Work

Phospholipase C-mediated hydrolysis of phosphatidylcholine is activated by muscarinic agonists

Year: 1989

Type: article

Abstract: The phospholipase C-catalysed breakdown of inositol-containing phospholipids is an important source of diacylglycerol in cells stimulated by several agonists. However, recent experimental evidence suggests that major phospholipids such as phosphatidylcholine may also be substrates of the phosphodiesteratic hydrolysis activated by hormones, growth factors and oncogene products. We show here that stimulation of muscarinic agonists activates the release of phosphocholine, which, along with diacylglycerol, is a metabolic product of phospholipase C-mediated hydrolysis of phosphatidylcholine. Fluoroaluminates mimic this muscarinic effect, strongly suggesting that carbachol-activated release of phosphocholine may be mediated by a guanine-nucleotide-binding protein. Evidence for this was obtained from experiments using permeabilized cells in which non-hydrolysable analogues of GTP activated phosphocholine release synergistically with carbachol.

Source: Biochemical Journal

DOI: 10.1042/bj2630115

Authors: M T Diaz-Meco, P Larrodera, M Lopez-Barahona, M E Cornet, P G Barreno, J Moscat

Institution: Hospital General Universitario Gregorio Marañón

Language: English

Topic: Protein Kinase Regulation and GTPase Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funder: Comunidad de Madrid

OpenAlex ID: W2328589028