RhCG Protein Active Ammonia Transporter - Reversed by Metals.

"The major finding of this study is that RhCG protein is active as an NH(3) channel and that this function does not require any protein partner. This strong NH(3) transport was reversibly inhibited by mercuric and copper salts.

Notes:

• Acidosis changes expression transporter RhCG. (Sechadri)

CiteULike: Functional reconstitution into liposomes of purified human RhCG ammonia channel.: "Mouro-Chanteloup, I., Cochet, S., Chami, M., Genetet, S., Zidi-Yahiaoui, N., Engel, A., Colin, Y., Bertrand, O., and Ripoche, P. (2010). Functional reconstitution into liposomes of purified human rhcg ammonia channel. PloS one, 5(1)."

Seshadri, R. M., Klein, J. D., Smith, T., Sands, J. M., Handlogten, M. E., Verlander, J. W., and Weiner, D. I. (2006). Changes in subcellular distribution of the ammonia transporter, rhcg, in response to chronic metabolic acidosis. Am J Physiol Renal Physiol, 290(6):F1443-1452.
http://www.citeulike.org/group/5070/article/2944496
Lim, S. W., Ahn, K. O., Kim, W. Y., Han, D. H., Lie, C., Ghee, J. Y., Han, K. H., Kim, H.-Y., Handlogten, M. E., Kim, J., Yang, C. W., and Weiner, I. D. (2008). Expression of ammonia transporters, rhbg and rhcg, in chronic cyclosporine nephropathy in rats. Nephron- Experimental Nephrology, 110(2). http://www.citeulike.org/user/HEIRS/article/6777343