We are analyzing https://link.springer.com/article/10.1007/s11010-005-8050-5.

Title:
Agonist-induced phosphorylation and desensitization of the P2Y2 nucleotide receptor | Molecular and Cellular Biochemistry
Description:
Purification of HA-tagged P2Y2 receptors from transfected human 1321N1 astrocytoma cells yielded a protein with a molecular size determined by SDS-PAGE to be in the range of 57–76 kDa, which is typical of membrane glycoproteins with heterogeneous complex glycosylation. The protein phosphatase inhibitor, okadaic acid, attenuated the recovery of receptor activity from the agonist-induced desensitized state, suggesting a role for P2Y2 receptor phosphorylation in desensitization. Isolation of HA-tagged P2Y2 nucleotide receptors from metabolically [32P]-labelled cells indicated a (3.8 ± 0.2)-fold increase in the [32P]-content of the receptor after 15 min of treatment with 100 μM UTP, as compared to immunoprecipitated receptors from untreated control cells. Receptor sequestration studies indicated that ∼40% of the surface receptors were internalized after a 15-min stimulation with 100 μM UTP. Point mutation of three potential GRK and PKC phosphorylation sites in the third intracellular loop and C-terminal tail of the P2Y2 receptor (namely, S243A, T344A, and S356A) extinguished agonist-induced receptor phosphorylation, caused a marked reduction in the efficacy of UTP to desensitize P2Y2 receptor signalling to intracellular calcium mobilization, and impaired agonist-induced receptor internalization. Activation of PKC isoforms with phorbol 12-myristate 13-acetate that caused heterologous receptor desensitization did not increase the level of P2Y2 receptor phosphorylation. Our results indicate a role for receptor phosphorylation by phorbol-insensitive protein kinases in agonist-induced desensitization of the P2Y2 nucleotide receptor. (Mol Cell Biochem xxx: 35–45, 2005)
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Keywords {🔍}

receptor, google, scholar, cas, pubmed, article, receptors, desensitization, phosphorylation, protein, biol, chem, nucleotide, weisman, proteincoupled, usa, gonzalez, kinase, agonistinduced, human, cells, sci, erb, turner, garrad, kinases, content, expression, department, university, privacy, cookies, fernando, intracellular, internalization, extracellular, regulation, lefkowitz, signaling, publish, search, molecular, biochemistry, flores, aquino, role, grk, sites, mol, cell,

Topics {✒️}

month download article/chapter g-protein-coupled receptor kinases ha-tagged p2y2 receptors g-protein-coupled receptor regulation intracellular calcium mobilization parathyroid hormone-related protein g-protein-coupled receptor agonist-induced desensitized state protein-coupled receptor kinases cystic fibrosis pharmacotherapy protein-coupled p2 purinoceptors α 1b-adrenergic receptor suramin-derived compound library camp-dependent protein kinase santiago-perez li mitogen-activated protein kinases metabolically [32p]-labelled cells phospholipase c-β activity phorbol-insensitive protein kinases protein-coupled receptors edna aquino & fernando p2y2 receptor phosphorylation p2y2 nucleotide receptor human monocytic cells agonist-induced phosphorylation full article pdf p2 nucleotide receptors β2-adrenergic receptors edna aquino β 2-adrenergic receptor c-terminal tail privacy choices/manage cookies agonist-receptor-arrestin author correspondence agonist-induced desensitization al-ubaidi mr phorbol 12-myristate 13-acetate pkc phosphorylation sites extended protein kinase truncated at1a receptor rat neurotensin receptor cellular biochemistry aims nucleotide receptor signaling untreated control cells cho-k1 cells high agonist affinity protein phosphatase inhibitor elegans rgs protein hernandez-perez mg related subjects

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         headline:Agonist-induced phosphorylation and desensitization of the P2Y2 nucleotide receptor
         description:Purification of HA-tagged P2Y2 receptors from transfected human 1321N1 astrocytoma cells yielded a protein with a molecular size determined by SDS-PAGE to be in the range of 57–76 kDa, which is typical of membrane glycoproteins with heterogeneous complex glycosylation. The protein phosphatase inhibitor, okadaic acid, attenuated the recovery of receptor activity from the agonist-induced desensitized state, suggesting a role for P2Y2 receptor phosphorylation in desensitization. Isolation of HA-tagged P2Y2 nucleotide receptors from metabolically [32P]-labelled cells indicated a (3.8 ± 0.2)-fold increase in the [32P]-content of the receptor after 15 min of treatment with 100 μM UTP, as compared to immunoprecipitated receptors from untreated control cells. Receptor sequestration studies indicated that ∼40% of the surface receptors were internalized after a 15-min stimulation with 100 μM UTP. Point mutation of three potential GRK and PKC phosphorylation sites in the third intracellular loop and C-terminal tail of the P2Y2 receptor (namely, S243A, T344A, and S356A) extinguished agonist-induced receptor phosphorylation, caused a marked reduction in the efficacy of UTP to desensitize P2Y2 receptor signalling to intracellular calcium mobilization, and impaired agonist-induced receptor internalization. Activation of PKC isoforms with phorbol 12-myristate 13-acetate that caused heterologous receptor desensitization did not increase the level of P2Y2 receptor phosphorylation. Our results indicate a role for receptor phosphorylation by phorbol-insensitive protein kinases in agonist-induced desensitization of the P2Y2 nucleotide receptor. (Mol Cell Biochem xxx: 35–45, 2005)
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      description:Purification of HA-tagged P2Y2 receptors from transfected human 1321N1 astrocytoma cells yielded a protein with a molecular size determined by SDS-PAGE to be in the range of 57–76 kDa, which is typical of membrane glycoproteins with heterogeneous complex glycosylation. The protein phosphatase inhibitor, okadaic acid, attenuated the recovery of receptor activity from the agonist-induced desensitized state, suggesting a role for P2Y2 receptor phosphorylation in desensitization. Isolation of HA-tagged P2Y2 nucleotide receptors from metabolically [32P]-labelled cells indicated a (3.8 ± 0.2)-fold increase in the [32P]-content of the receptor after 15 min of treatment with 100 μM UTP, as compared to immunoprecipitated receptors from untreated control cells. Receptor sequestration studies indicated that ∼40% of the surface receptors were internalized after a 15-min stimulation with 100 μM UTP. Point mutation of three potential GRK and PKC phosphorylation sites in the third intracellular loop and C-terminal tail of the P2Y2 receptor (namely, S243A, T344A, and S356A) extinguished agonist-induced receptor phosphorylation, caused a marked reduction in the efficacy of UTP to desensitize P2Y2 receptor signalling to intracellular calcium mobilization, and impaired agonist-induced receptor internalization. Activation of PKC isoforms with phorbol 12-myristate 13-acetate that caused heterologous receptor desensitization did not increase the level of P2Y2 receptor phosphorylation. Our results indicate a role for receptor phosphorylation by phorbol-insensitive protein kinases in agonist-induced desensitization of the P2Y2 nucleotide receptor. (Mol Cell Biochem xxx: 35–45, 2005)
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         Medical Biochemistry
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