PMID- 10362770
OWN - NLM
STAT- MEDLINE
DCOM- 19990722
LR  - 20181127
IS  - 0002-9513 (Print)
IS  - 0002-9513 (Linking)
VI  - 276
IP  - 6
DP  - 1999 Jun
TI  - The nongastric H+-K+-ATPases: molecular and functional properties.
PG  - F812-24
LID - 10.1152/ajprenal.1999.276.6.F812 [doi]
AB  - The Na-K/H-K-ATPase gene family is divided in three subgroups including the
      Na-K-ATPases, mainly involved in whole body and cellular ion homeostasis, the
      gastric H-K-ATPase involved in gastric fluid acidification, and the newly
      described nongastric H-K-ATPases for which the identification of physiological
      roles is still in its infancy. The first member of this last subfamily was first 
      identified in 1992, rapidly followed by the molecular cloning of several other
      members. The relationship between each member remains unclear. The functional
      properties of these H-K-ATPases have been studied after their ex vivo expression 
      in various functional expression systems, including the Xenopus laevis oocyte,
      the insect Sf9 cell line, and the human HEK 293 cells. All these H-K-ATPase
      alpha-subunits appear to encode H-K-ATPases when exogenously expressed in such
      expression systems. Recent data suggest that these H-K-ATPases could also
      transport Na+ in exchange for K+, revealing a complex cation transport
      selectivity. Moreover, they display a unique pharmacological profile compared
      with the canonical Na-K-ATPases or the gastric H-K-ATPase. In addition to their
      molecular and functional characterizations, a major goal is to correlate the
      molecular expression of these cloned H-K-ATPases with the native K-ATPases
      activities described in vivo. This appears to be more complex than anticipated.
      The discrepancies between the functional data obtained by exogenous expression of
      the nongastric H-K-ATPases and the physiological data obtained in native organs
      could have several explanations as discussed in the present review. Extensive
      studies will be required in the future to better understand the physiological
      role of these H-K-ATPases, especially in disease processes including ionic or
      acid-base disorders.
FAU - Jaisser, F
AU  - Jaisser F
AD  - Institut National de la Sante et de la Recherche Medicale, Unite 478, Institut
      Federatif de Recherche Cellules Epitheliales, Faculte de Medecine Xavier Bichat, 
      Universite Paris VII, F-75870 Paris Cedex 18, France. jaisser@bichat.inserm.fr
FAU - Beggah, A T
AU  - Beggah AT
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - United States
TA  - Am J Physiol
JT  - The American journal of physiology
JID - 0370511
RN  - EC 3.6.3.10 (H(+)-K(+)-Exchanging ATPase)
SB  - IM
MH  - Amino Acid Sequence/genetics
MH  - Animals
MH  - H(+)-K(+)-Exchanging ATPase/*genetics/*metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Multigene Family/genetics
RF  - 82
EDAT- 1999/06/11 00:00
MHDA- 1999/06/11 00:01
CRDT- 1999/06/11 00:00
PHST- 1999/06/11 00:00 [pubmed]
PHST- 1999/06/11 00:01 [medline]
PHST- 1999/06/11 00:00 [entrez]
AID - 10.1152/ajprenal.1999.276.6.F812 [doi]
PST - ppublish
SO  - Am J Physiol. 1999 Jun;276(6):F812-24. doi: 10.1152/ajprenal.1999.276.6.F812.