Journal article
Deoxycholateinduces the preferential hydrolysis of polyphosphoinositides by human platelet and rat corneal phospholipase C
Biochemical and biophysical research communications, Vol.129(2), pp.411-416
1985
DOI: 10.1016/0006-291X(85)90166-4
Abstract
Deoxycholate promotes phospholipase C degradation of endogenous phosphatidyl[
3H]inositol (PI), 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.
Details
- Title: Subtitle
- Deoxycholateinduces the preferential hydrolysis of polyphosphoinositides by human platelet and rat corneal phospholipase C
- Creators
- S.M Chung - Department of Ophthalmology, Duke University Medical Center, Durham, NC 27710 USAA.D Proia - Department of Ophthalmology, Duke University Medical Center, Durham, NC 27710 USAG.K Klintworth - Department of Ophthalmology, Duke University Medical Center, Durham, NC 27710 USAS.P Watson - Molecular Biology Department, The Wellcome Research Laboratories, Burroughs Wellcome Co., Research Triangle Park, NC 27709 USAE.G Lapetina - Molecular Biology Department, The Wellcome Research Laboratories, Burroughs Wellcome Co., Research Triangle Park, NC 27709 USA
- Resource Type
- Journal article
- Publication Details
- Biochemical and biophysical research communications, Vol.129(2), pp.411-416
- Publisher
- Elsevier Inc
- DOI
- 10.1016/0006-291X(85)90166-4
- ISSN
- 0006-291X
- eISSN
- 1090-2104
- Language
- English
- Date published
- 1985
- Academic Unit
- Neurology; Ophthalmology and Visual Sciences
- Record Identifier
- 9984111987602771
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