作者: Myung Jong Kim , Do Sik Min , Sung Ho Ryu , Pann-Ghill Suh
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摘要: Abstract Phospholipase C (PLC)-β4 has been considered to be a mammalian homolog of the NorpA PLC, which is responsible for visual signal transduction in Drosophila.We reported previously cloning cDNA encoding rat phospholipase C-β4 (PLC-β4) (Kim, M. J., Bahk, Y. Y., Min, D. S., Lee, S. Ryu, H., and Suh, P.-G. (1993) Biochem. Biophys. Res. Commun. 194, 706–712). We report now isolation characterization splice variant (PLC-β4b). PLC-β4b identical 130-kDa PLC-β4 (PLC-β4a) except that carboxyl-terminal 162 amino acids PLC-β4a are replaced by 10 distinct acids. The existence transcripts brain was demonstrated reverse transcription-polymerase chain reaction analysis. Immunological analysis using polyclonal antibody specific revealed this exists cytosol. To investigate functional differences between two forms PLC-β4, transient expression studies COS-7 cells were conducted. found localized mainly particulate fraction cell, it could activated Gαq, whereas exclusively soluble fraction, not Gαq. In addition, both G-protein βγ-subunits purified from brain. These results suggest may regulated mechanism different PLC-β4a, therefore play role PLC-mediated transduction.