Regulation of sodium/potassium ATPase activity: Impact on salt balance and vascular contractility

被引:30
作者
Aperia A. [1 ]
机构
[1] Department of Women and Child Health, Karolinska Institutet
关键词
Dopamine; ATPase Activity; Ouabain; Atrial Natriuretic Peptide; Cytoskeleton Protein;
D O I
10.1007/s11906-001-0032-8
中图分类号
学科分类号
摘要
Na+,K+-ATPase distributes ions between the intracellular and extracellular space and is responsible for total-body sodium homeostasis. The activity of this ion pump is regulated by catecholamines and peptide hormones; by the ligand of Na+,K+-ATPase, ouabain; and by direct interaction with cytoskeleton proteins. This review summarizes recent advances in the field of short-term regulation of Na+,K+- ATPase and the implications of these advances for the regulation of blood pressure. Renal Na+,K+-ATPase activity is bidirectionally regulated by natriuretic and antinatriuretic hormones, and a shift in the balance between these forces may lead to salt retention and hypertension. Dopamine plays a key role in this interactive regulation. By inhibiting vascular Na +,K+-ATPase activity, an excess of circulating ouabain may increase calcium concentration in vascular cells and lead to increased vascular contractility. Finally, mutations in cytoskeleton proteins may stimulate renal Na+,K+-ATPase activity by way of protein/protein interaction and lead to salt retention and hypertension. Abnormalities in the systems regulating Na+,K+-ATPase should be explored further in the search for the multiple causes of essential hypertension. Copyright © 2001 by Current Science Inc.
引用
收藏
页码:165 / 171
页数:6
相关论文
共 56 条
[1]
Lingrel J.B., Kuntzweiler T., Na+,K(+)-ATPase, J Biol Chem, 269, pp. 19659-19662, (1994)
[2]
Lingrel J.B., Croyle M.L., Woo A.L., Et al., Ligand binding sites of Na,K-ATPase, Acta Physiol Scand Suppl, 643, pp. 69-77, (1998)
[3]
Crambert G., Hasler U., Beggah A.T., Et al., Transport and pharmacological properties of nine different human Na,KATPase isozymes, J Biol Chem, 275, pp. 1976-1986, (2000)
[4]
Therien A.G., Blostein R., Mechanisms of sodium pump regulation, Am J Physiol, 279, (2000)
[5]
Bertorello A., Aperia A., Walaas I., Et al., Phosphorylation of the catalytic subunit of Na+,K+-ATPase inhibits the activity of the enzyme, Proc Natl Acad Sci U S A, 88, pp. 11359-11362, (1991)
[6]
Fisone G., Cheng S.X.-J., Nairn A.C., Et al., Identification of the phosphorylation site for cAMP-dependent protein kinase on Na+,K+ATPase and effects of site-directed mutagenesis, J Biol Chem, 269, pp. 9368-9373, (1994)
[7]
Logvinenko N.S., Dulubova I., Fedosova N., Et al., Phosphorylation by protein kinase C of serine-23 of the a-1 subunit of rat Na+,K+-ATPase affects its conformational equilibrium, Proc Natl Acad Sci U S A, 93, pp. 9132-9137, (1996)
[8]
Belusa R., Wang Z., Matsubara T., Et al., Mutation of the site of protein kinase C phosphorylation on rat a1 Na+,K+-ATPase alters regulation of intracellular Na+, pH and influences cell shape and adhesiveness, J Biol Chem, 272, pp. 20179-20184, (1997)
[9]
Feschenko M.S., Sweadner K.J., Structural basis for species-specific differences in the phosphorylation of Na,K-ATPase by protein kinase C, J Biol Chem, 270, pp. 14072-14077, (1995)
[10]
Cheng X.J., Hoog J.O., Nairn A.C., Et al., Regulation of rat Na(+)-K(+)-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA, Am J Physiol, 273, 6 PART 1, (1997)