Two G protein-coupled receptors activate Na +/H + exchanger isoform 1 in Chinese hamster lung fibroblasts through an ERK-dependent pathway
The sodium hydrogen exchanger isoform 1 (NHE1) is present in nearly all cells. Regulation of proton flux via the exchanger is a permissive step in cell growth and tumorgenesis and is vital in control of cell volume. The regulation of NHE1 by growth factors involves the Ras-extracellular signal regul...
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| description | The sodium hydrogen exchanger isoform 1 (NHE1) is present in nearly all cells. Regulation of proton flux via the exchanger is a permissive step in cell growth and tumorgenesis and is vital in control of cell volume. The regulation of NHE1 by growth factors involves the Ras-extracellular signal regulated kinase (ERK) pathway, however, the mechanism for G protein-coupled receptor (GPCR) activation of NHE1 is not well established. In this report, the relationship between GPCRs, ERK, and NHE1 in CCL39 cells is investigated. We give evidence that two agonists, the specific α
1-adrenergic agonist, phenylephrine and the water-soluble lipid mitogen, lysophosphatidic acid (LPA) activate NHE1 in CCL39 cells. Activation of ERK by phenylephrine and LPA occurs in a dose- and time-dependent manner. Optimal ERK activation was observed at 10 min and displayed a maximum stimulation at 100 μM phenylephrine and 10 μM LPA. α
1-Adrenergic stimulation also led to a rise in steady-state pH
i of 0.16±0.02 pH units, and incubation with LPA induced a 0.43±0.06 pH unit increase in pH
i. Phenylephrine-induced activation of NHE1 transport and ERK activity was inhibited by pretreating the cells with the MEK inhibitor PD98059. While only half of the LPA activatable exchange activity was abolished by PD98059 and U0126. To further demonstrate the specificity of the phenylephrine and LPA regulation of NHE1 and ERK, CCL39 cells were transfected with a kinase inactive MEK. The data indicate that ERK activation is essential for phenylephrine stimulation of NHE1, and that ERK and RhoA are involved in LPA stimulation of NHE1 by more than one mechanism. In addition, evidence of the convergence of these two pathways is shown by the loss of NHE1 activity when both pathways are inhibited and by the partial additivity of the two agonists on ERK and NHE1 activity. These studies indicate a direct involvement of ERK in the α
1-adrenergic activation of NHE1 and a significant role for both ERK and RhoA in LPA stimulation of NHE1 in CCL39 fibroblasts. |
| doi_str_mv | 10.1016/j.cellsig.2004.07.004 |
| format | Article |
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1-adrenergic agonist, phenylephrine and the water-soluble lipid mitogen, lysophosphatidic acid (LPA) activate NHE1 in CCL39 cells. Activation of ERK by phenylephrine and LPA occurs in a dose- and time-dependent manner. Optimal ERK activation was observed at 10 min and displayed a maximum stimulation at 100 μM phenylephrine and 10 μM LPA. α
1-Adrenergic stimulation also led to a rise in steady-state pH
i of 0.16±0.02 pH units, and incubation with LPA induced a 0.43±0.06 pH unit increase in pH
i. Phenylephrine-induced activation of NHE1 transport and ERK activity was inhibited by pretreating the cells with the MEK inhibitor PD98059. While only half of the LPA activatable exchange activity was abolished by PD98059 and U0126. To further demonstrate the specificity of the phenylephrine and LPA regulation of NHE1 and ERK, CCL39 cells were transfected with a kinase inactive MEK. The data indicate that ERK activation is essential for phenylephrine stimulation of NHE1, and that ERK and RhoA are involved in LPA stimulation of NHE1 by more than one mechanism. In addition, evidence of the convergence of these two pathways is shown by the loss of NHE1 activity when both pathways are inhibited and by the partial additivity of the two agonists on ERK and NHE1 activity. These studies indicate a direct involvement of ERK in the α
1-adrenergic activation of NHE1 and a significant role for both ERK and RhoA in LPA stimulation of NHE1 in CCL39 fibroblasts.</description><identifier>ISSN: 0898-6568</identifier><identifier>EISSN: 1873-3913</identifier><identifier>DOI: 10.1016/j.cellsig.2004.07.004</identifier><identifier>PMID: 15494214</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Alpha adrenergic receptor ; Amides - pharmacology ; Animals ; Butadienes - pharmacology ; Cricetinae ; Cricetulus ; Dose-Response Relationship, Drug ; Enzyme Inhibitors - pharmacology ; ERK ; Extracellular Signal-Regulated MAP Kinases - metabolism ; Fibroblasts - drug effects ; Fibroblasts - metabolism ; Fibroblasts - physiology ; Flavonoids - pharmacology ; Hydrogen-Ion Concentration - drug effects ; Intracellular Signaling Peptides and Proteins ; Lysophosphatidic acid ; Lysophospholipids - pharmacology ; MAP Kinase Kinase 1 - antagonists & inhibitors ; MAP Kinase Kinase 1 - genetics ; MAP Kinase Kinase 1 - metabolism ; Nitriles - pharmacology ; Phenylephrine ; Phenylephrine - pharmacology ; Phosphorylation - drug effects ; Protein Isoforms - metabolism ; Protein-Serine-Threonine Kinases - antagonists & inhibitors ; Protein-Serine-Threonine Kinases - physiology ; Pyridines - pharmacology ; Receptors, Adrenergic, alpha - physiology ; Receptors, G-Protein-Coupled - agonists ; Receptors, G-Protein-Coupled - physiology ; rho-Associated Kinases ; Signal Transduction - drug effects ; Signal Transduction - physiology ; Sodium hydrogen exchanger ; Sodium-Hydrogen Exchangers - metabolism ; Transfection</subject><ispartof>Cellular signalling, 2005-02, Vol.17 (2), p.231-242</ispartof><rights>2004 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c361t-1a30dcc5f679bb999a0488a59020db7cc4847b1462552a0728b30fab51e5f3ca3</citedby><cites>FETCH-LOGICAL-c361t-1a30dcc5f679bb999a0488a59020db7cc4847b1462552a0728b30fab51e5f3ca3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.cellsig.2004.07.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15494214$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wallert, M.A.</creatorcontrib><creatorcontrib>Thronson, H.L.</creatorcontrib><creatorcontrib>Korpi, N.L.</creatorcontrib><creatorcontrib>Olmschenk, S.M.</creatorcontrib><creatorcontrib>McCoy, A.C.</creatorcontrib><creatorcontrib>Funfar, M.R.</creatorcontrib><creatorcontrib>Provost, J.J.</creatorcontrib><title>Two G protein-coupled receptors activate Na +/H + exchanger isoform 1 in Chinese hamster lung fibroblasts through an ERK-dependent pathway</title><title>Cellular signalling</title><addtitle>Cell Signal</addtitle><description>The sodium hydrogen exchanger isoform 1 (NHE1) is present in nearly all cells. Regulation of proton flux via the exchanger is a permissive step in cell growth and tumorgenesis and is vital in control of cell volume. The regulation of NHE1 by growth factors involves the Ras-extracellular signal regulated kinase (ERK) pathway, however, the mechanism for G protein-coupled receptor (GPCR) activation of NHE1 is not well established. In this report, the relationship between GPCRs, ERK, and NHE1 in CCL39 cells is investigated. We give evidence that two agonists, the specific α
1-adrenergic agonist, phenylephrine and the water-soluble lipid mitogen, lysophosphatidic acid (LPA) activate NHE1 in CCL39 cells. Activation of ERK by phenylephrine and LPA occurs in a dose- and time-dependent manner. Optimal ERK activation was observed at 10 min and displayed a maximum stimulation at 100 μM phenylephrine and 10 μM LPA. α
1-Adrenergic stimulation also led to a rise in steady-state pH
i of 0.16±0.02 pH units, and incubation with LPA induced a 0.43±0.06 pH unit increase in pH
i. Phenylephrine-induced activation of NHE1 transport and ERK activity was inhibited by pretreating the cells with the MEK inhibitor PD98059. While only half of the LPA activatable exchange activity was abolished by PD98059 and U0126. To further demonstrate the specificity of the phenylephrine and LPA regulation of NHE1 and ERK, CCL39 cells were transfected with a kinase inactive MEK. The data indicate that ERK activation is essential for phenylephrine stimulation of NHE1, and that ERK and RhoA are involved in LPA stimulation of NHE1 by more than one mechanism. In addition, evidence of the convergence of these two pathways is shown by the loss of NHE1 activity when both pathways are inhibited and by the partial additivity of the two agonists on ERK and NHE1 activity. These studies indicate a direct involvement of ERK in the α
1-adrenergic activation of NHE1 and a significant role for both ERK and RhoA in LPA stimulation of NHE1 in CCL39 fibroblasts.</description><subject>Alpha adrenergic receptor</subject><subject>Amides - pharmacology</subject><subject>Animals</subject><subject>Butadienes - pharmacology</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Dose-Response Relationship, Drug</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>ERK</subject><subject>Extracellular Signal-Regulated MAP Kinases - metabolism</subject><subject>Fibroblasts - drug effects</subject><subject>Fibroblasts - metabolism</subject><subject>Fibroblasts - physiology</subject><subject>Flavonoids - pharmacology</subject><subject>Hydrogen-Ion Concentration - drug effects</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Lysophosphatidic acid</subject><subject>Lysophospholipids - pharmacology</subject><subject>MAP Kinase Kinase 1 - antagonists & inhibitors</subject><subject>MAP Kinase Kinase 1 - genetics</subject><subject>MAP Kinase Kinase 1 - metabolism</subject><subject>Nitriles - pharmacology</subject><subject>Phenylephrine</subject><subject>Phenylephrine - pharmacology</subject><subject>Phosphorylation - drug effects</subject><subject>Protein Isoforms - metabolism</subject><subject>Protein-Serine-Threonine Kinases - antagonists & inhibitors</subject><subject>Protein-Serine-Threonine Kinases - physiology</subject><subject>Pyridines - pharmacology</subject><subject>Receptors, Adrenergic, alpha - physiology</subject><subject>Receptors, G-Protein-Coupled - agonists</subject><subject>Receptors, G-Protein-Coupled - physiology</subject><subject>rho-Associated Kinases</subject><subject>Signal Transduction - drug effects</subject><subject>Signal Transduction - physiology</subject><subject>Sodium hydrogen exchanger</subject><subject>Sodium-Hydrogen Exchangers - metabolism</subject><subject>Transfection</subject><issn>0898-6568</issn><issn>1873-3913</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUc1u1DAYtBCILoVHAPnEpUpqO7GTnBBa9QdRgYTK2bKdLxuvEjvYTn9egafGq12pR05z-Ga-0cwg9JGSkhIqLvelgWmKdlcyQuqSNGWGV2hD26Yqqo5Wr9GGtF1bCC7aM_Quxj0hlBPB3qIzyuuuZrTeoL_3jx7f4CX4BNYVxq_LBD0OYGBJPkSsTLIPKgH-ofDF5S2-wPBkRuV2ELCNfvBhxhRbh7ejdRABj2qOKR-n1e3wYHXwelIxRZzG4NfdiJXDV7--Fz0s4HpwCS8qjY_q-T16M6gpwocTnqPf11f329vi7ufNt-3Xu8JUgqaCqor0xvBBNJ3WXdcpUret4h1hpNeNMXVbN5rWgnHOFGlYqysyKM0p8KEyqjpHn49_c-g_K8QkZxsPZSoHfo1SNIwz0fFM5EeiCT7GAINcgp1VeJaUyMMIci9PI8jDCJI0MkPWfToZrHqG_kV1aj0TvhwJkGM-WAgyGgvOQG9z8Un23v7H4h8L9Jv0</recordid><startdate>20050201</startdate><enddate>20050201</enddate><creator>Wallert, M.A.</creator><creator>Thronson, H.L.</creator><creator>Korpi, N.L.</creator><creator>Olmschenk, S.M.</creator><creator>McCoy, A.C.</creator><creator>Funfar, M.R.</creator><creator>Provost, J.J.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20050201</creationdate><title>Two G protein-coupled receptors activate Na +/H + exchanger isoform 1 in Chinese hamster lung fibroblasts through an ERK-dependent pathway</title><author>Wallert, M.A. ; Thronson, H.L. ; Korpi, N.L. ; Olmschenk, S.M. ; McCoy, A.C. ; Funfar, M.R. ; Provost, J.J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c361t-1a30dcc5f679bb999a0488a59020db7cc4847b1462552a0728b30fab51e5f3ca3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Alpha adrenergic receptor</topic><topic>Amides - pharmacology</topic><topic>Animals</topic><topic>Butadienes - pharmacology</topic><topic>Cricetinae</topic><topic>Cricetulus</topic><topic>Dose-Response Relationship, Drug</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>ERK</topic><topic>Extracellular Signal-Regulated MAP Kinases - metabolism</topic><topic>Fibroblasts - drug effects</topic><topic>Fibroblasts - metabolism</topic><topic>Fibroblasts - physiology</topic><topic>Flavonoids - pharmacology</topic><topic>Hydrogen-Ion Concentration - drug effects</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Lysophosphatidic acid</topic><topic>Lysophospholipids - pharmacology</topic><topic>MAP Kinase Kinase 1 - antagonists & inhibitors</topic><topic>MAP Kinase Kinase 1 - genetics</topic><topic>MAP Kinase Kinase 1 - metabolism</topic><topic>Nitriles - pharmacology</topic><topic>Phenylephrine</topic><topic>Phenylephrine - pharmacology</topic><topic>Phosphorylation - drug effects</topic><topic>Protein Isoforms - metabolism</topic><topic>Protein-Serine-Threonine Kinases - antagonists & inhibitors</topic><topic>Protein-Serine-Threonine Kinases - physiology</topic><topic>Pyridines - pharmacology</topic><topic>Receptors, Adrenergic, alpha - physiology</topic><topic>Receptors, G-Protein-Coupled - agonists</topic><topic>Receptors, G-Protein-Coupled - physiology</topic><topic>rho-Associated Kinases</topic><topic>Signal Transduction - drug effects</topic><topic>Signal Transduction - physiology</topic><topic>Sodium hydrogen exchanger</topic><topic>Sodium-Hydrogen Exchangers - metabolism</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wallert, M.A.</creatorcontrib><creatorcontrib>Thronson, H.L.</creatorcontrib><creatorcontrib>Korpi, N.L.</creatorcontrib><creatorcontrib>Olmschenk, S.M.</creatorcontrib><creatorcontrib>McCoy, A.C.</creatorcontrib><creatorcontrib>Funfar, M.R.</creatorcontrib><creatorcontrib>Provost, J.J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Cellular signalling</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wallert, M.A.</au><au>Thronson, H.L.</au><au>Korpi, N.L.</au><au>Olmschenk, S.M.</au><au>McCoy, A.C.</au><au>Funfar, M.R.</au><au>Provost, J.J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two G protein-coupled receptors activate Na +/H + exchanger isoform 1 in Chinese hamster lung fibroblasts through an ERK-dependent pathway</atitle><jtitle>Cellular signalling</jtitle><addtitle>Cell Signal</addtitle><date>2005-02-01</date><risdate>2005</risdate><volume>17</volume><issue>2</issue><spage>231</spage><epage>242</epage><pages>231-242</pages><issn>0898-6568</issn><eissn>1873-3913</eissn><abstract>The sodium hydrogen exchanger isoform 1 (NHE1) is present in nearly all cells. Regulation of proton flux via the exchanger is a permissive step in cell growth and tumorgenesis and is vital in control of cell volume. The regulation of NHE1 by growth factors involves the Ras-extracellular signal regulated kinase (ERK) pathway, however, the mechanism for G protein-coupled receptor (GPCR) activation of NHE1 is not well established. In this report, the relationship between GPCRs, ERK, and NHE1 in CCL39 cells is investigated. We give evidence that two agonists, the specific α
1-adrenergic agonist, phenylephrine and the water-soluble lipid mitogen, lysophosphatidic acid (LPA) activate NHE1 in CCL39 cells. Activation of ERK by phenylephrine and LPA occurs in a dose- and time-dependent manner. Optimal ERK activation was observed at 10 min and displayed a maximum stimulation at 100 μM phenylephrine and 10 μM LPA. α
1-Adrenergic stimulation also led to a rise in steady-state pH
i of 0.16±0.02 pH units, and incubation with LPA induced a 0.43±0.06 pH unit increase in pH
i. Phenylephrine-induced activation of NHE1 transport and ERK activity was inhibited by pretreating the cells with the MEK inhibitor PD98059. While only half of the LPA activatable exchange activity was abolished by PD98059 and U0126. To further demonstrate the specificity of the phenylephrine and LPA regulation of NHE1 and ERK, CCL39 cells were transfected with a kinase inactive MEK. The data indicate that ERK activation is essential for phenylephrine stimulation of NHE1, and that ERK and RhoA are involved in LPA stimulation of NHE1 by more than one mechanism. In addition, evidence of the convergence of these two pathways is shown by the loss of NHE1 activity when both pathways are inhibited and by the partial additivity of the two agonists on ERK and NHE1 activity. These studies indicate a direct involvement of ERK in the α
1-adrenergic activation of NHE1 and a significant role for both ERK and RhoA in LPA stimulation of NHE1 in CCL39 fibroblasts.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>15494214</pmid><doi>10.1016/j.cellsig.2004.07.004</doi><tpages>12</tpages></addata></record> |
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| subjects | Alpha adrenergic receptor Amides - pharmacology Animals Butadienes - pharmacology Cricetinae Cricetulus Dose-Response Relationship, Drug Enzyme Inhibitors - pharmacology ERK Extracellular Signal-Regulated MAP Kinases - metabolism Fibroblasts - drug effects Fibroblasts - metabolism Fibroblasts - physiology Flavonoids - pharmacology Hydrogen-Ion Concentration - drug effects Intracellular Signaling Peptides and Proteins Lysophosphatidic acid Lysophospholipids - pharmacology MAP Kinase Kinase 1 - antagonists & inhibitors MAP Kinase Kinase 1 - genetics MAP Kinase Kinase 1 - metabolism Nitriles - pharmacology Phenylephrine Phenylephrine - pharmacology Phosphorylation - drug effects Protein Isoforms - metabolism Protein-Serine-Threonine Kinases - antagonists & inhibitors Protein-Serine-Threonine Kinases - physiology Pyridines - pharmacology Receptors, Adrenergic, alpha - physiology Receptors, G-Protein-Coupled - agonists Receptors, G-Protein-Coupled - physiology rho-Associated Kinases Signal Transduction - drug effects Signal Transduction - physiology Sodium hydrogen exchanger Sodium-Hydrogen Exchangers - metabolism Transfection |
| title | Two G protein-coupled receptors activate Na +/H + exchanger isoform 1 in Chinese hamster lung fibroblasts through an ERK-dependent pathway |
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