New members of the mammalian P-glycoprotein gene family and their evolution.
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New members of the mammalian P-glycoprotein gene family and their evolution. by Sarah Jane Childs

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Published .
Written in English


Book details:

Edition Notes

Thesis (Ph.D.) -- University of Toronto, 1995.

The Physical Object
Pagination110 leaves.
Number of Pages110
ID Numbers
Open LibraryOL19733378M

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P-glycoprotein 1 (permeability glycoprotein, abbreviated as P-gp or Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) or cluster of differentiation (CD) is an important protein of the cell membrane that pumps many foreign substances out of cells. More formally, it is an ATP-dependent efflux pump with broad substrate Aliases: ABCB1, ABC20, CD, CLCS, GP, .   P-glycoprotein gene amplification has been described in several drug-resistant parasitic protozoa. The first P-glycoprotein related gene described in Leishmania was ltpgpA, a gene frequently amplified in arsenite resistant ization experiments indicated that ltpgpA was part of a gene family. In addition to ltpgpA, four novel genes were cloned that are present in two loci Cited by:   P-glycoproteins, encoded by families of evolutionarily conserved genes, can confer a multidrug-resistant phenotype to mammalian tumor cells. To obtain more information on their functions in normal cells we have cloned genomic and complementary DNA sequences of four P-glycoprotein gene homologs of the genetically well-characterized nematode Caenorhabditis elegans, termed pgp Cited by: Analysis of multidrug resistant cell lines has led to the identification of the P-glycoprotein multigene family. Two of the three classes of mammalian P-glycoproteins have the ability to confer cellular resistance to a broad range of structurally and functionally diverse cytotoxic agents.

  Gene duplications have a major role in the evolution of new biological functions. Theoretical studies often assume that a duplication per se is selectively neutral and that, following a duplication, one of the gene copies is freed from purifying (stabilizing) selection, which creates the potential for evolution of a new function. In search of systematic evidence of accelerated evolution .   P-glycoprotein is a member of the large ATP binding cassette (ABC) superfamily of membrane transporters. This review focuses on the use of structure–function analyses to elucidate further the mechanism of action of mammalian P-glycoproteins. Analysis of multidrug resistant cell lines has led to the identification of the P-glycoprotein multigene family. Two of the three classes of mammalian P-glycoproteins have the ability to confer cellular resistance to a broad range of structurally and functionally diverse cytotoxic agents. P-glycoproteins are integral membrane glycoproteins comprised of two similar halves, each consisting of. Abstract. Analysis of multidrug resistant cell lines has led to the identification of the P-glycoprotein multigene family. Two of the three classes of mammalian P-glycoproteins have the ability to confer cellular resistance to a broad range of structurally and functionally diverse cytotoxic agents.

  MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine. C Schinkel, A.H., et al., & Borst, P. (). Disruption of the mouse mdrl a P-glycoprotein gene leads to a deficiency in the blood-brain barrier and to increased sensitivity to drugs. The Arabidopsis ABC gene family alone contains members, including 54 full-size transporters (consisting of two hydrophobic and two hydrophilic domains; Sanchez-Fernandez et al., ;Martinoia et al., ) and, therefore, it is still too early to draw a general picture of their roles. It might turn out that the diversity of their roles. Differential overexpression of three mdr gene family members in multidrug-resistant J mouse cells. J Biol Chem ; – J Biol Chem ; – PubMed Google Scholar. Generally, members of the fungal GH18 gene family may be viewed as isozymes with chitinase activity (Seidl, ), although there is one example where a completely new enzymatic function has evolved (endo-N-acetylglucosaminidase, ENGase Stals et al., ) and possibly some cases where the chitinolytic activity is lost.