Transport of β-alanine in renal brush border membrane vesicles
Transport of β-alanine in renal brush border membrane vesicles
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β-丙氨酸在肾刷状缘膜囊泡中的转运
DOI:
10.1016/0005-2736(78)90052-4
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发表时间:
1978
期刊:
影响因子:
--
通讯作者:
B. Sacktor
中科院分区:
文献类型:
--
作者:
M. Hammerman;B. Sacktor
The findings that the equilibrium uptake of β-alanine decreased with increasing medium osmolarity and preincubation with β-alanine increased uptake of the amino acid indicate that the uptake of β-alanine by rabbit renal brush border membranes represents transport into membrane vesicles. A Na+electrochemical gradient (extravesicular > intravesicular) stimulated the initial rate of β-alanine uptake about three times and effected a transient accumulation of the amino acid twice the equilibrium value. Stimulation of the uptake was specific for Na+. Gramicidin abolished the overshoot, presumably by dissipating the gradient by accelerating the electrogenic entrance of Na+into the vesicle via a pathway not coupled to uptake of β-alanine. In K+-loaded vesicle, valinomycin enhanced the Na+gradient-dependent uptake of β-alanine. These findings indicate that the Na+gradient-dependent transport of β-alanine is an electrogenic process and suggest that the membrane potential is a determinant of β-analine transport. Uptake of β-aniline, at a given concentration, reflected the sum of contributions from Na+gradient-dependent and -independent transport systems. The dependent system saturated at 100 μM. The independent system did not saturate. At physiological concentrations the rate of the Na+gradient-dependent uptake was four times that in the absence of the gradient. The Na+gradient-dependent rate of β-alanine uptake was strongly inhibited by taurine, suggesting that β-amino acids have a common transport system, α-Amino acids, i.e.l-arginine,l-glutamate,l-proline, and glycine, representing previously reported specific α-amino acid transport systems in the brush border membrane, did not inhibit the uptake of β-alanine. These findings indicate that the brush border membrane has a distinct transport system for β-amino acids.