The abts and sulp families of anion transporters from Caenorhabditis elegans

被引:24
作者
Sherman, T
Chernova, MN
Clark, JS
Jiang, LW
Alper, SL
Nehrke, K
机构
[1] Univ Rochester, Med Ctr, Nephrol Unit, Dept Med, Rochester, NY 14642 USA
[2] Univ Rochester, Med Ctr, Dept Pharmacol & Physiol, Rochester, NY 14642 USA
[3] Beth Israel Deaconess Med Ctr, Mol & Vasc Med Unit, Boston, MA 02215 USA
[4] Beth Israel Deaconess Med Ctr, Div Renal, Boston, MA 02215 USA
[5] Harvard Univ, Sch Med, Dept Med, Boston, MA 02115 USA
来源
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY | 2005年 / 289卷 / 02期
关键词
D O I
10.1152/ajpcell.00071.2005
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The slc4 and slc26 gene families encode two distinct groups of gene products that transport HCO3- and other anions in mammalian cells. The SLC4 and SLC26 proteins are important contributors to transepithelial movement of fluids and electrolytes and to cellular pH and volume regulation. Herein we describe the cDNA cloning from the nematode Caenorhabditis elegans of four anion bicarbonate transporter (abts) homologs of slc4 cDNA and eight sulfate permease (sulp) homologs of slc26 cDNA. Analysis of transgenic nematode strains carrying promoter:: GFP fusions suggests relatively restricted expression patterns for many of these genes. At least three genes are expressed primarily in the intestine, three are expressed primarily in the excretory cell, and one is expressed in both of these polarized cell types. One of the genes is also expressed exclusively in the myoepithelium-like cells of the pharynx. Many of the sulp gene products localize to the basolateral membrane rather than to the apical membrane. Several ABTS and SULP proteins exhibited anion transport function in Xenopus oocytes. The strongest Cl- transporter among these also mediated Cl-/HCO3- exchange. These findings encourage exploitation of the genetic strengths of the nematode model system in the study of the physiological roles of anion transport by the proteins of these two highly conserved gene families.
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收藏
页码:C341 / C351
页数:11
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