Authors
Shmukler, Boris E.Clark, Jeffrey S.
Hsu, Ann
Vandorpe, David H.
Stewart, Andrew K.
Kurschat, Christine E.
Choe, Seong-Kyu
Zhou, Yi
Amigo, Julio D.
Paw, Barry H.
Alper, Seth L.
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyProgram in Gene Function and Expression
Graduate School of Biomedical Sciences
Document Type
Journal ArticlePublication Date
2007-11-30Keywords
Zebrafish; Zebrafish Proteins; Anion Transport Proteins; XenopusLife Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
The genome of zebrafish (Danio rerio) encodes two unlinked genes equally closely related to the SLC4A2/AE2 anion exchanger genes of mammals. One of these is the recently reported zebrafish ae2 gene (Shmukler BE, Kurschat CE, Ackermann GE, Jiang L, Zhou Y, Barut B, Stuart-Tilley AK, Zhao J, Zon LI, Drummond IA, Vandorpe DH, Paw BH, Alper SL. Am J Physiol Renal Physiol Renal Physiol 289: F835-F849, 2005), now called ae2.1. We now report the structural and functional characterization of Ae2.2, the product of the second zebrafish Ae2 gene, ae2.2. The ae2.2 gene of zebrafish linkage group 24 encodes a polypeptide of 1,232 aa in length, sharing 70% amino acid identity with zebrafish Ae2.1 and 67% identity with mouse AE2a. Zebrafish Ae2.2 expressed in Xenopus oocytes encodes a 135-kDa polypeptide that mediates bidirectional, DIDS-sensitive Cl(-)/Cl(-) exchange and Cl(-)/HCO(3)(-) exchange. Ae2.2-mediated Cl(-)/Cl(-) exchange is cation independent, voltage insensitive, and electroneutral. Acute regulation of anion exchange mediated by Ae2.2 includes activation by NH(4)(+) and independent inhibition by acidic intracellular pH and by acidic extracellular pH. In situ hybridization reveals low-level expression of Ae2.2 mRNA in zebrafish embryo, most notably in posterior tectum, eye, pharynx, epidermal cells, and axial vascular structures, without notable expression in the Ae2.1-expressing pronephric duct. Knockdown of Ae2.2 mRNA, of Ae2.1 mRNA, or of both with nontoxic or minimally toxic levels of N-morpholino oligomers produced no grossly detectable morphological phenotype, and preserved normal structure of the head and the pronephric duct at 24 h postfertilization.Source
2007 Nov 28. Link to article on publisher's siteDOI
10.1152/ajpregu.00690.2007Permanent Link to this Item
http://hdl.handle.net/20.500.14038/33681PubMed ID
18046018Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1152/ajpregu.00690.2007