PROSTANOID RECEPTORS: Subtypes and Signaling 1
Abstract Cyclooxygenases metabolize arachidonate to five primary prostanoids: PGE2, PGF2alpha, PGI2, TxA2, and PGD2. These autacrine lipid mediators interact with specific members of a family of distinct G-protein-coupled prostanoid receptors, designated EP, FP, IP, TP, and DP, respectively. Each of...
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E-Artikel |
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| Erschienen: |
2001 |
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| Umfang: |
30 |
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| Reproduktion: |
Annual Reviews Electronic Back Volume Collection 1932-2005ff |
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| Übergeordnetes Werk: |
in: Annual review of pharmacology and toxicology - Palo Alto, Calif., 1961, 41(2001), Seite 661-690 |
| Übergeordnetes Werk: |
volume:41 ; year:2001 ; pages:661-690 ; extent:30 |
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NLEJ164178414 |
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| 520 | |a Abstract Cyclooxygenases metabolize arachidonate to five primary prostanoids: PGE2, PGF2alpha, PGI2, TxA2, and PGD2. These autacrine lipid mediators interact with specific members of a family of distinct G-protein-coupled prostanoid receptors, designated EP, FP, IP, TP, and DP, respectively. Each of these receptors has been cloned, expressed, and characterized. This family of eight prostanoid receptor complementary DNAs encodes seven transmembrane proteins which are typical of G-protein-coupled receptors and these receptors are distinguished by their ligand-binding profiles and the signal transduction pathways activated on ligand binding. Ligand-binding selectivity of these receptors is determined by both the transmembrane sequences and amino acid residues in the putative extracellular-loop regions. The selectivity of interaction between the receptors and G proteins appears to be mediated at least in part by the C-terminal tail region. Each of the EP1, EP3, FP, and TP receptors has alternative splice variants described that alter the coding sequence in the C-terminal intracellular tail region. The C-terminal variants modulate signal transduction, phosphorylation, and desensitization of these receptors, as well as altering agonist-independent constitutive activity. | ||
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(DE-627)NLEJ164178414 DE-627 ger DE-627 rakwb PROSTANOID RECEPTORS: Subtypes and Signaling 1 2001 30 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Cyclooxygenases metabolize arachidonate to five primary prostanoids: PGE2, PGF2alpha, PGI2, TxA2, and PGD2. These autacrine lipid mediators interact with specific members of a family of distinct G-protein-coupled prostanoid receptors, designated EP, FP, IP, TP, and DP, respectively. Each of these receptors has been cloned, expressed, and characterized. This family of eight prostanoid receptor complementary DNAs encodes seven transmembrane proteins which are typical of G-protein-coupled receptors and these receptors are distinguished by their ligand-binding profiles and the signal transduction pathways activated on ligand binding. Ligand-binding selectivity of these receptors is determined by both the transmembrane sequences and amino acid residues in the putative extracellular-loop regions. The selectivity of interaction between the receptors and G proteins appears to be mediated at least in part by the C-terminal tail region. Each of the EP1, EP3, FP, and TP receptors has alternative splice variants described that alter the coding sequence in the C-terminal intracellular tail region. The C-terminal variants modulate signal transduction, phosphorylation, and desensitization of these receptors, as well as altering agonist-independent constitutive activity. Annual Reviews Electronic Back Volume Collection 1932-2005ff Breyer, Richard M oth Bagdassarian, Carey K oth Myers, Scott A oth Breyer, Matthew D oth in Annual review of pharmacology and toxicology Palo Alto, Calif., 1961 41(2001), Seite 661-690 Online-Ressource (DE-627)NLEJ164018646 (DE-600)1474461-2 0362-1642 nnns volume:41 year:2001 pages:661-690 extent:30 http://dx.doi.org/10.1146/annurev.pharmtox.41.1.661 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 41 2001 661-690 30 |
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(DE-627)NLEJ164178414 DE-627 ger DE-627 rakwb PROSTANOID RECEPTORS: Subtypes and Signaling 1 2001 30 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Cyclooxygenases metabolize arachidonate to five primary prostanoids: PGE2, PGF2alpha, PGI2, TxA2, and PGD2. These autacrine lipid mediators interact with specific members of a family of distinct G-protein-coupled prostanoid receptors, designated EP, FP, IP, TP, and DP, respectively. Each of these receptors has been cloned, expressed, and characterized. This family of eight prostanoid receptor complementary DNAs encodes seven transmembrane proteins which are typical of G-protein-coupled receptors and these receptors are distinguished by their ligand-binding profiles and the signal transduction pathways activated on ligand binding. Ligand-binding selectivity of these receptors is determined by both the transmembrane sequences and amino acid residues in the putative extracellular-loop regions. The selectivity of interaction between the receptors and G proteins appears to be mediated at least in part by the C-terminal tail region. Each of the EP1, EP3, FP, and TP receptors has alternative splice variants described that alter the coding sequence in the C-terminal intracellular tail region. The C-terminal variants modulate signal transduction, phosphorylation, and desensitization of these receptors, as well as altering agonist-independent constitutive activity. Annual Reviews Electronic Back Volume Collection 1932-2005ff Breyer, Richard M oth Bagdassarian, Carey K oth Myers, Scott A oth Breyer, Matthew D oth in Annual review of pharmacology and toxicology Palo Alto, Calif., 1961 41(2001), Seite 661-690 Online-Ressource (DE-627)NLEJ164018646 (DE-600)1474461-2 0362-1642 nnns volume:41 year:2001 pages:661-690 extent:30 http://dx.doi.org/10.1146/annurev.pharmtox.41.1.661 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 41 2001 661-690 30 |
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(DE-627)NLEJ164178414 DE-627 ger DE-627 rakwb PROSTANOID RECEPTORS: Subtypes and Signaling 1 2001 30 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Cyclooxygenases metabolize arachidonate to five primary prostanoids: PGE2, PGF2alpha, PGI2, TxA2, and PGD2. These autacrine lipid mediators interact with specific members of a family of distinct G-protein-coupled prostanoid receptors, designated EP, FP, IP, TP, and DP, respectively. Each of these receptors has been cloned, expressed, and characterized. This family of eight prostanoid receptor complementary DNAs encodes seven transmembrane proteins which are typical of G-protein-coupled receptors and these receptors are distinguished by their ligand-binding profiles and the signal transduction pathways activated on ligand binding. Ligand-binding selectivity of these receptors is determined by both the transmembrane sequences and amino acid residues in the putative extracellular-loop regions. The selectivity of interaction between the receptors and G proteins appears to be mediated at least in part by the C-terminal tail region. Each of the EP1, EP3, FP, and TP receptors has alternative splice variants described that alter the coding sequence in the C-terminal intracellular tail region. The C-terminal variants modulate signal transduction, phosphorylation, and desensitization of these receptors, as well as altering agonist-independent constitutive activity. Annual Reviews Electronic Back Volume Collection 1932-2005ff Breyer, Richard M oth Bagdassarian, Carey K oth Myers, Scott A oth Breyer, Matthew D oth in Annual review of pharmacology and toxicology Palo Alto, Calif., 1961 41(2001), Seite 661-690 Online-Ressource (DE-627)NLEJ164018646 (DE-600)1474461-2 0362-1642 nnns volume:41 year:2001 pages:661-690 extent:30 http://dx.doi.org/10.1146/annurev.pharmtox.41.1.661 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 41 2001 661-690 30 |
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(DE-627)NLEJ164178414 DE-627 ger DE-627 rakwb PROSTANOID RECEPTORS: Subtypes and Signaling 1 2001 30 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Cyclooxygenases metabolize arachidonate to five primary prostanoids: PGE2, PGF2alpha, PGI2, TxA2, and PGD2. These autacrine lipid mediators interact with specific members of a family of distinct G-protein-coupled prostanoid receptors, designated EP, FP, IP, TP, and DP, respectively. Each of these receptors has been cloned, expressed, and characterized. This family of eight prostanoid receptor complementary DNAs encodes seven transmembrane proteins which are typical of G-protein-coupled receptors and these receptors are distinguished by their ligand-binding profiles and the signal transduction pathways activated on ligand binding. Ligand-binding selectivity of these receptors is determined by both the transmembrane sequences and amino acid residues in the putative extracellular-loop regions. The selectivity of interaction between the receptors and G proteins appears to be mediated at least in part by the C-terminal tail region. Each of the EP1, EP3, FP, and TP receptors has alternative splice variants described that alter the coding sequence in the C-terminal intracellular tail region. The C-terminal variants modulate signal transduction, phosphorylation, and desensitization of these receptors, as well as altering agonist-independent constitutive activity. Annual Reviews Electronic Back Volume Collection 1932-2005ff Breyer, Richard M oth Bagdassarian, Carey K oth Myers, Scott A oth Breyer, Matthew D oth in Annual review of pharmacology and toxicology Palo Alto, Calif., 1961 41(2001), Seite 661-690 Online-Ressource (DE-627)NLEJ164018646 (DE-600)1474461-2 0362-1642 nnns volume:41 year:2001 pages:661-690 extent:30 http://dx.doi.org/10.1146/annurev.pharmtox.41.1.661 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 41 2001 661-690 30 |
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(DE-627)NLEJ164178414 DE-627 ger DE-627 rakwb PROSTANOID RECEPTORS: Subtypes and Signaling 1 2001 30 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Cyclooxygenases metabolize arachidonate to five primary prostanoids: PGE2, PGF2alpha, PGI2, TxA2, and PGD2. These autacrine lipid mediators interact with specific members of a family of distinct G-protein-coupled prostanoid receptors, designated EP, FP, IP, TP, and DP, respectively. Each of these receptors has been cloned, expressed, and characterized. This family of eight prostanoid receptor complementary DNAs encodes seven transmembrane proteins which are typical of G-protein-coupled receptors and these receptors are distinguished by their ligand-binding profiles and the signal transduction pathways activated on ligand binding. Ligand-binding selectivity of these receptors is determined by both the transmembrane sequences and amino acid residues in the putative extracellular-loop regions. The selectivity of interaction between the receptors and G proteins appears to be mediated at least in part by the C-terminal tail region. Each of the EP1, EP3, FP, and TP receptors has alternative splice variants described that alter the coding sequence in the C-terminal intracellular tail region. The C-terminal variants modulate signal transduction, phosphorylation, and desensitization of these receptors, as well as altering agonist-independent constitutive activity. Annual Reviews Electronic Back Volume Collection 1932-2005ff Breyer, Richard M oth Bagdassarian, Carey K oth Myers, Scott A oth Breyer, Matthew D oth in Annual review of pharmacology and toxicology Palo Alto, Calif., 1961 41(2001), Seite 661-690 Online-Ressource (DE-627)NLEJ164018646 (DE-600)1474461-2 0362-1642 nnns volume:41 year:2001 pages:661-690 extent:30 http://dx.doi.org/10.1146/annurev.pharmtox.41.1.661 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 41 2001 661-690 30 |
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Abstract Cyclooxygenases metabolize arachidonate to five primary prostanoids: PGE2, PGF2alpha, PGI2, TxA2, and PGD2. These autacrine lipid mediators interact with specific members of a family of distinct G-protein-coupled prostanoid receptors, designated EP, FP, IP, TP, and DP, respectively. Each of these receptors has been cloned, expressed, and characterized. This family of eight prostanoid receptor complementary DNAs encodes seven transmembrane proteins which are typical of G-protein-coupled receptors and these receptors are distinguished by their ligand-binding profiles and the signal transduction pathways activated on ligand binding. Ligand-binding selectivity of these receptors is determined by both the transmembrane sequences and amino acid residues in the putative extracellular-loop regions. The selectivity of interaction between the receptors and G proteins appears to be mediated at least in part by the C-terminal tail region. Each of the EP1, EP3, FP, and TP receptors has alternative splice variants described that alter the coding sequence in the C-terminal intracellular tail region. The C-terminal variants modulate signal transduction, phosphorylation, and desensitization of these receptors, as well as altering agonist-independent constitutive activity. |
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Abstract Cyclooxygenases metabolize arachidonate to five primary prostanoids: PGE2, PGF2alpha, PGI2, TxA2, and PGD2. These autacrine lipid mediators interact with specific members of a family of distinct G-protein-coupled prostanoid receptors, designated EP, FP, IP, TP, and DP, respectively. Each of these receptors has been cloned, expressed, and characterized. This family of eight prostanoid receptor complementary DNAs encodes seven transmembrane proteins which are typical of G-protein-coupled receptors and these receptors are distinguished by their ligand-binding profiles and the signal transduction pathways activated on ligand binding. Ligand-binding selectivity of these receptors is determined by both the transmembrane sequences and amino acid residues in the putative extracellular-loop regions. The selectivity of interaction between the receptors and G proteins appears to be mediated at least in part by the C-terminal tail region. Each of the EP1, EP3, FP, and TP receptors has alternative splice variants described that alter the coding sequence in the C-terminal intracellular tail region. The C-terminal variants modulate signal transduction, phosphorylation, and desensitization of these receptors, as well as altering agonist-independent constitutive activity. |
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Abstract Cyclooxygenases metabolize arachidonate to five primary prostanoids: PGE2, PGF2alpha, PGI2, TxA2, and PGD2. These autacrine lipid mediators interact with specific members of a family of distinct G-protein-coupled prostanoid receptors, designated EP, FP, IP, TP, and DP, respectively. Each of these receptors has been cloned, expressed, and characterized. This family of eight prostanoid receptor complementary DNAs encodes seven transmembrane proteins which are typical of G-protein-coupled receptors and these receptors are distinguished by their ligand-binding profiles and the signal transduction pathways activated on ligand binding. Ligand-binding selectivity of these receptors is determined by both the transmembrane sequences and amino acid residues in the putative extracellular-loop regions. The selectivity of interaction between the receptors and G proteins appears to be mediated at least in part by the C-terminal tail region. Each of the EP1, EP3, FP, and TP receptors has alternative splice variants described that alter the coding sequence in the C-terminal intracellular tail region. The C-terminal variants modulate signal transduction, phosphorylation, and desensitization of these receptors, as well as altering agonist-independent constitutive activity. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ164178414</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506101454.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070207s2001 xx |||||o 00| ||und c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ164178414</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">PROSTANOID RECEPTORS: Subtypes and Signaling 1</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2001</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">30</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Cyclooxygenases metabolize arachidonate to five primary prostanoids: PGE2, PGF2alpha, PGI2, TxA2, and PGD2. These autacrine lipid mediators interact with specific members of a family of distinct G-protein-coupled prostanoid receptors, designated EP, FP, IP, TP, and DP, respectively. Each of these receptors has been cloned, expressed, and characterized. This family of eight prostanoid receptor complementary DNAs encodes seven transmembrane proteins which are typical of G-protein-coupled receptors and these receptors are distinguished by their ligand-binding profiles and the signal transduction pathways activated on ligand binding. Ligand-binding selectivity of these receptors is determined by both the transmembrane sequences and amino acid residues in the putative extracellular-loop regions. The selectivity of interaction between the receptors and G proteins appears to be mediated at least in part by the C-terminal tail region. Each of the EP1, EP3, FP, and TP receptors has alternative splice variants described that alter the coding sequence in the C-terminal intracellular tail region. The C-terminal variants modulate signal transduction, phosphorylation, and desensitization of these receptors, as well as altering agonist-independent constitutive activity.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Annual Reviews Electronic Back Volume Collection 1932-2005ff</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Breyer, Richard M</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bagdassarian, Carey K</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Myers, Scott A</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Breyer, Matthew D</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Annual review of pharmacology and toxicology</subfield><subfield code="d">Palo Alto, Calif., 1961</subfield><subfield code="g">41(2001), Seite 661-690</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ164018646</subfield><subfield code="w">(DE-600)1474461-2</subfield><subfield code="x">0362-1642</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:41</subfield><subfield code="g">year:2001</subfield><subfield code="g">pages:661-690</subfield><subfield code="g">extent:30</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1146/annurev.pharmtox.41.1.661</subfield><subfield code="q">text/html</subfield><subfield code="z">Deutschlandweit zugänglich</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-ANR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">41</subfield><subfield code="j">2001</subfield><subfield code="h">661-690</subfield><subfield code="g">30</subfield></datafield></record></collection>
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