Molecular cloning and characterization of a cDNA for bovine phospholipase C-alpha: proposal of redesignation of phospholipase C-alpha.

Abstract We have isolated bovine phospholipase C (PLC)-α cDNA from bovine thymus. Sequence analysis showed that PLC-α is highly conserved among rat, mouse, and calf and that it has two Trp-Cys-Gly-His-Cys-Lys motifs completely conserved in the mammals. Southern blot analysis revealed that bovine PLC-α is derived from a single gene. When PLC-α cDNA was stably transfected in NIH3T3 cells, there was no increase in PLC activity. PLC-α is supposed to be a member not of PLC superfamily but of Trp-Cys-Gly-His-Cys-Lys motif-containing proteins consisting of protein disulfide isomerase, P5, ERp72, and thioredoxin. PLC-α should be redesignated ERp57 ( ER -resided p57 ).