Mj. Hemmer et al., IMMUNOHISTOCHEMICAL DETECTION OF P-GLYCOPROTEIN IN TELEOST TISSUES USING MAMMALIAN POLYCLONAL-ANTIBODIES AND MONOCLONAL-ANTIBODIES, The Journal of experimental zoology, 272(1), 1995, pp. 69-77
Mammalian P-glycoprotein is a highly conserved 170-kD integral plasma
membrane protein functioning as an energy-dependent efflux pump of exo
genous and endogenous lipophilic aromatic compounds entering the cell
by diffusion. In this study, the tissue specificities of one polyclona
l (pAb) and three monoclonal (mAbs) antibodies to mammalian P-glycopro
tein were identified in paraffin-embedded, parasagittal whole-body sec
tions of the guppy Poecilia reticulata. Polyclonal antibody mdr(Ab-l)
and mAbs C219, C494, and JSB-1 demonstrated differential staining patt
erns 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 mam
malian tissues of secretory and excretory function. These data indicat
e that one or more highly conserved members of the P-glycoprotein tran
sporter family exist in a teleost species and can be detected using co
mmercially available mammalian antibodies. (C) 1995 Wiley-Liss, Inc.