¦Ä1-Lf showed some distinct regulatory properties, such as tissue-specific expression and lipid binding specificity, particularly for phosphatidylserine.