[KSCI] Korea Science Citation Index Service

http://dx.doi.org/10.9799/ksfan.2016.29.1.033

Immunohistolocalization of Carbonic Anhydrase in Kidney and Intestine of Rainbow Trout, Oncorhynchus mykiss

Kim, Soo Cheol (Dept. of Biotechnology and Chemical Engineering, College of Engineering, Chonnam National University)
Kim, Jung Woo (Dept. of Anatomy, College of Medicine, Seonam University)
Choi, Myeong Rak (Dept. of Biotechnology and Chemical Engineering, College of Engineering, Chonnam National University)
Choi, Kap Seong (School of Food Science, Sunchon National University)
Kho, Kang Hee (Dept. of Aquatic Biology, College of Fisheries and Ocean Sciences, Chonnam National University)

Publication Information

The Korean Journal of Food And Nutrition / v.29, no.1, 2016 , pp. 33-36 More about this Journal

Abstract

Carbonic anhydrase is essential for the cellular transportation of hydrogen and bicarbonate ions and plays a key role in a wide variety of physiological processes. Rainbow trout, Oncorhynchus mykiss is an important freshwater fish in aquaculture industry and is known to be one of the most susceptible species to environmental contamination. In this study, carbonic anhydrase was detected in the kidney and intestine of rainbow trout. Carbonic anhydrase was isolated from cytosolic proteins and identified by using SDS-PAGE, isoelectric focusing, and immunohistochemical methods. A specific protein band with molecular weight of 30 kDa and pI of 7.0 was detected by Western blotting. The immunohistochemical results showed that carbonic anhydrase was located at various cells in the kidney and intestine of rainbow trout.

Keywords

carbonic anhydrase; rainbow trout; kidney; intestine; immunohistolocalization;

Citations & Related Records

Reference

1	Brack W, Schirmer K. 2003. Effect-directed identification of oxygen and sulfur heterocycles as major polycyclic aromatic cytochrome P 4501 A-inducers in a contaminated sediment. Environ Sci Technol 37:3062-3070 DOI
2	Chegwidden WR, Carter ND. 2000. Introduction to the carbonic anhydrase. In: Chegwidden WR, Carter ND and Edwards YH (eds) The Carbonic Anhydrases, New Horizons, Birkhauser Verlag, Basel, pp 13-28
3	Fridborg K, Kannan K, Liljas A, Lundin J, Strandberg R, Tilander B, Wiren G. 1967. Crystal structure of human erythrocyte carbonic anhydrase C.3. Molecular structure of enzyme and of one enzyme-inhibitor complex at 5.5 $A^{\circ}$ resolution. J Mol Biol 25:505-516 DOI
4	Hewett-Emmett D, Tashian RE. 1996. Functional diversity, conservation, and convergence in the revolution of the ${\alpha}-,\;{\beta}-$ , and ${\gamma}-$ carbonic anhydrase gene families. Mol Phylogenet Evol 5:50-77 DOI
5	Kannan K, Liljas A, Waara I, Bergsten PC, Lovgren S, Strandberg B, Bengtsson U, Carlbom U, Fridborg K, Jarup L, Petef M. 1971. Crystal structure of human erythrocyte carbonic anhydrase C.6. 3-dimensional structure at high resolution in relation to other mammalian carbonic anhydrases. Quant Biol 36:221-231
6	Kwak DJ, Choi KS, Han KH, Kho KH. 2011. Discovery of carbonic anhydrase isozyme in sea bass and rainbow trout. J Korean Soc Appl Biol Chem 54:649-652
7	Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277:680-685
8	Liljas A, Kannan K, Bergsten PC, Waara I, Fridborg K, Strandberg B, Carlbom U, Jarup L, Lovgren S, Petef M. 1972. Crystal structure of human carbonic anhydrase C. Nature New Biol 235:131-137
9	Linser P. 1991. Comparative immunochemistry of elasmobranch retina muller cells and horizontal cells. J Exp Zool 5:88-96
10	Lionetto MG, Giordano ME, Vilella S, Schettino T. 2000. Inhibition of eel enzymatic activities by cadmium. Aquat Toxicol 48:561 DOI
11	Rahim SM, Delaunoy JP, Laurent P. 1988. Identification and immunocytochemical localization of two different carbonic anhydrase isoenzymes in teleostean fish erythrocytes and gill epithelia. Histochem 89:451-459 DOI
12	Smith KS, Ferry JG. 2000. Prokaryotic carbonic anhydrase. FEMS Microbiol Rev 24:335-366 DOI
13	Supuran CT. 2008a. Carbonic anhydrases-an overview. Curr Pharm Des 14:603-614 DOI
14	Supuran CT. 2008b. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov 7:168-181 DOI
15	Xu Y, Feng L, Jeffrey PD, Shi Y, Morel FM. 2008. Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms. Nature 452:56-61 DOI
16	Tashian RE. 1989. The carbonic anhydrases: widening perspectives on their evolution, expression and function. Bioessays 10:186-192 DOI
17	Wilson JM, Randall DJ, Vogl AW, Harris J, Sly WS, Iwama GK. 2000. Branchial carbonic anhydrase is present in dogfish, Squalus acanthias. Fish Physiol Biochem 22:329-336 DOI