P-glycoprotein structure and evolutionary homologies
Identifieur interne : 002D80 ( Main/Exploration ); précédent : 002D79; suivant : 002D81P-glycoprotein structure and evolutionary homologies
Auteurs : James M. Croop [États-Unis]Source :
- Cytotechnology [ 0920-9069 ] ; 1993-02-01.
English descriptors
- KwdEn :
- Teeft :
- Acad, Acid, Amino, Amino acid homology, Amino acid identity, Amino acid sequence, Amino acid sequences, Amino acid similarity, Amino acids, Amino terminus, Amplification, Antibiotic, Arceci, Baas, Bacterial permeases, Bamhi fragment, Biochem, Biochem para, Biochim biophys acta, Biol, Biol chem, Biophys, Bliek, Borst, Carboxy, Carboxy half, Carboxy halves, Cdna, Cdnas encoding, Cell biol, Cell lines, Cellular resistance, Cerevisiae, Cftr, Chem, Chloroquine, Chloroquine resistance, Chromosomal, Chromosome, Clone, Colchicine, Coli, Consensus sequence, Consensus sequences, Corresponding region, Croop, Cystic, Cystic fibrosis, Cytoplasmic, Cytoplasmic domain, Cytoplasmic domains, Cytoplasmic region, Cytoplasmic side, Cytotoxic, Cytotoxic agents, Different classes, Distal half, Distal halves, Divergence, Domain, Doxorubicin, Drosophila, Drug resistance, Drug transport, Elegans, Embo, Encode, Encodes, Encoding, Endicott, Entire polypeptide, Escherichia coli, Evolutionary origins, Exon, Extracellular, Falciparum, Family members, Foote, Functional units, Gene, Gene amplification, Gene duplication, Gene family, Genetic databases, Genomic, Genomic clones, Glycosylation, Gottesman, Gros, Hamster, Heavy metals, High level, High levels, Highest level, Highest levels, Histolytica, Homolog, Homologs, Homology, Human cell lines, Human mdrl, Hybridization, Hydrophilic, Hydrophilic domain, Hydrophobic, Hydrophobic domains, Hydrophobicity, Hydrophobicity analysis, Intron, Kinase, Large cytoplasmic domain, Large superfamily, Leishmania, Lemdrl, Lincke, Ling, Ltpgpa, Mammalian, Mammalian class, Mammalian gene, Mammalian homologs, Mammalian multidrug, Mammalian pglycoproteins, Mdr2, Mdr3, Mdrl, Mdrl gene, Mefloquine, Mefloquine resistance, Membrane, Molecular analysis, Molecular probes, Molecular weight, Monoclonal antibody, Mrna, Mrna species, Multicomponent, Multicomponent transport systems, Multidrug, Multidrug resistance, Multigene, Multigene family, Multiple cytotoxic agents, Murine, Natl, Natl cancer inst, Normal tissues, Nucleic, Nucleic acid sequences, Nucleotide, Nucleotide binding, Nucleotide binding domain, Nucleotide binding domains, Nucleotide binding folds, Open reading frame, Operon, Other homologs, Overexpressed, Overexpression, Parasite, Pastan, Peptide, Peptide transporters, Periplasmic, Permeases, Personal communication, Pfmdrl, Pglycoprotein, Pglycoprotein homologs, Pglycoproteins, Phenotype, Plasma membrane, Plasmodium, Plasmodium falciparum, Plotsimilarity analysis, Polymerase, Polymerase chain reaction products, Polypeptide, Polysaccharide, Pombe, Potential transmembrane domains, Preliminary observations, Primary structure, Proc, Proc natl acad, Protein expression, Protein kinase, Proximal, Proximal half, Putative transmembrane domains, Resistant, Resistant line, Resistant phenotype, Roninson, Secretory, Similar halves, Similar structure, Ste6, Superfamily, Toxin, Traffic atpases, Transmembrane, Transmembrane domain, Transmembrane domains, Transmembrane loops, Transport protein, Transport proteins, Transport substrates, Transport systems, Transporter, Ueda, Uwgcg pileup program, Vinblastine, Wide range.
Abstract
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. P-glycoproteins are integral membrane glycoproteins comprised of two similar halves, each consisting of six membrane spanning domains followed by a cytoplasmic domain which includes a nucleotide binding fold. The P-glycoprotein is a member of a large superfamily of transport proteins which utilize ATP to translocate a wide range of substrates across biological membranes. This superfamily includes transport complexes comprised of multicomponent systems, half P-glycoproteins and P-glycoprotein-like homologs which appear to require 12 α-helical transmembrane domains and two nucleotide binding folds for substrate transport. P-glycoprotein homologs have been isolated and characterized from a wide range of species. Amino acid sequences, the similarities between the halves and intron/exon boundaries have been compared to understand the evolutionary origins of the P-glycoprotein.
Url:
DOI: 10.1007/BF00744656
Affiliations:
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Le document en format XML
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<term>multidrug resistance</term>
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<term>Acid</term>
<term>Amino</term>
<term>Amino acid homology</term>
<term>Amino acid identity</term>
<term>Amino acid sequence</term>
<term>Amino acid sequences</term>
<term>Amino acid similarity</term>
<term>Amino acids</term>
<term>Amino terminus</term>
<term>Amplification</term>
<term>Antibiotic</term>
<term>Arceci</term>
<term>Baas</term>
<term>Bacterial permeases</term>
<term>Bamhi fragment</term>
<term>Biochem</term>
<term>Biochem para</term>
<term>Biochim biophys acta</term>
<term>Biol</term>
<term>Biol chem</term>
<term>Biophys</term>
<term>Bliek</term>
<term>Borst</term>
<term>Carboxy</term>
<term>Carboxy half</term>
<term>Carboxy halves</term>
<term>Cdna</term>
<term>Cdnas encoding</term>
<term>Cell biol</term>
<term>Cell lines</term>
<term>Cellular resistance</term>
<term>Cerevisiae</term>
<term>Cftr</term>
<term>Chem</term>
<term>Chloroquine</term>
<term>Chloroquine resistance</term>
<term>Chromosomal</term>
<term>Chromosome</term>
<term>Clone</term>
<term>Colchicine</term>
<term>Coli</term>
<term>Consensus sequence</term>
<term>Consensus sequences</term>
<term>Corresponding region</term>
<term>Croop</term>
<term>Cystic</term>
<term>Cystic fibrosis</term>
<term>Cytoplasmic</term>
<term>Cytoplasmic domain</term>
<term>Cytoplasmic domains</term>
<term>Cytoplasmic region</term>
<term>Cytoplasmic side</term>
<term>Cytotoxic</term>
<term>Cytotoxic agents</term>
<term>Different classes</term>
<term>Distal half</term>
<term>Distal halves</term>
<term>Divergence</term>
<term>Domain</term>
<term>Doxorubicin</term>
<term>Drosophila</term>
<term>Drug resistance</term>
<term>Drug transport</term>
<term>Elegans</term>
<term>Embo</term>
<term>Encode</term>
<term>Encodes</term>
<term>Encoding</term>
<term>Endicott</term>
<term>Entire polypeptide</term>
<term>Escherichia coli</term>
<term>Evolutionary origins</term>
<term>Exon</term>
<term>Extracellular</term>
<term>Falciparum</term>
<term>Family members</term>
<term>Foote</term>
<term>Functional units</term>
<term>Gene</term>
<term>Gene amplification</term>
<term>Gene duplication</term>
<term>Gene family</term>
<term>Genetic databases</term>
<term>Genomic</term>
<term>Genomic clones</term>
<term>Glycosylation</term>
<term>Gottesman</term>
<term>Gros</term>
<term>Hamster</term>
<term>Heavy metals</term>
<term>High level</term>
<term>High levels</term>
<term>Highest level</term>
<term>Highest levels</term>
<term>Histolytica</term>
<term>Homolog</term>
<term>Homologs</term>
<term>Homology</term>
<term>Human cell lines</term>
<term>Human mdrl</term>
<term>Hybridization</term>
<term>Hydrophilic</term>
<term>Hydrophilic domain</term>
<term>Hydrophobic</term>
<term>Hydrophobic domains</term>
<term>Hydrophobicity</term>
<term>Hydrophobicity analysis</term>
<term>Intron</term>
<term>Kinase</term>
<term>Large cytoplasmic domain</term>
<term>Large superfamily</term>
<term>Leishmania</term>
<term>Lemdrl</term>
<term>Lincke</term>
<term>Ling</term>
<term>Ltpgpa</term>
<term>Mammalian</term>
<term>Mammalian class</term>
<term>Mammalian gene</term>
<term>Mammalian homologs</term>
<term>Mammalian multidrug</term>
<term>Mammalian pglycoproteins</term>
<term>Mdr2</term>
<term>Mdr3</term>
<term>Mdrl</term>
<term>Mdrl gene</term>
<term>Mefloquine</term>
<term>Mefloquine resistance</term>
<term>Membrane</term>
<term>Molecular analysis</term>
<term>Molecular probes</term>
<term>Molecular weight</term>
<term>Monoclonal antibody</term>
<term>Mrna</term>
<term>Mrna species</term>
<term>Multicomponent</term>
<term>Multicomponent transport systems</term>
<term>Multidrug</term>
<term>Multidrug resistance</term>
<term>Multigene</term>
<term>Multigene family</term>
<term>Multiple cytotoxic agents</term>
<term>Murine</term>
<term>Natl</term>
<term>Natl cancer inst</term>
<term>Normal tissues</term>
<term>Nucleic</term>
<term>Nucleic acid sequences</term>
<term>Nucleotide</term>
<term>Nucleotide binding</term>
<term>Nucleotide binding domain</term>
<term>Nucleotide binding domains</term>
<term>Nucleotide binding folds</term>
<term>Open reading frame</term>
<term>Operon</term>
<term>Other homologs</term>
<term>Overexpressed</term>
<term>Overexpression</term>
<term>Parasite</term>
<term>Pastan</term>
<term>Peptide</term>
<term>Peptide transporters</term>
<term>Periplasmic</term>
<term>Permeases</term>
<term>Personal communication</term>
<term>Pfmdrl</term>
<term>Pglycoprotein</term>
<term>Pglycoprotein homologs</term>
<term>Pglycoproteins</term>
<term>Phenotype</term>
<term>Plasma membrane</term>
<term>Plasmodium</term>
<term>Plasmodium falciparum</term>
<term>Plotsimilarity analysis</term>
<term>Polymerase</term>
<term>Polymerase chain reaction products</term>
<term>Polypeptide</term>
<term>Polysaccharide</term>
<term>Pombe</term>
<term>Potential transmembrane domains</term>
<term>Preliminary observations</term>
<term>Primary structure</term>
<term>Proc</term>
<term>Proc natl acad</term>
<term>Protein expression</term>
<term>Protein kinase</term>
<term>Proximal</term>
<term>Proximal half</term>
<term>Putative transmembrane domains</term>
<term>Resistant</term>
<term>Resistant line</term>
<term>Resistant phenotype</term>
<term>Roninson</term>
<term>Secretory</term>
<term>Similar halves</term>
<term>Similar structure</term>
<term>Ste6</term>
<term>Superfamily</term>
<term>Toxin</term>
<term>Traffic atpases</term>
<term>Transmembrane</term>
<term>Transmembrane domain</term>
<term>Transmembrane domains</term>
<term>Transmembrane loops</term>
<term>Transport protein</term>
<term>Transport proteins</term>
<term>Transport substrates</term>
<term>Transport systems</term>
<term>Transporter</term>
<term>Ueda</term>
<term>Uwgcg pileup program</term>
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<term>Wide range</term>
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<front><div type="abstract" xml:lang="en">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. P-glycoproteins are integral membrane glycoproteins comprised of two similar halves, each consisting of six membrane spanning domains followed by a cytoplasmic domain which includes a nucleotide binding fold. The P-glycoprotein is a member of a large superfamily of transport proteins which utilize ATP to translocate a wide range of substrates across biological membranes. This superfamily includes transport complexes comprised of multicomponent systems, half P-glycoproteins and P-glycoprotein-like homologs which appear to require 12 α-helical transmembrane domains and two nucleotide binding folds for substrate transport. P-glycoprotein homologs have been isolated and characterized from a wide range of species. Amino acid sequences, the similarities between the halves and intron/exon boundaries have been compared to understand the evolutionary origins of the P-glycoprotein.</div>
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