Molecular characterization of branchial aquaporin 1aa and effects of seawater acclimation, emersion or ammonia exposure on its mRNA expression in the gills, gut, kidney and skin of the freshwater climbing perch, Anabas testudineus.

作者: Yuen K Ip , Melody ML Soh , Xiu L Chen , Jasmine LY Ong , You R Chng

DOI: 10.1371/JOURNAL.PONE.0061163

关键词:

摘要: We obtained a full cDNA coding sequence of aquaporin 1aa (aqp1aa) from the gills freshwater climbing perch, Anabas testudineus, which had highest expression in and skin, suggesting an important role Aqp1aa these organs. Since seawater acclimation no significant effects on branchial intestinal aqp1aa mRNA expression, since gut was extremely low, it can be deduced that Aqp1aa, despite being water channel, did not play osmoregulatory A. testudineus. However, terrestrial exposure led to increases skin would lead evaporative loss, results further support proposition function predominantly for permeation through skin. Rather, increased might necessary facilitate ammonia excretion during emersion, because testudineus is known utilize amino acids as energy sources locomotor activity with production land. Furthermore, resulted decreases presumably reduce influx loading. This corroborates previous reports AQP1 able permeation. molecular characterization revealed its intrinsic aquapore NH3 transport. Hence, probably permeated central fifth pore tetramer suggested previously. Taken together, our indicate have greater physiological than osmoregulation

参考文章(81)
Shit F. Chew, Jonathan M. Wilson, Yuen K. Ip, David J. Randall, Nitrogen Excretion And Defense Against Ammonia Toxicity Fish Physiology. ,vol. 21, pp. 307- 395 ,(2005) , 10.1016/S1546-5098(05)21008-7
Stefan Hohmann, Solute Transport, Søren Nors Nielsen, Molecular Biology and Physiology of Water and Solute Transport ,(2012)
Christopher P. Cutler, Gordon Cramb, WATER TRANSPORT AND AQUAPORIN EXPRESSION IN FISH Springer, Boston, MA. pp. 433- 441 ,(2000) , 10.1007/978-1-4615-1203-5_57
G.M. Preston, J.S. Jung, W.B. Guggino, P. Agre, The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel. Journal of Biological Chemistry. ,vol. 268, pp. 17- 20 ,(1993) , 10.1016/S0021-9258(18)54108-9
W. B. Guggino, B. L. Smith, P. Agre, Jin Sup Jung, G. M. Preston, Molecular structure of the water channel through aquaporin CHIP. The hourglass model. Journal of Biological Chemistry. ,vol. 269, pp. 14648- 14654 ,(1994) , 10.1016/S0021-9258(17)36674-7
YK Ip, SF Chew, DJ Randall, None, Ammonia toxicity, tolerance, and excretion Fish Physiology. ,vol. 20, pp. 109- 148 ,(2001) , 10.1016/S1546-5098(01)20005-3
William R. Skach, A. S. Verkman, Lan Bo Shi, Functional independence of monomeric CHIP28 water channels revealed by expression of wild-type mutant heterodimers Journal of Biological Chemistry. ,vol. 269, pp. 10417- 10422 ,(1994) , 10.1016/S0021-9258(17)34076-0
Anchi Cheng, A. N. van Hoek, M. Yeager, A. S. Verkman, A. K. Mitra, Three-dimensional organization of a human water channel Nature. ,vol. 387, pp. 627- 630 ,(1997) , 10.1038/42517