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The expression of two P‐glycoprotein (pgp) genes in transgenic Caenorhabditis elegans is confined to intestinal cells.
Author(s) -
Lincke C.R.,
Broeks A.,
The I.,
Plasterk R.H.,
Borst P.
Publication year - 1993
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1993.tb05806.x
Subject(s) - biology , caenorhabditis elegans , p glycoprotein , gene , transgene , caenorhabditis , glycoprotein , microbiology and biotechnology , membrane glycoproteins , genetics , gene expression , genetically modified mouse , multiple drug resistance , antibiotics
P‐glycoproteins can cause multidrug resistance in mammalian tumor cells by active extrusion of cytotoxic drugs. The natural function of these evolutionarily conserved, membrane‐bound ATP binding transport proteins is unknown. In mammals, P‐glycoproteins are abundantly present in organs associated with the digestive tract. We have studied the tissue‐specific expression of Caenorhabditis elegans P‐glycoprotein genes pgp‐1 and pgp‐3 by transformation of nematodes with pgp‐lacZ gene fusion constructs in which the promoter area of the pgp genes was fused to the coding region of lacZ. Expression of pgp‐1 and pgp‐3, as inferred from pgp‐lacZ transgenic nematodes, was confined to the intestinal cells. The expression patterns of both genes were virtually indistinguishable. Quantitative analysis of pgp mRNA levels during development showed that pgp‐1, −2, and −3 were expressed throughout the life cycle of C.elegans, albeit with some variation indicating developmental regulation. The expression of P‐glycoprotein genes in intestinal cells is an evolutionarily conserved feature of these genes, consistent with the hypothesis that P‐glycoproteins provide a mechanism of protection against environmental toxins.