Immunohistochemical detection of P‐glycoprotein in teleost tissues using mammalian polyclonal and monoclonal antibodies

Abstract

Mammalian P-glycoprotein is a highly conserved 170-kD integral plasma membrane protein functioning as an energy-dependent efflux pump of exogenous and endogenous lipophilic aromatic compounds entering the cell by diffusion. In this study, the tissue specificities of one polyclonal (pAb) and three monoclonal (mAbs) antibodies to mammalian P-glycoprotein were identified in paraffin-embedded, parasagittal whole-body sections of the guppy Poecilia reticulata. Polyclonal antibody mdr(Ab-1) and mAbs C219, C494, and JSB-1 demonstrated differential staining patterns in the following tissues: bile canaliculi in the liver, exocrine pancreas, lumenal surface of the intestinal epithelium, renal tubules, interrenal tissue, branchial blood vessels, gas gland, pseudobranch, and the gill transverse septa. Positive P-glycoprotein expression in P. reticulata correlates well with published results for homologous mammalian tissues of secretory and excretory function. These data indicate that one or more highly conserved members of the P-glycoprotein transporter family exist in a teleost species and can be detected using commercially available mammalian antibodies.