Differential localization of putative amino acid receptors in taste buds of the channel catfish, Ictalurus punctatus

The Journal of Comparative Neurology
T E FingerJ G Brand

Abstract

The taste system of catfish, having distinct taste receptor sites for L-alanine and L-arginine, is highly sensitive to amino acids. A previously described monoclonal antibody (G-10), which inhibits L-alanine binding to a partial membrane fraction (P2) derived from catfish (Ictalurus punctatus) taste epithelium, was found in Western blots to recognize a single band, at apparent MW of 113,000 D. This MW differs from the apparent MW for the presumed arginine receptor identified previously by PHA-E lectin affinity. In order to test whether PHA-E lectin actually reacts with the arginine-receptor, reconstituted membrane proteins partially purified by PHA-E affinity were used in artificial lipid bilayers. These reconstituted channels exhibited L-arginine-activated activity similar to that found in taste cell membranes. Accordingly, we utilized the PHA-E lectin and G-10 antibody as probes to differentially localize the L-alanine and L-arginine binding sites on the apical surface of catfish taste buds. Each probe labels numerous, small (0.5-1.0 micron) patches within the taste pore of each taste bud. This observation suggests that each bud is not tuned to a single taste substance, but contains putative receptor sites for both L-arginine...Continue Reading

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Citations

Jul 15, 2003·Proceedings of the National Academy of Sciences of the United States of America·Thomas E FingerWayne L Silver
Feb 4, 1999·Annals of the New York Academy of Sciences·W GrosvenorJ G Brand
Oct 15, 2010·Journal of Cellular Physiology·Makoto Hamanoue, Hideyuki Okano
Apr 1, 1999·Annual Review of Physiology·M S Herness, T A Gilbertson
Jan 15, 2011·BMC Pulmonary Medicine·Marco TizzanoThomas E Finger
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Jun 7, 2014·Science·John CaprioSadao Kiyohara
Apr 1, 2011·The Journal of Comparative Neurology·Makoto OhmotoIchiro Matsumoto
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