Characterization of a novel Na+-independent amino acid transporter in horse erythrocytes.
نویسندگان
چکیده
Horse erythrocytes are polymorphic with respect to L-alanine permeability. The present investigation compared the specificity, kinetics and cation-dependence of erythrocyte amino acid transport in two groups of thoroughbred horses, those with erythrocyte L-alanine permeabilities in the range 5-15 mumol/h per litre of cells (0.2 mM extracellular L-alanine, 37 degrees C) (transport-negative type) and those with L-alanine permeabilities in the range 450-700 mumol/h per litre of cells (transport-positive type). Transport-positive cells are shown to possess a novel high-affinity, stereospecific, Na+-independent transporter selective for neutral amino acids of intermediate size. This carrier system (provisional designation asc) operates preferentially in an exchange mode and is functionally absent from erythrocytes of transport-negative-type horses.
منابع مشابه
Chemical activation of a high-affinity glutamate transporter in human erythrocytes and its implications for malaria-parasite-induced glutamate uptake.
Human erythrocytes have a low basal permeability to L-glutamate and are not known to have a functional glutamate transporter. Here, treatment of human erythrocytes with arsenite was shown to induce the uptake of L-glutamate and D-aspartate, but not that of D-glutamate or L-alanine. The majority of the arsenite-induced L-glutamate influx was via a high-affinity, Na(+)-dependent system showing ch...
متن کاملRED CELLS, IRON, AND ERYTHROPOIESIS Chemical activation of a high-affinity glutamate transporter in human erythrocytes and its implications for malaria-parasite–induced glutamate uptake
Human erythrocytes have a low basal permeability to L-glutamate and are not known to have a functional glutamate transporter. Here, treatment of human erythrocytes with arsenite was shown to induce the uptake of L-glutamate and D-aspartate, but not that of D-glutamate or L-alanine. The majority of the arseniteinduced L-glutamate influx was via a highaffinity, Na -dependent system showing charac...
متن کاملCharacterization of L-arginine transport in adrenal cells: effect of ACTH.
Nitric oxide synthesis depends on the availability of its precursor L-arginine, which could be regulated by the presence of a specific uptake system. In the present report, the characterization of the L-arginine transport system in mouse adrenal Y1 cells was performed. L-arginine transport was mediated by the cationic/neutral amino acid transport system y+L and the cationic amino acid transport...
متن کاملIdentification and functional characterization of a Na+-independent neutral amino acid transporter with broad substrate selectivity.
We have isolated a cDNA from rat small intestine that encodes a novel Na+-independent neutral amino acid transporter with distinctive characteristics in substrate selectivity and transport property. The encoded protein, designated L-type amino acid transporter-2 (LAT-2), shows amino acid sequence similarity to the system L Na+-independent neutral amino acid transporter LAT-1 (Kanai, Y., Segawa,...
متن کاملIsolation and Characterization of a New Peroxisome Deficient CHO Mutant Cell Belonging to Complementation Group 12
We searched for novel Chinese hamster ovary (CHO) cell mutants defective in peroxisome biogenesis by an improved method using peroxisome targeting sequence (PTS) of Pex3p (amino acid residues 1–40)-fused enhanced green fluorescent protein (EGFP). From mutagenized TKaEG3(1–40) cells, the wild-type CHO-K1 stably expressing rat Pex2p and of rat Pex3p(1–40)-EGFP, numerous cell colonies resistant to...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Biochemical journal
دوره 227 1 شماره
صفحات -
تاریخ انتشار 1985