Cation transport properties of a synthetic Ca2+-selective peptide ionophore in phospholipid and sarcoplasmic reticulum vesicles.
Transport by the synthetic cyclic peptide ionophore CYCLEX-2E (Deber, C.M. Young, M.E.M., and Tom-Kun, J. (1980) Biochemistry 19, 6194-6198), which in contrast to Ca2+ ionophore A23187 contains no ionizable protons, has been studied with respect to Ca2+ and Na+ transport, and the involvement of exchanged, or counter-transported ions during the transport process. CYCLEX-2E was found to equilibrate Na+ and Ca2+ gradients across phospholipid vesicle membranes. Experiments using the indicator dye Arsenazo III established that calcium ions were indeed reaching the aqueous intravesicular compartments. Absence of metal cations in the external buffer slowed, but did not eliminate, the efflux of Ca2+ from phosphatidylcholine vesicles. As an example of its activity in a biological membrane, CYCLEX-2E was shown to be capable of producing Ca2+ efflux from sarcoplasmic reticulum vesicles which has been loaded with Ca2+ in an ATP-dependent manner. The overall results suggest that in transport by synthetic peptide ionophores typified by CYCLEX-2E, electroneutrality is achieved either through (a) peptide-mediated compensating (but not coupled) fluxes of other cations, or where this is not an option, by (b) transmembrane diffusion of permeant ions such as H+, OH-, or Cl-.
D000818:Animals; D001693:Biological Transport, Active; D017301:Ca(2+) Mg(2+)-ATPase; D002118:Calcium / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D008051:Lipid Bilayers / Q000378:metabolism*; D009994:Osmolar Concentration; D010456:Peptides, Cyclic / Q000378:metabolism*; D010743:Phospholipids; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*; D013010:Sonication
D008051:Lipid Bilayers; D010456:Peptides, Cyclic; D010743:Phospholipids; C028698:CYCLEX-2E; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases; D002118:Calcium