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Journal of Experimental Biology 136,363-381 (1988)
Published by Company of Biologists 1988


Electroneutral Na+-2 Cl--Leucine Cotransport by Lobster Hepatopancreatic Brush-Border Membrane Vesicles

GREGORY A. AHEARN 1 and LAUREL P. CLAY 1

1 Department of Zoology, 2538 The Mall, University of Hawaii at Manoa, Honolulu, HI 96822, USA

Uptake of L-[3H]leucine by lobster hepatopancreatic brush-border membrane vesicles was stimulated by a transmembrane NaCl gradient (o>i), but not by identical gradients of NaSCN or other Cl- salts (e.g. K+, Li+, NH4+, Cs+ or choline), suggesting that amino acid transfer depended upon both Na+ and Cl-. In NaCl medium at acidic pH, leucine uptake was largely electroneutral and unresponsive to a transmembrane potential generated by permeable anions; however, in Na+-free medium, amino acid transport was strongly electrogenic under the same conditions. Leucine influx occurred by a combination of two carrier processes at physiologically acidic pH. One exhibited an influx Kt of 0.59 mmol l-1, a JM of 390 pmol mg protein-1 S-1 and a cotransport stoichiometry of 1 Na+: 2 Cl+: 1 leucine. This process was most strongly cis-inhibited by the non-polar amino acids phenylalanine, methionine and isoleucine, and most weakly inhibited by the more polar species methylaminoisobutyric acid (MeAIB), hydroxyproline, glutamate and arginine. The second leucine carrier system showed a very low binding affinity and could not be distinguished from diffusion, was Na+- and Cl--independent, and was cis-inhibited by more polar amino acids such as lysine, hydroxyproline, MeAIB, alanine and glutamate. These results suggest that brush-border leucine transport in lobster hepatopancreas at acidic pH may occur by a combination of a modified L-system, that includes ion cosubstrates, and either by a second undefined Na+-independent process with a broad structural specificity or by multiple Na+-independent processes.

Key words: cotransport, leucine transport, brush-border membrane vesicles, Na+-dependent, hepatopancreas, Homarus americanus, ion gradients

Accepted on November 25, 1987




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J. Exp. Biol.Home page
E. M. Conrad and G. A. Ahearn
3H-L-histidine and 65Zn2+ are cotransported by a dipeptide transport system in intestine of lobster Homarus americanus
J. Exp. Biol., January 15, 2005; 208(2): 287 - 296.
[Abstract] [Full Text] [PDF]




© The Company of Biologists Ltd 1988