Peroxisomal membrane permeability and solute transfer.
The review is dedicated to recent progress in the study of peroxisomal membrane permeability to solutes which has been a matter of debate for more than 40 years. Apparently, the mammalian peroxisomal membrane is freely permeable to small solute molecules owing to the presence of pore-forming channels. However, the membrane forms a permeability barrier for 'bulky' solutes including cofactors (NAD/H, NADP/H, CoA, and acetyl/acyl-CoA esters) and ATP. Therefore, peroxisomes need specific protein transporters to transfer these compounds across the membrane. Recent electrophysiological studies have revealed channel-forming activities in the mammalian peroxisomal membrane. The possible involvement of the channels in the transfer of small metabolites and in the formation of peroxisomal shuttle systems is described.
Antonenkov
Vasily D
VD
Department of Biochemistry and Biocenter Oulu, University of Oulu, P.O. Box 3000, FIN-90014 Oulu, Finland. vasily.antonenkov@oulu.fi
Hiltunen
J Kalervo
JK
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001692:Biological Transport; D003065:Coenzyme A / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000378:metabolism*; D008954:Models, Biological; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D010539:Permeability; D020675:Peroxisomes / Q000378:metabolism*; D011755:Pyrophosphatases / Q000378:metabolism; D017382:Reactive Oxygen Species / Q000378:metabolism; D000096964:Nudix Hydrolases
D000255:Adenosine Triphosphate; D003065:Coenzyme A; D026901:Membrane Transport Proteins; D009243:NAD; D009249:NADP; D011755:Pyrophosphatases; D017382:Reactive Oxygen Species; D000096964:Nudix Hydrolases