| First Author | Kim NY | Year | 2013 |
| Journal | Gene | Volume | 528 |
| Issue | 2 | Pages | 170-7 |
| PubMed ID | 23892088 | Mgi Jnum | J:202624 |
| Mgi Id | MGI:5520128 | Doi | 10.1016/j.gene.2013.07.022 |
| Citation | Kim NY, et al. (2013) PLC-delta1-Lf, a novel N-terminal extended phospholipase C-delta1. Gene 528(2):170-7 |
| abstractText | Phospholipase C-delta (PLC-delta), a key enzyme in phosphoinositide turnover, is involved in a variety of physiological functions. The widely expressed PLC-delta1 isoform is the best characterized and the most well understood phospholipase family member. However, the functional and molecular mechanisms of PLC-delta1 remain obscure. Here, we identified that the N-terminal region of mouse PLC-delta1 gene has two variants, a novel alternative splicing form, named as long form (mPLC-delta1-Lf) and the previously reported short form (mPLC-delta1-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-delta1 genes were compared. Expression of mPLC-delta1-Lf was found to be tissue specific, whereas mPLC-delta1-Sf was widely distributed. The recombinant mPLC-delta1-Sf protein exhibited higher activity than recombinant mPLC-delta1-Lf protein. Although, the general catalytic and regulatory properties of mPLC-delta1-Lf are similar to those of PLC-delta1-Sf isozyme, the mPLC-delta1-Lf showed some distinct regulatory properties, such as tissue-specific expression and lipid binding specificity, particularly for phosphatidylserine. |
