Shear stress-mediated extracellular signal-regulated kinase activation is regulated by sodium in endothelial cells. Potential role for a voltage-dependent sodium channel
Fluid shear stress is an important regulator of endothelial cell (EC) function. To determine whether mechanosensitive ion channels participate in the EC response to shear stress, we characterized the role of ion transport in shear stress-mediated extracellular signal-regulated kinase (ERK1/2) stimul...
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| Veröffentlicht in: | The Journal of biological chemistry 1999-07, Vol.274 (29), p.20144-20150 |
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| container_end_page | 20150 |
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| container_issue | 29 |
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| container_title | The Journal of biological chemistry |
| container_volume | 274 |
| creator | Traub, O Ishida, T Ishida, M Tupper, J C Berk, B C |
| description | Fluid shear stress is an important regulator of endothelial cell (EC) function. To determine whether mechanosensitive ion channels participate in the EC response to shear stress, we characterized the role of ion transport in shear stress-mediated extracellular signal-regulated kinase (ERK1/2) stimulation. Replacement of all extracellular Na+ with either N-methyl-D-glucamine or choline chloride increased the ERK1/2 stimulation in response to shear stress by 1.89 +/- 0.1-fold. The Na+ effect was concentration-dependent (maximal effect, |
| doi_str_mv | 10.1074/jbc.274.29.20144 |
| format | Article |
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Potential role for a voltage-dependent sodium channel</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Traub, O ; Ishida, T ; Ishida, M ; Tupper, J C ; Berk, B C</creator><creatorcontrib>Traub, O ; Ishida, T ; Ishida, M ; Tupper, J C ; Berk, B C</creatorcontrib><description>Fluid shear stress is an important regulator of endothelial cell (EC) function. To determine whether mechanosensitive ion channels participate in the EC response to shear stress, we characterized the role of ion transport in shear stress-mediated extracellular signal-regulated kinase (ERK1/2) stimulation. Replacement of all extracellular Na+ with either N-methyl-D-glucamine or choline chloride increased the ERK1/2 stimulation in response to shear stress by 1.89 +/- 0.1-fold. The Na+ effect was concentration-dependent (maximal effect, </=12.5 mM) and was specific for shear stress-mediated ERK1/2 activation as epidermal growth factor-stimulated ERK1/2 activation was unaffected by removal of extracellular Na+. Shear stress-mediated ERK1/2 activation was potentiated by the voltage-gated sodium channel antagonist, tetrodotoxin (100 nM), to a magnitude similar to that achieved with extracellular Na+ withdrawal. Transfection of Chinese hamster ovary cells with a rat brain type IIa voltage-gated sodium channel completely inhibited shear stress-mediated ERK1/2 activation in these cells. Inhibition was reversed by performing the experiment in sodium-free buffer or by including tetrodotoxin in the buffer. Western blotting of bovine and human EC lysates with SP19 antibody detected a 250-kDa protein consistent with the voltage-gated sodium channel. Degenerate polymerase chain reaction of cDNA from primary human EC yielded transcripts whose sequences were identical to the sodium channel SCN4a and SCN8a alpha subunit genes. 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Potential role for a voltage-dependent sodium channel</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Fluid shear stress is an important regulator of endothelial cell (EC) function. To determine whether mechanosensitive ion channels participate in the EC response to shear stress, we characterized the role of ion transport in shear stress-mediated extracellular signal-regulated kinase (ERK1/2) stimulation. Replacement of all extracellular Na+ with either N-methyl-D-glucamine or choline chloride increased the ERK1/2 stimulation in response to shear stress by 1.89 +/- 0.1-fold. The Na+ effect was concentration-dependent (maximal effect, </=12.5 mM) and was specific for shear stress-mediated ERK1/2 activation as epidermal growth factor-stimulated ERK1/2 activation was unaffected by removal of extracellular Na+. Shear stress-mediated ERK1/2 activation was potentiated by the voltage-gated sodium channel antagonist, tetrodotoxin (100 nM), to a magnitude similar to that achieved with extracellular Na+ withdrawal. Transfection of Chinese hamster ovary cells with a rat brain type IIa voltage-gated sodium channel completely inhibited shear stress-mediated ERK1/2 activation in these cells. Inhibition was reversed by performing the experiment in sodium-free buffer or by including tetrodotoxin in the buffer. Western blotting of bovine and human EC lysates with SP19 antibody detected a 250-kDa protein consistent with the voltage-gated sodium channel. Degenerate polymerase chain reaction of cDNA from primary human EC yielded transcripts whose sequences were identical to the sodium channel SCN4a and SCN8a alpha subunit genes. These results indicate that shear stress-mediated ERK1/2 activation is regulated by extracellular sodium and demonstrate that ion transport via Na+ channels modulates EC responses to shear stress.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Calcium Channels - metabolism</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>Carrier Proteins - antagonists & inhibitors</subject><subject>Cattle</subject><subject>Cells, Cultured</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>DNA</subject><subject>Endothelium, Vascular - enzymology</subject><subject>Endothelium, Vascular - metabolism</subject><subject>Enzyme Activation</subject><subject>Humans</subject><subject>Ion Channel Gating</subject><subject>Molecular Sequence Data</subject><subject>Potassium - metabolism</subject><subject>Rats</subject><subject>Sodium - metabolism</subject><subject>Sodium Channels - metabolism</subject><subject>Space life sciences</subject><issn>0021-9258</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkT1PJDEMhlOADti7ngqlopshyXwlJUJ8nIQEEnf1ypN4drNkkyXJIPhJ9y-Z0S2ixI1lP69fWTYhp5yVnHX1xabXpejqUqhSMF7XB-SYMcELJRp5RE5S2rApasV_kCPOasZaIY_Jv6c1QqQpR0yp2KKxkNFQfMsRNDo3upnalQdXRFxN5YyfrYeEFHS2r5Bt8NQm-oX7d5qCseOWWk_Rm5DX6Cw4Ojumkj6GjD7PjRgc0iFECvQ1uAwrLAzuppGJf3roNXiP7ic5HMAl_LXPC_L35vrP1V1x_3D7--ryvtiJSuYCW9UA9kPHuGyqpmWNEFq2Epp2YFoLrbVinRQGB6E0mNogVw3rsUPDsFLVgpz_993F8DJiysutTfPi4DGMadkqKaWo-bdC3omm7To2Cc_2wrGfLrzcRbuF-L78_EL1AdqsjMg</recordid><startdate>19990716</startdate><enddate>19990716</enddate><creator>Traub, O</creator><creator>Ishida, T</creator><creator>Ishida, M</creator><creator>Tupper, J C</creator><creator>Berk, B C</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>19990716</creationdate><title>Shear stress-mediated extracellular signal-regulated kinase activation is regulated by sodium in endothelial cells. 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Potential role for a voltage-dependent sodium channel</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1999-07-16</date><risdate>1999</risdate><volume>274</volume><issue>29</issue><spage>20144</spage><epage>20150</epage><pages>20144-20150</pages><issn>0021-9258</issn><abstract>Fluid shear stress is an important regulator of endothelial cell (EC) function. To determine whether mechanosensitive ion channels participate in the EC response to shear stress, we characterized the role of ion transport in shear stress-mediated extracellular signal-regulated kinase (ERK1/2) stimulation. Replacement of all extracellular Na+ with either N-methyl-D-glucamine or choline chloride increased the ERK1/2 stimulation in response to shear stress by 1.89 +/- 0.1-fold. The Na+ effect was concentration-dependent (maximal effect, </=12.5 mM) and was specific for shear stress-mediated ERK1/2 activation as epidermal growth factor-stimulated ERK1/2 activation was unaffected by removal of extracellular Na+. Shear stress-mediated ERK1/2 activation was potentiated by the voltage-gated sodium channel antagonist, tetrodotoxin (100 nM), to a magnitude similar to that achieved with extracellular Na+ withdrawal. Transfection of Chinese hamster ovary cells with a rat brain type IIa voltage-gated sodium channel completely inhibited shear stress-mediated ERK1/2 activation in these cells. Inhibition was reversed by performing the experiment in sodium-free buffer or by including tetrodotoxin in the buffer. Western blotting of bovine and human EC lysates with SP19 antibody detected a 250-kDa protein consistent with the voltage-gated sodium channel. Degenerate polymerase chain reaction of cDNA from primary human EC yielded transcripts whose sequences were identical to the sodium channel SCN4a and SCN8a alpha subunit genes. These results indicate that shear stress-mediated ERK1/2 activation is regulated by extracellular sodium and demonstrate that ion transport via Na+ channels modulates EC responses to shear stress.</abstract><cop>United States</cop><pmid>10400628</pmid><doi>10.1074/jbc.274.29.20144</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Base Sequence Calcium Channels - metabolism Calcium-Calmodulin-Dependent Protein Kinases - metabolism Carrier Proteins - antagonists & inhibitors Cattle Cells, Cultured CHO Cells Cricetinae DNA Endothelium, Vascular - enzymology Endothelium, Vascular - metabolism Enzyme Activation Humans Ion Channel Gating Molecular Sequence Data Potassium - metabolism Rats Sodium - metabolism Sodium Channels - metabolism Space life sciences |
| title | Shear stress-mediated extracellular signal-regulated kinase activation is regulated by sodium in endothelial cells. Potential role for a voltage-dependent sodium channel |
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