The P-glycoprotein gene family of Caenorhabditis elegans

Lincke, Carsten R.; Groenigen, Marjon van; Borst, Piet

doi:10.1016/0022-2836(92)90855-e

Cited by 76 publications

(33 citation statements)

References 43 publications

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“…1991). The constructs are subclones derived from bacterial phage X clones containing genomic DNA made by Lincke et al (1992 NLl36[pgp-l(pkExv581)], a wild-type strain over-expressing pgp-l as a transgene, ]. with the pgp-3 gene as a transgene in a pg/,-3 deletion mutant background, pgp-l(pkEx58l)], containing pgp-I as a transgene in a pgp-3 mutant background, and NL143 [pgp-l(pkl7) ].…”

Section: Generating Transgenic Nematodesmentioning

confidence: 99%

“…They share similarities with mammalian P-glycoproteins in their predicted protein structure (Lincke et al, 1992; A.Broeks, unpublished results). pgp-l and pgp-3 are expressed throughout the life cycle and promoter-LacZ fusion experiments indicated that they are exclusively expressed in the intestinal cells (Lincke et al, 1993).…”

mentioning

confidence: 90%

“…P-glycoproteins are also found in many other organisms, e.g. invertebrates (Wu et al, 1991;Lincke et al, 1992;Gerrard et al, 1993) and parasitic protozoa (Foote et al, 1989;Wilson et al, 1989;Ouellette et al, 1990;Samuelson et al, 1990; Legare et al, 1995). In Drosophila melanogaster three P-glycoprotein genes have been identified and at least one of them (Mdr49) has been suggested to be implicated in drug resistance (Wu et al, 1991).…”

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confidence: 99%

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A P-glycoprotein protects Caenorhabditis elegans against natural toxins

Broeks¹,

Janssen²,

Calafat³

et al. 1995

Parasitology Today

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Section: Generating Transgenic Nematodesmentioning

confidence: 99%

mentioning

confidence: 90%

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confidence: 99%

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A P-glycoprotein protects Caenorhabditis elegans against natural toxins

Broeks¹,

Janssen²,

Calafat³

et al. 1995

Parasitology Today

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“…Notably Stage-specific expression of pgp genes To examine whether the more intense and uniform staining patterns of early larval stages correlated with steady state levels of native pgp mRNA during development, we analyzed these levels by RNase-protection assays (Figure 3). An actin-IV probe was used in these experiments as internal control and pgp-2, a third pgp gene (Lincke et al, 1992) not yet studied by lacZ fusion experiments, was included in these experiments. The mRNAs ofpgp-1, pgp-2 and pgp-3 were detectable throughout the life cycle of C. elegans.…”

Section: Resultsmentioning

confidence: 99%

“…These genes share extensive structural homology with their mammalian counterparts (Lincke et al, 1992). We have analyzed the tissuespecific expression of these genes by generating transgenic worms carrying genomic pgp sequences expected to control pgp gene expression fused to a modified bacterial lacZ reporter gene (Fire et al, 1990).…”

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confidence: 99%

The expression of two p-glycoprotein (pgp) genes in transgenic caenorhabditis elegans is confined to intestinal cells

1993

Parasitology Today

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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.

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The expression of two P-glycoprotein (pgp) genes in transgenic Caenorhabditis elegans is confined to intestinal cells.

et al. 1993

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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.

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The P-glycoprotein gene family of Caenorhabditis elegans

Cited by 76 publications

References 43 publications

A P-glycoprotein protects Caenorhabditis elegans against natural toxins

A P-glycoprotein protects Caenorhabditis elegans against natural toxins

The expression of two p-glycoprotein (pgp) genes in transgenic caenorhabditis elegans is confined to intestinal cells

The expression of two P-glycoprotein (pgp) genes in transgenic Caenorhabditis elegans is confined to intestinal cells.

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