University of Surrey

Test tubes in the lab Research in the ATI Dance Research

Isoforms of Na+,K+-ATPase in primary human bone derived osteoblasts

Mobasheri, A, Trujillo, E, Golding, S, Ellory, JC, Pagakis, SN, Pocock, AE, Martin-Vasallo, P and Francis, MJO (2000) Isoforms of Na+,K+-ATPase in primary human bone derived osteoblasts Journal of Biochemistry, Molecular Biology and Biophysics, 4 (5). pp. 343-357.

Full text not available from this repository.


Osteoblasts play a critical role in bone formation and mineralization, a process that depends on optimal calcium and phosphate homeostasis. Transcellular transport of free calcium [Ca2+], uptake of inorganic phosphate (P(i)) and numerous other transport systems in osteoblasts depend on a low intracellular Na+:K+ ratio furnished by (Na++K+)-stimulated adenosine triphosphatase (Na+,K+-ATPase), an enzyme embedded in the plasma membrane. In this study, we have examined, for the first time, the expression of the catalytic α and regulatory β subunit isoforms of Na+,K+-ATPase in primary human bone derived osteoblasts using isoform specific monoclonal and polyclonal antibodies. Immunofluorescence was used to detect the α1, β1 and β2 isoforms of Na+,K+-ATPase in dispersed osteoblasts. Laser scanning confocal microscopy also revealed an abundance of Na+,K+-ATPase isoforms in subcellular compartments. The existence of α1, β1 and β2 suggests that at least two major isozyme combinations of Na+,K+-ATPase are present in human bone (α1β1,α1β2).

Item Type: Article
Divisions : Surrey research (other units)
Authors :
Trujillo, E
Golding, S
Ellory, JC
Pagakis, SN
Pocock, AE
Martin-Vasallo, P
Francis, MJO
Date : 1 January 2000
Depositing User : Symplectic Elements
Date Deposited : 17 May 2017 10:17
Last Modified : 24 Jan 2020 18:54

Actions (login required)

View Item View Item


Downloads per month over past year

Information about this web site

© The University of Surrey, Guildford, Surrey, GU2 7XH, United Kingdom.
+44 (0)1483 300800