Demonstration and characterization of phosphate transport in mammalian peroxisomes.

It is now well established that the peroxisomal membrane is not freely permeable to small molecules in vivo, which implies the existence of metabolite transporters in the peroxisomal membrane. A few putative peroxisomal metabolite transporters have indeed been identified, but the function of these proteins has remained largely unresolved so far. The only peroxisomal transporter characterized to a significant extent is the adenine nucleotide transporter, which is presumably required to sustain the activity of the intraperoxisomal very-long-chain-acyl-CoA synthetase. In addition to AMP, this acyl-CoA synthetase also produces pyrophosphate, which must be exported from the peroxisome. In the present study, we demonstrate that the peroxisomal membrane contains a transporter activity that facilitates the passage of phosphate and possibly pyrophosphate across the peroxisomal membrane. By reconstitution of peroxisomal membrane proteins in proteoliposomes, some kinetic parameters of the transporter could be established in vitro. The transporter can be distinguished from the mitochondrial phosphate transporter by its different sensitivity to inhibitors.