Regulation of platelet-activating factor synthesis by acetyl-coenzyme A

C. Tetta, G. Camussi, F. Bussolino, C. Baglioni

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Human neutrophils (PMN) stimulated by tumor necrosis factor (TNF) synthesize and release platelet-activating factor (PAF) transiently. In the present investigation, we have examined the mechanism responsible for the down-regulation of PAF synthesis. The response of PMN is proportional to the occupancy of high-affinity TNF receptors on the PMN plasma membrane, as shown by binding assays with [125]TNF. These receptors are down-regulated within 10 min of the addition of TNF; the receptors reappear after 60 min, but the PMN do not resume PAF synthesis. Further PAF synthesis is obtained by adding acetyl-coenzyme A (CoA) to the culture medium. However, this compound does not diffuse into PMN, as shown by incubating these cells with labeled acetyl-CoA. This finding suggests that PAF synthesis is regulated by the amount of acetyl-CoA available to the lyso-PAF: acetyltransferase on the cell plasma membrane. This acetyl-CoA is accessible to chemicals in the culture mdium, since it is hydrolysed by hydroxylamine. The inhibition of PAF synthesis by hydroxylamine is reversed by adding acetyl-CoA. PAF synthesis in TNF-treated cells appears to be regulated either by the amount of acetyl-CoA available or by the ability to transfer acetyl-CoA from the cellular pool to the lyso-PAF: acetyltransferase.

Original languageEnglish
JournalJournal of Lipid Mediators
Volume2
Issue numberSUPPL.
Publication statusPublished - 1990

Fingerprint

Acetyl Coenzyme A
Platelet Activating Factor
Hydroxylamine
Acetyltransferases
Tumor Necrosis Factor-alpha
Tumor Necrosis Factor Receptors
Cell Membrane
Culture Media
Neutrophils
Down-Regulation

ASJC Scopus subject areas

  • Immunology
  • Pharmacology

Cite this

Regulation of platelet-activating factor synthesis by acetyl-coenzyme A. / Tetta, C.; Camussi, G.; Bussolino, F.; Baglioni, C.

In: Journal of Lipid Mediators, Vol. 2, No. SUPPL., 1990.

Research output: Contribution to journalArticle

@article{21934c00ed3b4df080fe879df2c4ff6b,
title = "Regulation of platelet-activating factor synthesis by acetyl-coenzyme A",
abstract = "Human neutrophils (PMN) stimulated by tumor necrosis factor (TNF) synthesize and release platelet-activating factor (PAF) transiently. In the present investigation, we have examined the mechanism responsible for the down-regulation of PAF synthesis. The response of PMN is proportional to the occupancy of high-affinity TNF receptors on the PMN plasma membrane, as shown by binding assays with [125]TNF. These receptors are down-regulated within 10 min of the addition of TNF; the receptors reappear after 60 min, but the PMN do not resume PAF synthesis. Further PAF synthesis is obtained by adding acetyl-coenzyme A (CoA) to the culture medium. However, this compound does not diffuse into PMN, as shown by incubating these cells with labeled acetyl-CoA. This finding suggests that PAF synthesis is regulated by the amount of acetyl-CoA available to the lyso-PAF: acetyltransferase on the cell plasma membrane. This acetyl-CoA is accessible to chemicals in the culture mdium, since it is hydrolysed by hydroxylamine. The inhibition of PAF synthesis by hydroxylamine is reversed by adding acetyl-CoA. PAF synthesis in TNF-treated cells appears to be regulated either by the amount of acetyl-CoA available or by the ability to transfer acetyl-CoA from the cellular pool to the lyso-PAF: acetyltransferase.",
author = "C. Tetta and G. Camussi and F. Bussolino and C. Baglioni",
year = "1990",
language = "English",
volume = "2",
journal = "Journal of Lipid Mediators",
issn = "0921-8319",
publisher = "Elsevier BV",
number = "SUPPL.",

}

TY - JOUR

T1 - Regulation of platelet-activating factor synthesis by acetyl-coenzyme A

AU - Tetta, C.

AU - Camussi, G.

AU - Bussolino, F.

AU - Baglioni, C.

PY - 1990

Y1 - 1990

N2 - Human neutrophils (PMN) stimulated by tumor necrosis factor (TNF) synthesize and release platelet-activating factor (PAF) transiently. In the present investigation, we have examined the mechanism responsible for the down-regulation of PAF synthesis. The response of PMN is proportional to the occupancy of high-affinity TNF receptors on the PMN plasma membrane, as shown by binding assays with [125]TNF. These receptors are down-regulated within 10 min of the addition of TNF; the receptors reappear after 60 min, but the PMN do not resume PAF synthesis. Further PAF synthesis is obtained by adding acetyl-coenzyme A (CoA) to the culture medium. However, this compound does not diffuse into PMN, as shown by incubating these cells with labeled acetyl-CoA. This finding suggests that PAF synthesis is regulated by the amount of acetyl-CoA available to the lyso-PAF: acetyltransferase on the cell plasma membrane. This acetyl-CoA is accessible to chemicals in the culture mdium, since it is hydrolysed by hydroxylamine. The inhibition of PAF synthesis by hydroxylamine is reversed by adding acetyl-CoA. PAF synthesis in TNF-treated cells appears to be regulated either by the amount of acetyl-CoA available or by the ability to transfer acetyl-CoA from the cellular pool to the lyso-PAF: acetyltransferase.

AB - Human neutrophils (PMN) stimulated by tumor necrosis factor (TNF) synthesize and release platelet-activating factor (PAF) transiently. In the present investigation, we have examined the mechanism responsible for the down-regulation of PAF synthesis. The response of PMN is proportional to the occupancy of high-affinity TNF receptors on the PMN plasma membrane, as shown by binding assays with [125]TNF. These receptors are down-regulated within 10 min of the addition of TNF; the receptors reappear after 60 min, but the PMN do not resume PAF synthesis. Further PAF synthesis is obtained by adding acetyl-coenzyme A (CoA) to the culture medium. However, this compound does not diffuse into PMN, as shown by incubating these cells with labeled acetyl-CoA. This finding suggests that PAF synthesis is regulated by the amount of acetyl-CoA available to the lyso-PAF: acetyltransferase on the cell plasma membrane. This acetyl-CoA is accessible to chemicals in the culture mdium, since it is hydrolysed by hydroxylamine. The inhibition of PAF synthesis by hydroxylamine is reversed by adding acetyl-CoA. PAF synthesis in TNF-treated cells appears to be regulated either by the amount of acetyl-CoA available or by the ability to transfer acetyl-CoA from the cellular pool to the lyso-PAF: acetyltransferase.

UR - http://www.scopus.com/inward/record.url?scp=0025253989&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025253989&partnerID=8YFLogxK

M3 - Article

C2 - 1966818

AN - SCOPUS:0025253989

VL - 2

JO - Journal of Lipid Mediators

JF - Journal of Lipid Mediators

SN - 0921-8319

IS - SUPPL.

ER -