Title

Phospholipase C Activity in Palate Mesenchyme Cells: Calcium and pH Requirements, Substrate Specificity, and Subcellular Localization

Document Type

Article

Publication Date

1-1-1986

Abstract

Primary cultures of mouse embryo palate mesenchyme cells were incubated with [3H]arachidonic acid and [14C]stearic acid in order to radiolabel their lipids. The cells were then washed, collected by centrifugation, and homogenized. Incubation of the homogenates under various conditions revealed that deoxycholate inhibited phospholipase A activity and stimulated a phospholipase C activity in these cells which preferentially degraded phosphatidylinositol (PI) compared to phosphatidylcholine (PC), -ethanolamine (PE), and -serine (PS). Expression of this phospholipase C (E.C. 3.1.4.10) activity was dependent on Ca2+ and had a pH optimum of no more than 7.0-7.5. Centrifugation of the homogenates at 105,000g for 30 min produced a membranous fraction that contained phospholipase C activity with characteristics similar to those of the enzyme found in the supernatant. Such a dual distribution of this enzyme may reflect that mouse embryo palate mesenchyme cells are neural crest in origin.

Publication Title

Journal of Craniofacial Genetics and Developmental Biology

Volume

6

Issue

4

First Page

383

Last Page

392

PubMed ID

3793862

Comments

This article was published in Journal of Craniofacial Genetics and Developmental Biology, Volume 6, Issue 4, Pages 383-392.

Copyright © 1986.

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