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

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Citation

Hirano N, Shibasaki F, Kato H, Sakai R, Tanaka T, Nishida J, Yazaki Y, Takenawa T, Hirai H

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

Biochem Biophys Res Commun. 1994 Oct 14;204(1):375-82.

PubMed ID
7945384 [ View in PubMed
]
Abstract

We have isolated bovine phospholipase C (PLC)-alpha cDNA from bovine thymus. Sequence analysis showed that PLC-alpha 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-alpha is derived from a single gene. When PLC-alpha cDNA was stably transfected in NIH3T3 cells, there was no increase in PLC activity. PLC-alpha 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-alpha should be redesignated ERp57 (ER-resided p57).

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Protein disulfide-isomerase A3P30101Details