PUBLICATION
Knockdown of V-ATPase subunit A ({alpha}tp6v1{alpha}) impairs acid secretion and ion balance in zebrafish Danio rerio
- Authors
- Horng, J.L., Lin, L.Y., Huang, C.J., Katoh, F., Kaneko, T., and Hwang, P.P.
- ID
- ZDB-PUB-070212-26
- Date
- 2007
- Source
- American journal of physiology. Regulatory, integrative and comparative physiology 292(5): R2068-2076 (Journal)
- Registered Authors
- Horng, Jiun-Lin, Huang, Chang-Jen, Hwang, Pung Pung
- Keywords
- H+-ATPase, HR cell, morpholino-knockdown, Na+, Ca2+
- MeSH Terms
-
- Acids/metabolism*
- Animals
- Embryo, Nonmammalian/metabolism*
- Fresh Water
- Gene Expression Regulation, Enzymologic
- Mutation
- Protein Subunits/deficiency
- Protein Subunits/genetics
- Protein Subunits/metabolism
- Proton-Translocating ATPases/chemistry
- Proton-Translocating ATPases/deficiency*
- Proton-Translocating ATPases/genetics
- Proton-Translocating ATPases/metabolism
- Protons
- Vacuolar Proton-Translocating ATPases/deficiency
- Vacuolar Proton-Translocating ATPases/genetics*
- Vacuolar Proton-Translocating ATPases/metabolism*
- Water-Electrolyte Balance*
- Yolk Sac/metabolism
- Zebrafish/metabolism*
- Zebrafish Proteins/deficiency
- Zebrafish Proteins/genetics*
- Zebrafish Proteins/metabolism*
- PubMed
- 17272665 Full text @ Am. J. Physiol. Regul. Integr. Comp. Physiol.
Citation
Horng, J.L., Lin, L.Y., Huang, C.J., Katoh, F., Kaneko, T., and Hwang, P.P. (2007) Knockdown of V-ATPase subunit A ({alpha}tp6v1{alpha}) impairs acid secretion and ion balance in zebrafish Danio rerio. American journal of physiology. Regulatory, integrative and comparative physiology. 292(5):R2068-2076.
Abstract
In the skin of zebrafish embryo, the vacuolar H(+)-ATPase (V-ATPase, H(+) pump) distributed mainly in the apical membrane of H(+)-pump rich cells, which pump internal acid out of the embryo and function similar to acid-secreting intercalated cells in mammalian kidney. In addition to acid excretion, the electrogenic H(+) efflux via the H(+)-ATPases in the gill apical membrane of freshwater fish was proposed to act as a driving force for Na(+) entry through the apical Na(+) channels. However, convincing molecular physiological evidence in vivo for this model is still lacking. In this study, we used morpholino-modified antisense oligo-nucleotides to knockdown the gene product of H(+)-ATPase subunit A (alphatp6v1alpha) and examined the phenotype of the mutants. The H(+)-ATP knockdown embryos revealed several abnormalities, including suppression of acid-secretion from skin, growth retardation, trunk deformation, and loss of internal Ca(2+) and Na(+). This finding reveals the critical role of H(+)-ATPase in embryonic acid-secretion and ion balance as well. Key words: H+-ATPase, morpholino-knockdown, acid/base regulation, Na+, Ca2+
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping