Protein-mediated chloride-phosphate and lactate-lactate exchange in cytoskeleton-free vesicles budded from rabbit erythrocytes

Donovan, Jerald A.

doi:10.1016/0005-2736(85)90394-3

Biochimica et Biophysica Acta (BBA) - Biomembranes

1985

DOI: 10.1016/0005-2736(85)90394-3

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Protein-mediated chloride-phosphate and lactate-lactate exchange in cytoskeleton-free vesicles budded from rabbit erythrocytes

Jerald A. Donovan¹

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1986

1991

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Cited by 4 publications

(1 citation statement)

References 28 publications

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“…Thus, rabbit red cell membranes are a likely model for the identification and isolation of this transport protein. In our laboratory, chemical labeling with [3H]H2DIDS at concentrations that inhibit specific lactate exchange suggests that a 40-50-kDa integral membrane polypeptide (band R) is associated with lactate transport in rabbit erythrocytes (Jennings & Adams-Lackey, 1982) and in spectrin-free vesicles budded from rabbit erythrocytes (Donovan, 1985). We have also shown that the site of [3H]H2DIDS labeling on band R is protected by the potent lactate transport inhibitor iBCLA (Donovan & Jennings, 1985).…”

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N-hydroxysulfosuccinimido active esters and the L-(+)-lactate transport protein in rabbit erythrocytes

Donovan¹,

Jennings²

1986

Biochemistry

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Esters of N-hydroxysulfosuccinimide strongly inhibit L-(+)-lactate transport in rabbit erythrocytes, probably by acylating amino groups on the transport protein. Lactate transport studies using bis(sulfosuccinimido) suberate (BS3), bis(sulfosuccinimido) adipate (BS2A), bis(sulfosuccinimido) dithiobis(propionate), and a variety of monocarboxylate esters suggest that an exofacial amino group of the lactate transport protein is essential for lactate transport. Also, reductive methylation studies show that even when positive charge is preserved in modified amino groups, the transport is strongly inhibited. At pH less than 6, band 3 mediated inorganic anion transport is enhanced in BS3-treated cells, while at pH greater than 6, it is inhibited. BS3-induced inhibition of L-(+)-lactate transport does not have this pH dependence. BS3 reduces the labeling of a 40-50-kDa membrane polypeptide (band R) by tritiated 4,4'-diisothiocyanato-2,2-dihydrostilbenedisulfonate ([3H]H2DIDS) and by tritiated bis(sulfosuccinimido) adipate ([3H]BS2A). Tritiated sulfosuccinimido acetate (S2[3H]acetate) also labels band R, over a range of concentrations where lactate transport is inhibited in a dose-dependent manner by S2 acetate. BS3 is a known impermeant protein cross-linker. S2 acetate permeates rabbit red cell membranes by an H2DIDS-inhibitable mechanism. BS3 cross-links the proteolytic fragments of rabbit band 3 produced by extracellular chymotrypsin. These labeling experiments support an association between band R and specific monocarboxylate transport.

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confidence: 86%

N-hydroxysulfosuccinimido active esters and the L-(+)-lactate transport protein in rabbit erythrocytes

Donovan¹,

Jennings²

1986

Biochemistry

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Blood lactate accumulation in intermittent supramaximal exercise

Rieu

Duvallet²,

Scharapan³

et al. 1988

Europ. J. Appl. Physiol.

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Blood lactate accumulation rate and oxygen consumption have been studied in six trained male runners, aged 20 to 30 years. Subjects ran on a treadmill at a rate representing 172 +/- 5% VO2max for four 45 s sessions, separated by 9 min rest periods. Oxygen consumption was measured throughout. Blood lactate was determined in samples taken from the ear and VO2 was measured at the end of each exercise session, and two, five and nine minutes later. After the fourth exercise session, the same measurements were made every five min for 30 min. 4 subjects repeated a single exercise of the same type, duration and intensity and the same measurements were taken. With repetitive intermittent exercise, gradual increases in blood lactate concentration [( LA]b) occurred, whereas its rate of accumulation (delta[LA]b) decreased. The amount of oxygen consumed during each 45 s exercise session remained unchanged for a given subject. After cessation of intermittent exercise, the half-time of blood lactate was 26 min, whereas it was only 15 min after a single exercise session. VO2 values, on the other hand, returned to normal after 15 to 20 min. All other conditions being equal, the gradual decrease in delta[LA]b during intermittent exercise could be explained if the lactate produced during the first exercise session is used during the second period, and/or if the diffusion space of lactate increases. The diffusion space seems to be multi-compartmental on the basis of half-time values noted for [LA]b after intermittent exercise, compared with those noted after a single exercise session.(ABSTRACT TRUNCATED AT 250 WORDS)

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Muscle lactate transport studied in sarcolemmal giant vesicles

Juel

1991

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Protein-mediated chloride-phosphate and lactate-lactate exchange in cytoskeleton-free vesicles budded from rabbit erythrocytes

Cited by 4 publications

References 28 publications

N-hydroxysulfosuccinimido active esters and the L-(+)-lactate transport protein in rabbit erythrocytes

N-hydroxysulfosuccinimido active esters and the L-(+)-lactate transport protein in rabbit erythrocytes

Blood lactate accumulation in intermittent supramaximal exercise

Muscle lactate transport studied in sarcolemmal giant vesicles

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