Inactivation of Mitochondrial Permeability Transition Pore by Octylguanidine and Octylamine

被引:0
|
作者
Edmundo Chávez
Antonio Penña
Cecilia Zazueta
Jorge Ramírez
Noemí García
Raymundo Carrillo
机构
[1] Instituto Nacional de Cardiología,Departamento de Bioquímica
[2] Ignacio Chávez,Departamento de Microbiología
[3] Instituto de Fisiología Celular,Departamento de Bioquímica
[4] UNAM,undefined
[5] Instituto Nacional de Cardiología,undefined
[6] Ignacio Chávez,undefined
来源
Journal of Bioenergetics and Biomembranes | 2000年 / 32卷
关键词
Mitochondria; octylguanidine; octylamine; carboxyatractyloside; permeability transition; kidney mitochondria; nonspecific pore; calcium; mitochondrial calcium; mitochondrial membrane;
D O I
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中图分类号
学科分类号
摘要
Mitochondrial permeability transition occurs through a Ca2+-dependent opening of atransmembrane pore, whose identity has been attributed to that of the adenine nucleotide translocase(ANT). In this work, we induced permeability transition by adding 0.5 μM carboxyatractyloside.The process was evaluated analyzing Ca2+ efflux, a drop in transmembrane electric gradient,and swelling. We found that the amphiphyllic cations octylguanidine and octylamine, at theconcentration of 100 μM, inhibited, almost completely, nonspecific membrane permeability.Hexylguanidine, hexylamine, as well as guanidine chloride and hydroxylamine failed to doso. The inhibition was reversed after the addition of 40 mM Li+, Na+ K+,Rb+, or Cs+; K+ wasthe most effective. We propose that the positive charge of the amines interact with negativecharges of membrane proteins, more likely the ADP/ATP carrier, while the alkyl chain penetratesinto the hydrophobic milieu of the inner membrane, fixing the reagent.
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页码:193 / 198
页数:5
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