Dataset Information

Transport of phosphoenolpyruvate through the erythrocyte membrane.

ABSTRACT: Phosphoenolpyruvate was transported through the erythrocyte membrane at low pH (4.5-6.5). The influx was observed not only in an iso-osmotic sucrose medium, but also in 0.1 M-citrate solution, but it was negligible in an iso-osmotic NaC1 solution. Efflux, however, was observed in both the sucrose and NaC1 solutions. Compounds derived from phosphoenolpyruvate by replacing the methene group by similarly hydrophobic groups such as hydrogen or the methyl group were permeant but those with the hydrophilic hydroxymethyl group were impermeant. This transport was inhibited by the treatment with 4-acetamido-4'-isothiocyanostilbene-2,2'-disulphonic acid or pyridoxal phosphate/NaBH4, which are known to be specific for the transport of anions such as C1-, SO42- and HPO42-. It showed saturation kinetics with respect to phosphoenolpyruvate concentration in the medium. These results suggest that the transport of phosphoenolpyruvate is mediated by the anion-transport system. Although phosphoenolpyruvate was transported against the concentration gradient, the transport was characterized as a passive transport, and this apparent uphill transport was interpreted by the Donnan equilibrium.

SUBMITTER: Hamasaki N

PROVIDER: S-EPMC1183858 | biostudies-other | 1978 Jan

REPOSITORIES: biostudies-other

ACCESS DATA

Similar Datasets

Project description:Erythrocyte shape and membrane integrity is imparted by the membrane skeleton, which can be isolated as a Triton X-100 insoluble structure that retains the biconcave shape of intact erythrocytes, indicating isolation of essentially intact membrane skeletons. These erythrocyte "Triton Skeletons" have been studied morphologically and biochemically, but unbiased proteome analysis of this substructure of the membrane has not been reported. In this study, different extraction buffers and in-depth proteome analyses were used to more fully define the protein composition of this functionally critical macromolecular complex. As expected, the major, well-characterized membrane skeleton proteins and their associated membrane anchors were recovered in good yield. But surprisingly, a substantial number of additional proteins that are not considered in erythrocyte membrane skeleton models were recovered in high yields, including myosin-9, lipid raft proteins (stomatin, flotillin1 and 2), multiple chaperone proteins (HSPs, protein disulfide isomerase and calnexin), and several other proteins. These results show that the membrane skeleton is substantially more complex than previous biochemical studies indicated, and it apparently has localized regions with unique protein compositions and functions. This comprehensive catalog of the membrane skeleton should lead to new insights into erythrocyte membrane biology and pathogenic mutations that perturb membrane stability. Biological significance Current models of erythrocyte membranes describe fairly simple homogenous structures that are incomplete. Proteome analysis of the erythrocyte membrane skeleton shows that it is quite complex and includes a substantial number of proteins whose roles and locations in the membrane are not well defined. Further elucidation of interactions involving these proteins and definition of microdomains in the membrane that contain these proteins should yield novel insights into how the membrane skeleton produces the normal biconcave erythrocyte shape and how it is perturbed in pathological conditions that destabilize the membrane.

Dataset Information

Transport of phosphoenolpyruvate through the erythrocyte membrane.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure