The hydrolysis of phosphatidylinositol 4-phosphate in membranes of Xenopus laevis oocytes: Characteristics of a phosphomonoesterase

Autor: Jorge E. Allende, Catherine C. Allende, Germaine Jacob
Rok vydání: 1991
Předmět:
Zdroj: Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 100:809-816
ISSN: 0305-0491
DOI: 10.1016/0305-0491(91)90295-o
Popis: 1. 1. Phosphatidylinositol 4-phosphate (PtdIns4P) is degraded by isolated membranes from Xenopus laevis oocytes. 2. 2. Incubation of [4- 32 P]PtdIns4P with membranes yields only radioactive inorganic phosphate, indicating the presence of a phosphomonoesterase. 3. 3. Membranes hydrolyze Ptd[2- 3 H]Ins4P to produce mainly Ptd[2- 3 H]Ins in the lipid phase. In this incubation [ 3 H]inositol and inositol monophosphate appear in the water phase. 4. 4. Membrane incubations of Ptd[2- 3 H]Ins4P carried out in the presence of excess non-radioactive Ins(1,4)P 2 allows the trapping of small amounts of [ 3 H]Ins(1,4)P 2 . These results demonstrate the presence of a phospholipase C. 5. 5. Testing several phosphorylated analogs, it is determined that fructose 1,6-bisphosphate and α-glycerophosphate are potent inhibitors of the oocyte PtdIns4P phosphomonoesterase.
Databáze: OpenAIRE