Al3+-mediated changes on membrane fluidity affects the activity of PI-PLC but not of PLC

Sandra V. Verstraeten, Marcela S. Villaverde, Patricia I. Oteiza

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

We investigated whether Al3+-mediated changes in membrane fluidity can affect the activity of prokaryotic enzymes phospholipase C (PLC) and phospholipase C-phosphatidyl inositol specific (PI-PLC) in liposomes of phosphatidyl choline (PC), PC:phosphatidyl inositol (PI), or PC and polyphosphoinositides (PPI). Al3+ (10-100 μM) promoted membrane rigidification, evaluated with the probes 1,6-diphenyl-1,3,5-hexatriene and Laurdan, and followed the order: PC:PPI>PC:PI>PC. Al3+ (25 and 50 μM) did not affect PLC-mediated hydrolysis of PC, PI and PIP2, but stimulated PIP hydrolysis (48.6%). PI-PLC did not affect PC, PI, and PIP concentrations, but caused a 67% decrease in PIP2. Al3+ significantly inhibited PIP2 hydrolysis in a concentration-dependent (25-50 μM) manner. Results suggest that the inhibition of PIP2 hydrolysis by Al3+ could be partially due to a higher lipid packing induced by Al3+ which could affect the interaction between the enzyme and its substrate.

Original languageEnglish (US)
Pages (from-to)159-163
Number of pages5
JournalChemistry and Physics of Lipids
Volume122
Issue number1-2
DOIs
StatePublished - Jan 2003
Externally publishedYes

Fingerprint

Membrane Fluidity
Fluidity
Type C Phospholipases
Phosphatidylinositols
Phosphatidylcholines
Membranes
Hydrolysis
Phosphatidylinositol Phosphates
Diphenylhexatriene
Enzymes
Liposomes
Lipids
Substrates

Keywords

  • Aluminum
  • Fluidity
  • Membranes
  • Phosphoinositides
  • Phospholipase
  • PI-PLC
  • PLC

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics

Cite this

Al3+-mediated changes on membrane fluidity affects the activity of PI-PLC but not of PLC. / Verstraeten, Sandra V.; Villaverde, Marcela S.; Oteiza, Patricia I.

In: Chemistry and Physics of Lipids, Vol. 122, No. 1-2, 01.2003, p. 159-163.

Research output: Contribution to journalArticle

Verstraeten, Sandra V. ; Villaverde, Marcela S. ; Oteiza, Patricia I. / Al3+-mediated changes on membrane fluidity affects the activity of PI-PLC but not of PLC. In: Chemistry and Physics of Lipids. 2003 ; Vol. 122, No. 1-2. pp. 159-163.
@article{74dc81002be94cf5a331c5b34504a693,
title = "Al3+-mediated changes on membrane fluidity affects the activity of PI-PLC but not of PLC",
abstract = "We investigated whether Al3+-mediated changes in membrane fluidity can affect the activity of prokaryotic enzymes phospholipase C (PLC) and phospholipase C-phosphatidyl inositol specific (PI-PLC) in liposomes of phosphatidyl choline (PC), PC:phosphatidyl inositol (PI), or PC and polyphosphoinositides (PPI). Al3+ (10-100 μM) promoted membrane rigidification, evaluated with the probes 1,6-diphenyl-1,3,5-hexatriene and Laurdan, and followed the order: PC:PPI>PC:PI>PC. Al3+ (25 and 50 μM) did not affect PLC-mediated hydrolysis of PC, PI and PIP2, but stimulated PIP hydrolysis (48.6{\%}). PI-PLC did not affect PC, PI, and PIP concentrations, but caused a 67{\%} decrease in PIP2. Al3+ significantly inhibited PIP2 hydrolysis in a concentration-dependent (25-50 μM) manner. Results suggest that the inhibition of PIP2 hydrolysis by Al3+ could be partially due to a higher lipid packing induced by Al3+ which could affect the interaction between the enzyme and its substrate.",
keywords = "Aluminum, Fluidity, Membranes, Phosphoinositides, Phospholipase, PI-PLC, PLC",
author = "Verstraeten, {Sandra V.} and Villaverde, {Marcela S.} and Oteiza, {Patricia I.}",
year = "2003",
month = "1",
doi = "10.1016/S0009-3084(02)00192-5",
language = "English (US)",
volume = "122",
pages = "159--163",
journal = "Chemistry and Physics of Lipids",
issn = "0009-3084",
publisher = "Elsevier Ireland Ltd",
number = "1-2",

}

TY - JOUR

T1 - Al3+-mediated changes on membrane fluidity affects the activity of PI-PLC but not of PLC

AU - Verstraeten, Sandra V.

AU - Villaverde, Marcela S.

AU - Oteiza, Patricia I.

PY - 2003/1

Y1 - 2003/1

N2 - We investigated whether Al3+-mediated changes in membrane fluidity can affect the activity of prokaryotic enzymes phospholipase C (PLC) and phospholipase C-phosphatidyl inositol specific (PI-PLC) in liposomes of phosphatidyl choline (PC), PC:phosphatidyl inositol (PI), or PC and polyphosphoinositides (PPI). Al3+ (10-100 μM) promoted membrane rigidification, evaluated with the probes 1,6-diphenyl-1,3,5-hexatriene and Laurdan, and followed the order: PC:PPI>PC:PI>PC. Al3+ (25 and 50 μM) did not affect PLC-mediated hydrolysis of PC, PI and PIP2, but stimulated PIP hydrolysis (48.6%). PI-PLC did not affect PC, PI, and PIP concentrations, but caused a 67% decrease in PIP2. Al3+ significantly inhibited PIP2 hydrolysis in a concentration-dependent (25-50 μM) manner. Results suggest that the inhibition of PIP2 hydrolysis by Al3+ could be partially due to a higher lipid packing induced by Al3+ which could affect the interaction between the enzyme and its substrate.

AB - We investigated whether Al3+-mediated changes in membrane fluidity can affect the activity of prokaryotic enzymes phospholipase C (PLC) and phospholipase C-phosphatidyl inositol specific (PI-PLC) in liposomes of phosphatidyl choline (PC), PC:phosphatidyl inositol (PI), or PC and polyphosphoinositides (PPI). Al3+ (10-100 μM) promoted membrane rigidification, evaluated with the probes 1,6-diphenyl-1,3,5-hexatriene and Laurdan, and followed the order: PC:PPI>PC:PI>PC. Al3+ (25 and 50 μM) did not affect PLC-mediated hydrolysis of PC, PI and PIP2, but stimulated PIP hydrolysis (48.6%). PI-PLC did not affect PC, PI, and PIP concentrations, but caused a 67% decrease in PIP2. Al3+ significantly inhibited PIP2 hydrolysis in a concentration-dependent (25-50 μM) manner. Results suggest that the inhibition of PIP2 hydrolysis by Al3+ could be partially due to a higher lipid packing induced by Al3+ which could affect the interaction between the enzyme and its substrate.

KW - Aluminum

KW - Fluidity

KW - Membranes

KW - Phosphoinositides

KW - Phospholipase

KW - PI-PLC

KW - PLC

UR - http://www.scopus.com/inward/record.url?scp=0037277581&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037277581&partnerID=8YFLogxK

U2 - 10.1016/S0009-3084(02)00192-5

DO - 10.1016/S0009-3084(02)00192-5

M3 - Article

VL - 122

SP - 159

EP - 163

JO - Chemistry and Physics of Lipids

JF - Chemistry and Physics of Lipids

SN - 0009-3084

IS - 1-2

ER -