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10.1124/pr.114.009464 http://scihub22266oqcxt.onion/10.1124/pr.114.009464 C4394688!4394688 !25713287     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25713287 &cmd=llinks): Failed to open stream: HTTP request failed! 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International Union of Basic and Clinical Pharmacology XCIII The parathyroid hormone receptors--family B G protein-coupled receptors |pdf=|usr=}}{{25713287 }} gab.com Text International Union of Basic and Clinical Pharmacology XCIII The parathyroid hormone receptors--family B G protein-coupled receptors JO: Pharmacol Rev http://www.kidney.de/pget.php?&tw=1&pmid=25713287 #FOAvip The type-1 parathyroid hormone receptor (PTHR1) is a family B G protein-coupled receptor (GPCR) that mediates the actions of two polypeptide ligands; parathyroid hormone (PTH), an endocrine hormone that regulates the levels of calcium and inorganic phosphate in the blood by acting on bone and kidney, and PTH-related protein (PTHrP), a paracrine-factor that regulates cell differentiation and proliferation programs in developing bone and other tissues. The type-2 parathyroid hormone receptor (PTHR2) binds a peptide ligand, called tuberoinfundibular peptide-39 (TIP39), and while the biologic role of the PTHR2/TIP39 system is not as defined as that of the PTHR1, it likely plays a role in the central nervous system as well as in spermatogenesis. Mechanisms of action at these receptors have been explored through a variety of pharmacological and biochemical approaches, and the data obtained support a basic "two-site" mode of ligand binding now thought to be used by each of the family B peptide hormone GPCRs. Recent crystallographic studies on the family B GPCRs are providing new insights that help to further refine the specifics of the overall receptor architecture and modes of ligand docking. One intriguing pharmacological finding for the PTHR1 is that it can form surprisingly stable complexes with certain PTH/PTHrP ligand analogs and thereby mediate markedly prolonged cell signaling responses that persist even when the bulk of the complexes are found in internalized vesicles. The PTHR1 thus appears to be able to activate the G?(s)/cAMP pathway not only from the plasma membrane but also from the endosomal domain. The cumulative findings could have an impact on efforts to develop new drug therapies for the PTH receptors. Twit Text FOAVip International Union of Basic and Clinical Pharmacology XCIII The parathyroid hormone receptors--family B G protein-coupled receptors ????Pharmacol Rev http://www.kidney.de/pget.php?&tw=1&pmid=25713287 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25713287 #FOAvip English Wikipedia <ref>{{Cite pmid|25713287 }}</ref> International Union of Basic and Clinical Pharmacology XCIII The parathyroid hormone receptors--family B G protein-coupled receptors #MMPMID25713287 Gardella TJ ; Vilardaga JP Pharmacol Rev 2015[]; 67 (2 ): 310-37 PMID25713287 show ga The type-1 parathyroid hormone receptor (PTHR1) is a family B G protein-coupled receptor (GPCR) that mediates the actions of two polypeptide ligands; parathyroid hormone (PTH), an endocrine hormone that regulates the levels of calcium and inorganic phosphate in the blood by acting on bone and kidney, and PTH-related protein (PTHrP), a paracrine-factor that regulates cell differentiation and proliferation programs in developing bone and other tissues. The type-2 parathyroid hormone receptor (PTHR2) binds a peptide ligand, called tuberoinfundibular peptide-39 (TIP39), and while the biologic role of the PTHR2/TIP39 system is not as defined as that of the PTHR1, it likely plays a role in the central nervous system as well as in spermatogenesis. Mechanisms of action at these receptors have been explored through a variety of pharmacological and biochemical approaches, and the data obtained support a basic "two-site" mode of ligand binding now thought to be used by each of the family B peptide hormone GPCRs. Recent crystallographic studies on the family B GPCRs are providing new insights that help to further refine the specifics of the overall receptor architecture and modes of ligand docking. One intriguing pharmacological finding for the PTHR1 is that it can form surprisingly stable complexes with certain PTH/PTHrP ligand analogs and thereby mediate markedly prolonged cell signaling responses that persist even when the bulk of the complexes are found in internalized vesicles. The PTHR1 thus appears to be able to activate the G?(s)/cAMP pathway not only from the plasma membrane but also from the endosomal domain. The cumulative findings could have an impact on efforts to develop new drug therapies for the PTH receptors. |*Models, Molecular [MESH] |*Second Messenger Systems [MESH] |Animals [MESH] |Cell Membrane/enzymology/metabolism [MESH] |Cyclic AMP/*physiology [MESH] |Endosomes/enzymology/metabolism [MESH] |GTP-Binding Protein alpha Subunits, Gs/chemistry/*metabolism [MESH] |Humans [MESH] |International Agencies [MESH] |Ligands [MESH] |Pharmacology, Clinical/trends [MESH] |Pharmacology/trends [MESH] |Protein Isoforms/agonists/chemistry/classification/metabolism [MESH] |Receptors, Parathyroid Hormone/agonists/chemistry/classification/*metabolism [MESH] |Societies, Scientific [MESH]International Union of Basic and Clinical Pharmacology XCIII The par(epmc).pdf DeepDyve Pubget Overpricing