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Na+/K+-ATPase is a membrane protein and plays a key role in osmotic regulation in living organisms. In the present study, a cDNA sequence encoding the Na+/K+-ATPase alpha subunit from the monogonont rotifer, Brachionus koreanus was cloned by rapid amplification of cDNA ends technique. To investigate the role of this enzyme in osmotic stress, enzymatic activities of Na+/K+-ATPase were measured after exposure to different salinities for 48 h. The full-length Bk Na+/K+-ATPase cDNA was 3069 bp-long, encoding a 1022-amino acid polypeptide. Bk Na+/K+- ATPase possesses eight membrane spanning regions and five conserved domains. Phylogenetic analysis showed that Bk Na+/K+-ATPase had high identity with those of other species, and was closely clustered with other Brachionus sp. These findings indicate that this protein was conserved both structurally and functionally. B. koreanus Na+/K+-ATPase activity was stimulated in both hyposaline (6 psu) and hypersaline (32 psu) conditions, suggesting that this protein may play a role in osmoregulation. This study would provide better understanding of the physiology of B. koreanus and this enzyme may be useful as a molecular marker for evaluation of osmotic stress in aquatic environment.
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참고문헌 (37)
참고문헌 신청
Barwe SP / 2005 / Novel role for Na,K-ATPase in phosphatidylinositol 3-kinase signaling and suppression of cell motility / Mol. Biol. Cell 16:1082~1094
Blanco G / 1998 / Isozymes of the Na-K-ATPase: heterogeneity in structure, diversity in function / Am. J. Physiol 275:F633~F650
Bradford MM / 1976 / A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding / Anal. Biochem 7:248~254
Brooks SJ / 2003 / The effect of copper on osmoregulation in the freshwater amphipod Gammarus Pulex / Comp. Biochem. Physiol. A Mol. Integr. Physiol 135:527~537
Colina C / 2007 / Structural basis of Na+/K+-ATPase adaptation to marine environments / Nat. Struct. Mol. Biol 14:427~431
Blanco G / 1998 / Isozymes of the Na-K-ATPase: heterogeneity in structure, diversity in function / Am. J. Physiol 275:F633~F650
Bradford MM / 1976 / A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding / Anal. Biochem 7:248~254
Brooks SJ / 2003 / The effect of copper on osmoregulation in the freshwater amphipod Gammarus Pulex / Comp. Biochem. Physiol. A Mol. Integr. Physiol 135:527~537
Colina C / 2007 / Structural basis of Na+/K+-ATPase adaptation to marine environments / Nat. Struct. Mol. Biol 14:427~431
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