The H,K-ATPase beta-subunit can act as a surrogate for the beta-subunit of Na,K-pumps.
J Biol Chem
; 266(29): 19131-4, 1991 Oct 15.
Article
en En
| MEDLINE
| ID: mdl-1717460
Na,K-ATPase and H,K-ATPase are the only members of the P-type ATPases in which a glycosylated beta-subunit is part of the purified active enzyme. In this study, we have followed the synthesis and the posttranslational processing of the beta-subunit of H,K-ATPase (beta HK) in Xenopus oocytes injected with beta HK cRNA and have tested whether it can act as a surrogate for the beta-subunit of Na,K-ATPase (beta NaK) to support the functional expression of Na,K-pumps. In Xenopus oocytes, beta HK is processed from an Endo H-sensitive 51-kDa coreglycosylated form to an Endo H-resistant 71-kDa fully glycosylated form. Similar to beta NaK, beta HK can stabilize and increase the trypsin resistance of alpha-subunits of Na,K-ATPase (alpha NaK). Finally, expression of beta HK together with alpha NaK leads to an increased number of ouabain binding sites at the plasma membrane accompanied by an increased Rb+ uptake and Na,K-pump current. Our data suggest that beta HK, similar to beta NaK, can assemble to alpha NaK, support the structural maturation and the intracellular transport of catalytic alpha NaK, and ultimately form active alpha NaK-beta HK complexes with Na,K-pump transport properties.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Adenosina Trifosfatasas
/
ATPasa Intercambiadora de Sodio-Potasio
Límite:
Animals
Idioma:
En
Revista:
J Biol Chem
Año:
1991
Tipo del documento:
Article
País de afiliación:
Suiza
Pais de publicación:
Estados Unidos