Ukr.Biochem.J. 2015; Volume 87, Issue 1, Jan-Feb, pp. 83-90
doi: https://doi.org/10.15407/ubj87.01.083
The influence of iron ions on ATP-hydrolases activity of cell membranes of rat colon smooth muscle and kidney
A. A. Kaplia
Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: kaplya@biochem.kiev.ua
To elucidate the specific features of the АТР- hydrolases structural resistance in the membrane under the action of the prooxidants: Fe2+ and hydrogen peroxide, and N-ethylmaleimide (NEM) the colonic smooth muscle (CSM) Na+,K+-AТРase activity was compared with activities of the corresponding Mg2+-АТР-hydrolase and ATP-ases from kidney medullar layer of rats. The inhibition study of the CSM Na+,K+-AТРase by divalent iron shows the decrease of the activity by 30% at 0.1 µM FeSO4 and in the range of 0.1-10 µM – to 45% of residual activity. When comparing with kidney enzyme (represents exclusively α1-isozyme) the CSM Na+,K+-AТРase sensitivity to Fe2+ is reliably higher at its submicromolar concentration. CSM Mg2+-АТРase is much more resistant to iron ions effect, than kidney one. However for two tissues Mg2+-АТРase activity is always more resistant as compared with corresponding Na+,K+-AТРase activity. Against 1 mM EGTA Na+,K+-AТРase and Mg2+-АТРase activities of GMOK and kidneys are equally insensitive to effect of hydrogen peroxide in concentration up to 1 mM. But in the presence of 20 µM FeSO4 in the concentration range of 1 nМ – 1 mM of Н2О2 the Na+,K+-AТРase is inhibited to greater extent, than Mg2+-АТРase activity. NEM sensitivity of the two АТР-hydrolase systems corresponds to prooxidant sensitivity that indicates the distinct importance of SH-groups for their functioning. It is concluded that Na+,K+-AТРase can serve as a marker of membrane sensitivity to oxidation, Mg2+-АТРase is resistant to oxidation and can be considered as criterion of the oxidation resistance when comparing membrane enzyme complexes, especially in GMOK.
Keywords: ATP-hydrolases, colonic smooth muscle, ferrum ions, hydrogen peroxide, kidney, N-ethylmaleimide, Na(+)-K(+)-ATPase, prooxidants
References:
- Baraboy V. A., Sutkovoy D. A. Oxidative and antioxidative homeostasis in norm and pathology. Kiev: Chernobylinform, 1997. 420 p. (In Russian).
- Lubianova I. P. Modern concepts about the methabolism of iron from the position of the occupational pathologist. Actual Problems of Transport Medicine. 2010;20(2):47-57. (In Russian).
- Iron overloading deseases (hemochromatosis). Ed. By A. G. Rummianceva and Yu. N. Tokareva. М: Medpractica Press, 2004. 325 p. (In Russian).
- Belous A. M., Konnic A. T. Physiological role of iron. Kiev: Naukova Dumka, 1991. 104 p. (In Russian).
- Iron and human disease. Ed. By Randall BnLauffer. CRC Press, Boca Raton Ann Arbor: London – Tokio, 1992. 534 p.
- Lingrel JB, Kuntzweiler T. Na+,K(+)-ATPase. J Biol Chem. 1994 Aug 5;269(31):19659-62. Review. PubMed
- Kaplia A. A. Structural organization and functional role of Na+,K+-ATР-ase isozymes. Kiev: Kiev University Press, 1998. 162 p. (In Russian).
- Blanco G. Na,K-ATPase subunit heterogeneity as a mechanism for tissue-specific ion regulation. Semin Nephrol. 2005 Sep;25(5):292-303. Review. PubMed
- Lingrel J, Moseley A, Dostanic I, Cougnon M, He S, James P, Woo A, O’Connor K, Neumann J. Functional roles of the alpha isoforms of the Na,K-ATPase. Ann N Y Acad Sci. 2003 Apr;986:354-9. PubMed
- Kaplia AA, Mishchuk DO. Na+,K+-ATPase isoenzymes of excitable tissues in pathological states. Ukr Biokhim Zhurn. 2001 Sep-Oct;73(5):17-22. Review. Russian. PubMed
- Kaplia AA, Khizhniak SV, Kudriavtseva AG, Papageorgakopulu N, Osinskiy DS. Na+,K+-ATPase and Ca2+-ATPase isozymes in malignant neoplasms. Ukr Biokhim Zhurn. 2006 Jan-Feb;78(1):29-42. Review. Russian. PubMed
- Kaplia AA, Morozova VS. Na+,K(+)-ATPase activity in polarized cells. Ukr Biokhim Zhurn (1999). 2010 Jan-Feb;82(1):5-20. Review. Russian. PubMed
- Knowles AF, Isler RE, Reece JF. The common occurrence of ATP diphosphohydrolase in mammalian plasma membranes. Biochim Biophys Acta. 1983 May 26;731(1):88-96. PubMed
- Knowles AF, Chiang WC. Enzymatic and transcriptional regulation of human ecto-ATPase/E-NTPDase 2. Arch Biochem Biophys. 2003 Oct 15;418(2):217-27. PubMed
- Boldyrev AA, Bulygina ER, Kramarenko GG. Is Na,K-ATPase the target of oxidative stress?. Biull Eksp Biol Med. 1996 Mar;121(3):275-8. Russian. PubMed
- Kako K, Kato M, Matsuoka T, Mustapha A. Depression of membrane-bound Na+-K+-ATPase activity induced by free radicals and by ischemia of kidney. Am J Physiol. 1988 Feb;254(2 Pt 1):C330-7. PubMed
- Rajasekaran AK, Rajasekaran SA. Role of Na-K-ATPase in the assembly of tight junctions. Am J Physiol Renal Physiol. 2003 Sep;285(3):F388-96. PubMed
- Kaplia AA. The heterogeneity of the Na+, K(+)-ATPase ouabain sensitivity in microsomal membranes of rat colon smooth muscles. Ukr Biokhim Zhurn. 2011 Sep-Oct;83(5):89-93. Russian. PubMed
- Burke EP, Sanders KM, Horowitz B. Sodium pump isozymes are differentially expressed in electrically dissimilar regions of colonic circular smooth muscle. Proc Natl Acad Sci USA. 1991 Mar 15;88(6):2370-4. PubMed, PubMedCentral
- Xie Z, Jack-Hays M, Wang Y, Periyasamy SM, Blanco G, Huang WH, Askari A. Different oxidant sensitivities of the alpha1 and alpha2 isoforms of Na+,K+-ATPase expressed in baculovirus-infected insect cells. Biochem Biophys Res Commun. 1995;207(1):155-159.
- Cadman E, Bostwick JR, Eichberg J. Determination of protein by a modified Lowry procedure in the presence of some commonly used detergents. Anal Biochem. 1979 Jul 1;96(1):21-3. PubMed
- Kaplia AA, Kudriavtseva AG, Kizhniak SV, Osinskiy DS, Demin EN. Na+,K+ -ATPase activity characteristics in human colon adenocarcinoma. Ukr Biokhim Zhurn. 2007 Jul-Aug;79(4):90-6. Russian. PubMed
- Kaplya O, Khyzhnyak S, Kudryavceva A, Dyomin E, Osynski D. Na+,K+-ATPase functioning in human colorectal adenocarcinomas depending on tumor differentiation. Annales Universitatis Mariae-Sklodowska (Lublin, Polonia). Sectio DDD. 2008;21(1):303-305.
- Chen PS, Toribara TY, Warner H. Microdetermination of phosphorus. Anal Chem. 1956;28(11):1756-1758.
- Huang WH, Wang Y, Askari A, Zolotarjova N, Ganjeizadeh M. Different sensitivities of the Na+/K(+)-ATPase isoforms to oxidants. Biochim Biophys Acta. 1994 Feb 23;1190(1):108-14. PubMed
- Huang WH, Wang Y, Askari A. (Na+ + K+)-ATPase: inactivation and degradation induced by oxygen radicals. Int J Biochem. 1992 Apr;24(4):621-6. PubMed
- Goldshleger R, Bar Shimon M, Or E, Karlish SJ. Metal-catalysed cleavage of Na,K-ATPase as a tool for study of structure-function relations. Acta Physiol Scand Suppl. 1998 Aug;643:89-97. Review. PubMed
- Goldshleger R, Patchornik G, Shimon MB, Tal DM, Post RL, Karlish SJ. Structural organization and energy transduction mechanism of Na+,K+-ATPase studied with transition metal-catalyzed oxidative cleavage. J Bioenerg Biomembr. 2001 Oct;33(5):387-99. Review. PubMed
- Krstić D, Krinulović K, Vasić V. Inhibition of Na+/K(+)-ATPase and Mg(2+)-ATPase by metal ions and prevention and recovery of inhibited activities by chelators. J Enzyme Inhib Med Chem. 2005 Oct;20(5):469-76. PubMed
- Floyd RV, Wray S, Quenby S, Martín-Vasallo P, Mobasheri A. Expression and distribution of Na, K-ATPase isoforms in the human uterus. Reprod Sci. 2010 Apr;17(4):366-76. PubMed, CrossRef
- Shelly DA, He S, Moseley A, Weber C, Stegemeyer M, Lynch RM, Lingrel J, Paul RJ. Na(+) pump alpha 2-isoform specifically couples to contractility in vascular smooth muscle: evidence from gene-targeted neonatal mice. Am J Physiol Cell Physiol. 2004 Apr;286(4):C813-20. PubMed
