A rabbit erythrocyte membrane protein associated with L-lactate transport.

نویسندگان

  • M L Jennings
  • M Adams-Lackey
چکیده

Chemical Labeling has been employed to attempt to identify the lactate transport protein of rabbit erythrocytes, which have a very high capacity for stereoselective lactate transport. The lactate transport protein catalyzes lactate/proton cotransport (or lactate/hydroxyl exchange) at physiological pH, as demonstrated by uphill proton fluxes induced by lactate gradients. However, lactate/lactate and lactate/pyruvate exchange are considerably more rapid than lactate/proton cotransport. Although the lactate transporter is less sensitive to inhibition by the stilbenedisulfonate derivative H2DIDS (4,4'diisothiocyano-2,2'-dihydrostilbenedisulfonate) than is the inorganic anion exchanger (band 3), H2DIDS is nonetheless a reasonably potent inhibitor of the lactate transport. A 1-h treatment with 10(-4) M H2DIDS irreversibly inhibits lactate/lactate exchange by greater than 80%. This inhibition appears to be related to the labeling (by [3H]H2DIDS) of an integral membrane polypeptide of Mr = 43,000. This [3H]H2DIDS-labeled polypeptide is absent from human erythrocytes, which have a 100-fold lower Vmax for lactate transport than do rabbit erythrocytes. These experiments suggest that the polypeptide of Mr = 43,000 is a component of the lactate transport system.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

N-terminal protein sequence analysis of the rabbit erythrocyte lactate transporter suggests identity with the cloned monocarboxylate transport protein MCT1.

An improved purification for the rabbit erythrocyte lactate transporter, using aminoethyl-Sepharose chromatography, is described. The process of purification of the 40-50 kDa transporter, labelled with 4,4'-diisothiocyanostilbene-2,2'-disulphonate (DIDS), was followed by Western blotting with anti-DIDS antibodies [Poole, R. C. and Halestrap, A. P. (1992) Biochem. J. 283, 855-862]. Fractions hig...

متن کامل

Reconstitution of the L-lactate carrier from rat and rabbit erythrocyte plasma membranes.

1. Rat and rabbit erythrocyte plasma-membrane proteins were solubilized with decanoyl-N-methylglucamide and reconstituted into liposomes. The procedure includes detergent removal by gel filtration, followed by a freeze-thaw step. 2. The rate of [1-14C]pyruvate uptake into these vesicles was inhibited by approx. 70% by alpha-cyano-4-hydroxycinnamate and p-chloromercuribenzenesulphonate. The exte...

متن کامل

Carrier-mediated transport of monocarboxylate drugs in the pigmented rabbit conjunctiva.

PURPOSE To determine whether an Na+-dependent monocarboxylate transport process exists on the mucosal side of the pigmented rabbit conjunctiva and to evaluate how it may contribute to the absorption of ophthalmic monocarboxylate drugs. METHODS L-lactate was used as a model substrate. The excised pigmented rabbit conjunctiva was mounted in a modified Ussing chamber for the measurement of short...

متن کامل

Carrier-mediated L-lactate transport in brush-border membrane vesicles from rat placenta during late gestation.

The mechanism for L-lactate transport across microvillous membrane vesicles prepared from rat placenta was examined. Uptake of L-lactate into these vesicles was mainly the result of transport into the intravesicular (osmotically active) space. The initial rate of L-lactate uptake was not affected by the presence of an inward gradient of either Na+ or K+. In the presence of an inward-directed pr...

متن کامل

Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice.

Previous research has shown that glycolytic enzymes (GEs) exist as multienzyme complexes on the inner surface of human erythrocyte membranes. Because GE binding sites have been mapped to sequences on the membrane protein, band 3, that are not conserved in other mammalian homologs, the question arose whether GEs can organize into complexes on other mammalian erythrocyte membranes. To address thi...

متن کامل

ذخیره 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 نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 257 21  شماره 

صفحات  -

تاریخ انتشار 1982