Deoxycholateinduces the preferential hydrolysis of polyphosphoinositides by human platelet and rat corneal phospholipase C

S. M. Chung; Alan Proia; G. K. Klintworth; S. P. Watson; E. G. Lapetina

doi:10.1016/0006-291X(85)90166-4

Deoxycholateinduces the preferential hydrolysis of polyphosphoinositides by human platelet and rat corneal phospholipase C

S. M. Chung, Alan Proia, G. K. Klintworth, S. P. Watson, E. G. Lapetina

Campbell University

Research output: Contribution to journal › Article › peer-review

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.

Original language	American English
Journal	Biochemical and Biophysical Research Communications
Volume	129
DOIs	https://doi.org/10.1016/0006-291X(85)90166-4
State	Published - Jun 14 1985

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title = "Deoxycholateinduces the preferential hydrolysis of polyphosphoinositides by human platelet and rat corneal phospholipase C",

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.",

author = "Chung, {S. M.} and Alan Proia and Klintworth, {G. K.} and Watson, {S. P.} and Lapetina, {E. G.}",

year = "1985",

month = jun,

day = "14",

doi = "10.1016/0006-291X(85)90166-4",

language = "American English",

volume = "129",

journal = "Biochemical and Biophysical Research Communications",

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TY - JOUR

T1 - Deoxycholateinduces the preferential hydrolysis of polyphosphoinositides by human platelet and rat corneal phospholipase C

AU - Chung, S. M.

AU - Proia, Alan

AU - Klintworth, G. K.

AU - Watson, S. P.

AU - Lapetina, E. G.

PY - 1985/6/14

Y1 - 1985/6/14

N2 - 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.

AB - 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.

UR - https://cufind.campbell.edu/medicine_school/520

UR - https://doi.org/10.1016/0006-291X(85)90166-4

U2 - 10.1016/0006-291X(85)90166-4

DO - 10.1016/0006-291X(85)90166-4

M3 - Article

VL - 129

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

ER -

Deoxycholateinduces the preferential hydrolysis of polyphosphoinositides by human platelet and rat corneal phospholipase C

Abstract

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