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Al(3+)-mediated changes in membrane physical properties participate in the inhibition of polyphosphoinositide hydrolysis.

Abstract：

:We investigated the possible involvement of Al(3+)-induced alterations in membrane physical properties in Al(3+)-mediated inhibition of polyphosphoinositide (PPI) hydrolysis by the enzyme phosphatidylinositol-specific phospholipase C (PI-PLC). Liposomes composed of brain phosphatidylcholine (PC) or of PC and a mixture of brain PPI (PC:PPI) were incubated in the presence of Al(3+) (1-100 microM). We evaluated: (1) the amount of membrane-bound Al(3+), (2) the effects of Al(3+) on key membrane physical properties (surface potential, lipid fluidity, and lipid arrangement), and (3) the hydrolysis of PPI. Al(3+) binding to PC:PPI (60:40 mol/mol) liposomes was 1.3 times higher than to PC:PPI (90:10 mol/mol) liposomes and did not change after treatment with Triton X-100. Al(3+) increased membrane surface potential, promoted the loss of membrane fluidity, and caused lateral phase separation in PC:PPI liposomes. Phosphatidylinositol and phosphatidylinositol monophosphate hydrolysis in the presence of PI-PLC was not affected by Al(3+), but a significant and concentration-dependent inhibition of PIP(2) hydrolysis was observed, an effect that was prevented by previous bilayer disruption with Triton X-100. The obtained results support the hypothesis that Al(3+) binding to liposomes promotes the formation of rigid clusters enriched in PPI, restricting the accessibility of the enzyme to the substrate and subsequently inhibiting PIP(2) hydrolysis by PI-PLC.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Verstraeten SV,Oteiza PI

doi

10.1016/s0003-9861(02)00557-x

subject

Has Abstract

pub_date

2002-12-15 00:00:00

pages

263-71

issue

2

eissn

0003-9861

issn

1096-0384

pii

S000398610200557X

journal_volume

408

pub_type

杂志文章

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