Gamma-linolenic acid alters the composition of mitochondrial membrane subfractions, decreases outer mitochondrial membrane binding of hexokinase and alters carnitine palmitoyltransferase I properties in the Walker 256 rat tumour

Author(s):  
Alison Colquhoun
2007 ◽  
Vol 282 (37) ◽  
pp. 26908-26916 ◽  
Author(s):  
Audrey Faye ◽  
Catherine Esnous ◽  
Nigel T. Price ◽  
Marie Anne Onfray ◽  
Jean Girard ◽  
...  

2002 ◽  
Vol 277 (51) ◽  
pp. 49360-49365 ◽  
Author(s):  
Gorka Basañez ◽  
Juanita C. Sharpe ◽  
Jennifer Galanis ◽  
Teresa B. Brandt ◽  
J. Marie Hardwick ◽  
...  

During apoptosis, Bax-type proteins permeabilize the outer mitochondrial membrane to release intermembrane apoptogenic factors into the cytosol via a poorly understood mechanism. We have proposed that Bax and ΔN76Bcl-xL(the Bax-like cleavage fragment of Bcl-xL) function by forming pores that are at least partially composed of lipids (lipidic pore formation). Since the membrane monolayer must bend during lipidic pore formation, we here explore the effect of intrinsic membrane monolayer curvature on pore formation. Nonlamellar lipids with positive intrinsic curvature such as lysophospholipids promoted membrane permeabilization, whereas nonlamellar lipids with negative intrinsic curvature such as diacylglycerol and phosphatidylethanolamine inhibited membrane permeabilization. The differential effects of nonlamellar lipids on membrane permeabilization were not correlated with lipid-induced changes in membrane binding or insertion of Bax or ΔN76Bcl-xL. Altogether, these results are consistent with a model whereby Bax-type proteins change the bending propensity of the membrane to form pores comprised at least in part of lipids in a structure of net positive monolayer curvature.


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