Deoxycholate induces the preferential hydrolysis of polyphosphoinositides by human platelet and rat corneal phospholipase C |
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| Authors: | S M Chung A D Proia G K Klintworth S P Watson E G Lapetina |
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| Affiliation: | 1. Department of Ophthalmology, Duke University Medical Center, Durham, NC 27710 USA;2. Department of Pathology, Duke University Medical Center, Durham, NC 27710 USA;3. Molecular Biology Department, The Wellcome Research Laboratories, Burroughs Wellcome Co., Research Triangle Park, NC 27709 USA;1. Institut des Maladies Métaboliques et Cardiovasculaires (I2MC), INSERM UMR-1297 and Université Paul Sabatier, F-31432, Toulouse, France;2. Laboratoire d’Hématologie, Centre de Référence des Pathologies Plaquettaires, Centre Hospitalier Universitaire de Toulouse Rangueil, F-31432, Toulouse, France;3. Max-Planck Institute for Intelligent Systems, 70569 Stuttgart, Germany,;4. Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany, and;5. Heidelberg University Biochemistry Center, 69120 Heidelberg, Germany |
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| Abstract: | Deoxycholate promotes phospholipase C degradation of endogenous phosphatidyl[3H]inositol (Pl), phosphatidyl[3H]inositol monophosphate (PIP) and phosphatidyl[3H]inositol bisphosphate (PIP2) in rat cornea and human platelets. Hydrolysis of phosphatidyl[3H]inositol significantly lags polyphospho[3H]inositide degradation. Concomitantly, formation of [3H]inositol monophosphate (IP1) lags behind [3H]inositol bisphosphate (IP2) and [3H]inositol trisphosphate (IP3) production. These results demonstrate that rat cornea and human platelet phospholipase C cause a preferential hydrolysis of the endogenous polyphosphoinositides rather than phosphatidylinositol. |
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