Abstract

BackgroundSLC22 protein family is a member of the SLC (Solute carriers) superfamily of polyspecific membrane transporters responsible for uptake of a wide range of organic anions and cations, including numerous endo- and xenobiotics. Due to the lack of knowledge on zebrafish Slc22 family, we performed initial characterization of these transporters using a detailed phylogenetic and conserved synteny analysis followed by the tissue specific expression profiling of slc22 transcripts.ResultsWe identified 20 zebrafish slc22 genes which are organized in the same functional subgroups as human SLC22 members. Orthologies and syntenic relations between zebrafish and other vertebrates revealed consequences of the teleost-specific whole genome duplication as shown through one-to-many orthologies for certain zebrafish slc22 genes. Tissue expression profiles of slc22 transcripts were analyzed using qRT-PCR determinations in nine zebrafish tissues: liver, kidney, intestine, gills, brain, skeletal muscle, eye, heart, and gonads. Our analysis revealed high expression of oct1 in kidney, especially in females, followed by oat3 and oat2c in females, oat2e in males and orctl4 in females. oct1 was also dominant in male liver. oat2d showed the highest expression in intestine with less noticeable gender differences. All slc22 genes showed low expression in gills, and moderate expression in heart and skeletal muscle. Dominant genes in brain were oat1 in females and oct1 in males, while the highest gender differences were determined in gonads, with dominant expression of almost all slc22 genes in testes and the highest expression of oat2a.ConclusionsOur study offers the first insight into the orthology relationships, gene expression and potential role of Slc22 membrane transporters in zebrafish. Clear orthological relationships of zebrafish slc22 and other vertebrate slc22 genes were established. slc22 members are mostly highly conserved, suggesting their physiological and toxicological importance. One-to-many orthologies and differences in tissue expression patterns of zebrafish slc22 genes in comparison to human orthologs were observed. Our expression data point to partial similarity of zebrafish versus human Slc22 members, with possible compensatory roles of certain zebrafish transporters, whereas higher number of some orthologs implies potentially more diverse and specific roles of these proteins in zebrafish.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-016-2981-y) contains supplementary material, which is available to authorized users.

Highlights

  • SLC22 protein family is a member of the Solute Carrier (SLC) (Solute carriers) superfamily of polyspecific membrane transporters responsible for uptake of a wide range of organic anions and cations, including numerous endo- and xenobiotics

  • This assumption is supported by the highest expression of oct2 in comparison to other examined slc22 transcripts in zebrafish eye, which is similar to expression of human and murine OCT3/Oct3 in the eye, where it plays an important role in absorption, distribution and clearance of various xenobiotic substrates [54, 55]

  • Phylogenetic and synteny analysis of SLC22/slc22 genes point to certain similarities among human and zebrafish Slc22 transporters

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Summary

Introduction

SLC22 protein family is a member of the SLC (Solute carriers) superfamily of polyspecific membrane transporters responsible for uptake of a wide range of organic anions and cations, including numerous endo- and xenobiotics. Human SLC22 protein family belongs to the large Solute Carrier (SLC) superfamily of plasma membrane proteins which is a part of the Major Facilitator Superfamily (MFS) clan of proteins [1]. It is a highly diverse group of transport proteins comprising uniporters, symporters, and antiporters which facilitate the transport of a large number of substrates including ions, drugs, neurotransmitters, nucleosides, amino acids, and peptides across biological membranes. The order and localization of TMDs structurally define the polyspecific active region of the SLC22 transporters [4]

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