Sustained Intracellular Acidosis Triggers the Na + /H + Exchager-1 Activation in Glutamate Excitotoxicity
The Na⁺/H⁺ exchanger-1 (NHE-1) is a ubiquitously expressed pH-regulatory membrane protein that functions in the brain, heart, and other organs. It is increased by intracellular acidosis through the interaction of intracellular H⁺ with an allosteric modifier site in the transport domain. In the previ...
Saved in:
| Published in | Biomolecules & therapeutics Vol. 25; no. 6; pp. 593 - 598 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Korea (South)
The Korean Society of Applied Pharmacology
01.11.2017
한국응용약물학회 |
| Subjects | |
| Online Access | Get full text |
| ISSN | 2005-4483 1976-9148 1976-9148 2005-4483 |
| DOI | 10.4062/biomolther.2017.018 |
Cover
| Abstract | The Na⁺/H⁺ exchanger-1 (NHE-1) is a ubiquitously expressed pH-regulatory membrane protein that functions in the brain, heart, and other organs. It is increased by intracellular acidosis through the interaction of intracellular H⁺ with an allosteric modifier site in the transport domain. In the previous study, we reported that glutamate-induced NHE-1 phosphorylation mediated by activation of protein kinase C-β (PKC-β) in cultured neuron cells via extracellular signal-regulated kinases (ERK)/p90 ribosomal s6 kinases (p90RSK) pathway results in NHE-1 activation. However, whether glutamate stimulates NHE-1 activity solely by the allosteric mechanism remains elusive. Cultured primary cortical neuronal cells were subjected to intracellular acidosis by exposure to 100 μM glutamate or 20 mM NH₄Cl. After the desired duration of intracellular acidosis, the phosphorylation and activation of PKC-β, ERK1/2 and p90RSK were determined by Western blotting. We investigated whether the duration of intracellular acidosis is controlled by glutamate exposure time. The NHE-1 activation increased while intracellular acidosis sustained for 〉3 min. To determine if sustained intracellular acidosis induced NHE-1 phosphorylation, we examined phosphorylation of NHE-1 induced by intracellular acidosis by transient exposure to NH₄Cl. Sustained intracellular acidosis led to activation and phosphorylation of NHE-1. In addition, sustained intracellular acidosis also activated the PKC-β, ERK1/2, and p90RSK in neuronal cells. We conclude that glutamate stimulates NHE-1 activity through sustained intracellular acidosis, which mediates NHE-1 phosphorylation regulated by PKC-β/ERK1/2/p90RSK pathway in neuronal cells. |
|---|---|
| AbstractList | The Na+/H+ exchanger-1 (NHE-1) is a ubiquitously expressed pH-regulatory membrane protein that functions in the brain, heart, and other organs. It is increased by intracellular acidosis through the interaction of intracellular H+ with an allosteric modifier site in the transport domain. In the previous study, we reported that glutamate-induced NHE-1 phosphorylation mediated by activation of protein kinase C-β (PKC-β) in cultured neuron cells via extracellular signal-regulated kinases (ERK)/p90 ribosomal s6 kinases (p90RSK) pathway results in NHE-1 activation. However, whether glutamate stimulates NHE-1 activity solely by the allosteric mechanism remains elusive. Cultured primary cortical neuronal cells were subjected to intracellular acidosis by exposure to 100 μM glutamate or 20 mM NH4Cl. After the desired duration of intracellular acidosis, the phosphorylation and activation of PKC-β, ERK1/2 and p90RSK were determined by Western blotting. We investigated whether the duration of intracellular acidosis is controlled by glutamate exposure time. The NHE-1 activation increased while intracellular acidosis sustained for >3 min. To determine if sustained intracellular acidosis induced NHE-1 phosphorylation, we examined phosphorylation of NHE-1 induced by intracellular acidosis by transient exposure to NH4Cl. Sustained intracellular acidosis led to activation and phosphorylation of NHE-1. In addition, sustained intracellular acidosis also activated the PKC-β, ERK1/2, and p90RSK in neuronal cells. We conclude that glutamate stimulates NHE-1 activity through sustained intracellular acidosis, which mediates NHE-1 phosphorylation regulated by PKC-β/ERK1/2/p90RSK pathway in neuronal cells. The Na+/H+ exchanger-1 (NHE-1) is a ubiquitously expressed pH-regulatory membrane protein that functions in the brain, heart, and other organs. It is increased by intracellular acidosis through the interaction of intracellular H+ with an allosteric modifier site in the transport domain. In the previous study, we reported that glutamate-induced NHE-1 phosphorylation mediated by activation of protein kinase C-β (PKC-β) in cultured neuron cells via extracellular signal-regulated kinases (ERK)/p90 ribosomal s6 kinases (p90RSK) pathway results in NHE-1 activation. However, whether glutamate stimulates NHE-1 activity solely by the allosteric mechanism remains elusive. Cultured primary cortical neuronal cells were subjected to intracellular acidosis by exposure to 100 μM glutamate or 20 mM NH4Cl. After the desired duration of intracellular acidosis, the phosphorylation and activation of PKC-β, ERK1/2 and p90RSK were determined by Western blotting. We investigated whether the duration of intracellular acidosis is controlled by glutamate exposure time. The NHE-1 activation increased while intracellular acidosis sustained for >3 min. To determine if sustained intracellular acidosis induced NHE-1 phosphorylation, we examined phosphorylation of NHE-1 induced by intracellular acidosis by transient exposure to NH4Cl. Sustained intracellular acidosis led to activation and phosphorylation of NHE-1. In addition, sustained intracellular acidosis also activated the PKC-β, ERK1/2, and p90RSK in neuronal cells. We conclude that glutamate stimulates NHE-1 activity through sustained intracellular acidosis, which mediates NHE-1 phosphorylation regulated by PKC-β/ERK1/2/p90RSK pathway in neuronal cells. KCI Citation Count: 8 The Na⁺/H⁺ exchanger-1 (NHE-1) is a ubiquitously expressed pH-regulatory membrane protein that functions in the brain, heart, and other organs. It is increased by intracellular acidosis through the interaction of intracellular H⁺ with an allosteric modifier site in the transport domain. In the previous study, we reported that glutamate-induced NHE-1 phosphorylation mediated by activation of protein kinase C-β (PKC-β) in cultured neuron cells via extracellular signal-regulated kinases (ERK)/p90 ribosomal s6 kinases (p90RSK) pathway results in NHE-1 activation. However, whether glutamate stimulates NHE-1 activity solely by the allosteric mechanism remains elusive. Cultured primary cortical neuronal cells were subjected to intracellular acidosis by exposure to 100 μM glutamate or 20 mM NH₄Cl. After the desired duration of intracellular acidosis, the phosphorylation and activation of PKC-β, ERK1/2 and p90RSK were determined by Western blotting. We investigated whether the duration of intracellular acidosis is controlled by glutamate exposure time. The NHE-1 activation increased while intracellular acidosis sustained for 〉3 min. To determine if sustained intracellular acidosis induced NHE-1 phosphorylation, we examined phosphorylation of NHE-1 induced by intracellular acidosis by transient exposure to NH₄Cl. Sustained intracellular acidosis led to activation and phosphorylation of NHE-1. In addition, sustained intracellular acidosis also activated the PKC-β, ERK1/2, and p90RSK in neuronal cells. We conclude that glutamate stimulates NHE-1 activity through sustained intracellular acidosis, which mediates NHE-1 phosphorylation regulated by PKC-β/ERK1/2/p90RSK pathway in neuronal cells.The Na⁺/H⁺ exchanger-1 (NHE-1) is a ubiquitously expressed pH-regulatory membrane protein that functions in the brain, heart, and other organs. It is increased by intracellular acidosis through the interaction of intracellular H⁺ with an allosteric modifier site in the transport domain. In the previous study, we reported that glutamate-induced NHE-1 phosphorylation mediated by activation of protein kinase C-β (PKC-β) in cultured neuron cells via extracellular signal-regulated kinases (ERK)/p90 ribosomal s6 kinases (p90RSK) pathway results in NHE-1 activation. However, whether glutamate stimulates NHE-1 activity solely by the allosteric mechanism remains elusive. Cultured primary cortical neuronal cells were subjected to intracellular acidosis by exposure to 100 μM glutamate or 20 mM NH₄Cl. After the desired duration of intracellular acidosis, the phosphorylation and activation of PKC-β, ERK1/2 and p90RSK were determined by Western blotting. We investigated whether the duration of intracellular acidosis is controlled by glutamate exposure time. The NHE-1 activation increased while intracellular acidosis sustained for 〉3 min. To determine if sustained intracellular acidosis induced NHE-1 phosphorylation, we examined phosphorylation of NHE-1 induced by intracellular acidosis by transient exposure to NH₄Cl. Sustained intracellular acidosis led to activation and phosphorylation of NHE-1. In addition, sustained intracellular acidosis also activated the PKC-β, ERK1/2, and p90RSK in neuronal cells. We conclude that glutamate stimulates NHE-1 activity through sustained intracellular acidosis, which mediates NHE-1 phosphorylation regulated by PKC-β/ERK1/2/p90RSK pathway in neuronal cells. The Na⁺/H⁺ exchanger-1 (NHE-1) is a ubiquitously expressed pH-regulatory membrane protein that functions in the brain, heart, and other organs. It is increased by intracellular acidosis through the interaction of intracellular H⁺ with an allosteric modifier site in the transport domain. In the previous study, we reported that glutamate-induced NHE-1 phosphorylation mediated by activation of protein kinase C-β (PKC-β) in cultured neuron cells via extracellular signal-regulated kinases (ERK)/p90 ribosomal s6 kinases (p90RSK) pathway results in NHE-1 activation. However, whether glutamate stimulates NHE-1 activity solely by the allosteric mechanism remains elusive. Cultured primary cortical neuronal cells were subjected to intracellular acidosis by exposure to 100 μM glutamate or 20 mM NH₄Cl. After the desired duration of intracellular acidosis, the phosphorylation and activation of PKC-β, ERK1/2 and p90RSK were determined by Western blotting. We investigated whether the duration of intracellular acidosis is controlled by glutamate exposure time. The NHE-1 activation increased while intracellular acidosis sustained for 〉3 min. To determine if sustained intracellular acidosis induced NHE-1 phosphorylation, we examined phosphorylation of NHE-1 induced by intracellular acidosis by transient exposure to NH₄Cl. Sustained intracellular acidosis led to activation and phosphorylation of NHE-1. In addition, sustained intracellular acidosis also activated the PKC-β, ERK1/2, and p90RSK in neuronal cells. We conclude that glutamate stimulates NHE-1 activity through sustained intracellular acidosis, which mediates NHE-1 phosphorylation regulated by PKC-β/ERK1/2/p90RSK pathway in neuronal cells. |
| Author | Jung, Yi-Sook Lee, Bo Kyung |
| AuthorAffiliation | 1 College of Pharmacy, Ajou University, Suwon 16499, Republic of Korea 2 Research Institute of Pharmaceutical Sciences and Technology, Ajou University, Suwon 16499, Republic of Korea |
| AuthorAffiliation_xml | – name: 1 College of Pharmacy, Ajou University, Suwon 16499, Republic of Korea – name: 2 Research Institute of Pharmaceutical Sciences and Technology, Ajou University, Suwon 16499, Republic of Korea |
| Author_xml | – sequence: 1 givenname: Bo Kyung surname: Lee fullname: Lee, Bo Kyung organization: College of Pharmacy, Ajou University, Suwon 16499, Republic of Korea – sequence: 2 givenname: Yi-Sook surname: Jung fullname: Jung, Yi-Sook organization: College of Pharmacy, Ajou University, Suwon 16499, Republic of Korea, Research Institute of Pharmaceutical Sciences and Technology, Ajou University, Suwon 16499, Republic of Korea |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/28605830$$D View this record in MEDLINE/PubMed https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART002280018$$DAccess content in National Research Foundation of Korea (NRF) |
| BookMark | eNqNkVFv0zAUhS00xLrBL0BCeQShdNeO7TgvSNU0tkoTSFCeLTdxWjPHLrYz1n-Psw4GPCBefCX7O_dcn3uCjpx3GqGXGOYUODlbGz94m7Y6zAngeg5YPEEz3NS8bDAVR2hGAFhJqaiO0UmMXwF4jRl_ho6J4MBEBTNkPo8xKeN0VyxdCqrV1o5WhWLRms5HE4tVMJuNDrHITsUHVbwtzq7ycXHXblW-L3FGk7lVyXhXGFdc2jGpQSU9ISb55O9Mrvvn6GmvbNQvHuop-vL-YnV-VV5_vFyeL67LllZNKnWleooZgboB6KhucFdVPRYdYRzWSrRcENYpLXCr6453WGCoaQ99pTlmvapO0ZtDXxd6edMa6ZW5rxsvb4JcfFotJcHACCOZpQd2dDu1_66slbtgBhX2EoOcUpaPKcspZZlTzrJ3B9luXA-6a_WU3KN0MvzzxZlttr-VjAtGydTg9UOD4L-NOiY5mDhFr5z2Y5S4gSYnIHCd0Ve_e_0y-bnCDFQHoA0-xqD7__xC85cq7-h-h3lgY_-p_QFixcc8 |
| CitedBy_id | crossref_primary_10_1038_s41598_021_88089_8 crossref_primary_10_1113_JP283834 crossref_primary_10_1007_s00018_022_04393_0 crossref_primary_10_17116_jnevro201911902135 crossref_primary_10_1016_j_brs_2020_03_008 crossref_primary_10_1038_s41598_024_54249_9 crossref_primary_10_17116_jnevro2020120061144 crossref_primary_10_1016_j_hrthm_2019_01_029 crossref_primary_10_1007_s00702_018_1904_2 crossref_primary_10_1016_j_abb_2024_109951 crossref_primary_10_3389_fmmed_2021_777088 crossref_primary_10_1007_s11064_021_03297_y crossref_primary_10_17116_jnevro202412408256 crossref_primary_10_1016_j_lfs_2018_05_005 crossref_primary_10_17116_jnevro201711710144_48 |
| Cites_doi | 10.1152/ajpregu.91038.2008 10.1101/cshperspect.a004556 10.1016/0166-2236(92)90191-A 10.1113/jphysiol.2004.071068 10.1161/CIRCRESAHA.108.175877 10.1042/BJ20051628 10.1016/j.ejphar.2007.03.056 10.1152/physrev.1981.61.2.296 10.1073/pnas.87.16.6445 10.1016/j.cellsig.2013.12.011 10.1152/jn.1994.72.6.2563 10.1111/j.1749-6632.1989.tb25165.x 10.1016/S0896-6273(01)00535-9 10.3389/fphys.2014.00043 10.1523/JNEUROSCI.13-11-04690.1993 10.1016/j.brainres.2008.10.061 10.1016/j.bbrc.2004.05.217 10.1161/01.STR.0000106910.42815.C2 10.1074/jbc.274.29.20206 10.1016/0896-6273(93)90183-R 10.1523/JNEUROSCI.14-03-01352.1994 10.1073/pnas.1312982110 10.1111/j.1471-4159.2008.05355.x 10.1074/jbc.M413015200 10.1074/jbc.M114.555284 10.1002/jnr.22818 10.1074/jbc.M304400200 |
| ContentType | Journal Article |
| Copyright | Copyright © 2017 The Korean Society of Applied Pharmacology 2017 |
| Copyright_xml | – notice: Copyright © 2017 The Korean Society of Applied Pharmacology 2017 |
| DBID | AAYXX CITATION NPM 7X8 5PM ADTOC UNPAY ACYCR |
| DOI | 10.4062/biomolther.2017.018 |
| DatabaseName | CrossRef PubMed MEDLINE - Academic PubMed Central (Full Participant titles) Unpaywall for CDI: Periodical Content Unpaywall Korean Citation Index |
| DatabaseTitle | CrossRef PubMed MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic PubMed |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: UNPAY name: Unpaywall url: https://proxy.k.utb.cz/login?url=https://unpaywall.org/ sourceTypes: Open Access Repository |
| DeliveryMethod | fulltext_linktorsrc |
| EISSN | 1976-9148 2005-4483 |
| EndPage | 598 |
| ExternalDocumentID | oai_kci_go_kr_ARTI_2105252 oai:pubmedcentral.nih.gov:5685428 PMC5685428 28605830 10_4062_biomolther_2017_018 |
| Genre | Journal Article |
| GroupedDBID | --- 23N 5-W 5GY 8JR 9ZL AAYXX ADBBV ADRAZ AENEX ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL CITATION DIK DU5 EF. F5P HYE HZB JDI KQ8 M48 OK1 PGMZT RPM .UV NPM 7X8 5PM ADTOC UNPAY ACYCR |
| ID | FETCH-LOGICAL-c439t-e3af415207900d4e91d33f18d2560ba8c6825dae81ce7d6d181074f0f3e615fa3 |
| IEDL.DBID | M48 |
| ISSN | 2005-4483 1976-9148 |
| IngestDate | Tue Nov 21 21:37:16 EST 2023 Wed Oct 29 11:17:56 EDT 2025 Tue Sep 30 16:55:50 EDT 2025 Thu Jul 10 18:09:57 EDT 2025 Thu Jan 02 22:21:20 EST 2025 Thu Apr 24 23:12:37 EDT 2025 Tue Jul 01 04:15:28 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | false |
| IsScholarly | true |
| Issue | 6 |
| Keywords | Na⁺/H⁺ exchanger-1 Sustained acidosis Extracellular signal-regulated kinases 1/2 Glutamate Cortical neurons Protein kinase C-β |
| Language | English |
| License | This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c439t-e3af415207900d4e91d33f18d2560ba8c6825dae81ce7d6d181074f0f3e615fa3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| OpenAccessLink | http://journals.scholarsportal.info/openUrl.xqy?doi=10.4062/biomolther.2017.018 |
| PMID | 28605830 |
| PQID | 1909207817 |
| PQPubID | 23479 |
| PageCount | 6 |
| ParticipantIDs | nrf_kci_oai_kci_go_kr_ARTI_2105252 unpaywall_primary_10_4062_biomolther_2017_018 pubmedcentral_primary_oai_pubmedcentral_nih_gov_5685428 proquest_miscellaneous_1909207817 pubmed_primary_28605830 crossref_primary_10_4062_biomolther_2017_018 crossref_citationtrail_10_4062_biomolther_2017_018 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2017-11-01 |
| PublicationDateYYYYMMDD | 2017-11-01 |
| PublicationDate_xml | – month: 11 year: 2017 text: 2017-11-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | Korea (South) |
| PublicationPlace_xml | – name: Korea (South) |
| PublicationTitle | Biomolecules & therapeutics |
| PublicationTitleAlternate | Biomol Ther (Seoul) |
| PublicationYear | 2017 |
| Publisher | The Korean Society of Applied Pharmacology 한국응용약물학회 |
| Publisher_xml | – name: The Korean Society of Applied Pharmacology – name: 한국응용약물학회 |
| References | ref13 ref12 ref15 ref14 ref11 ref10 ref2 ref1 ref17 ref16 ref19 ref18 ref24 ref23 ref26 ref25 ref20 ref22 ref21 ref27 ref8 ref7 ref9 ref4 ref3 ref6 ref5 18757828 - Circ Res. 2008 Oct 10;103(8):881-90 15840586 - J Biol Chem. 2005 Jun 24;280(25):24135-42 2483875 - Ann N Y Acad Sci. 1989;574:287-93 19022230 - Brain Res. 2009 Jan 12;1248:22-30 15550467 - J Physiol. 2005 Jan 15;562(Pt 2):455-75 14671239 - Stroke. 2004 Jan;35(1):185-90 7897473 - J Neurophysiol. 1994 Dec;72(6):2563-9 8102533 - Neuron. 1993 Aug;11(2):267-77 11754841 - Neuron. 2001 Dec 20;32(6):1107-17 7901350 - J Neurosci. 1993 Nov;13(11):4690-9 22420041 - J Neurosci Res. 2012 Apr;90(4):860-9 24936055 - J Biol Chem. 2014 Jul 25;289(30):20879-97 24592239 - Front Physiol. 2014 Feb 13;5:43 17482160 - Eur J Pharmacol. 2007 Jul 12;567(1-2):131-8 1696732 - Proc Natl Acad Sci U S A. 1990 Aug;87(16):6445-9 8120630 - J Neurosci. 1994 Mar;14(3 Pt 1):1352-7 23940334 - Proc Natl Acad Sci U S A. 2013 Aug 27;110(35):14426-31 12791686 - J Biol Chem. 2003 Aug 22;278(34):31676-84 7012859 - Physiol Rev. 1981 Apr;61(2):296-434 10400637 - J Biol Chem. 1999 Jul 16;274(29):20206-14 1279865 - Trends Neurosci. 1992 Oct;15(10):396-402 18363831 - J Neurochem. 2008 Jul;106(1):231-43 24378530 - Cell Signal. 2014 Apr;26(4):697-704 19710385 - Am J Physiol Regul Integr Comp Physiol. 2009 Nov;297(5):R1409-20 15240117 - Biochem Biophys Res Commun. 2004 Jul 30;320(3):789-94 21628429 - Cold Spring Harb Perspect Biol. 2011 Jul 01;3(7):null 16831126 - Biochem J. 2006 Nov 1;399(3):493-501 |
| References_xml | – ident: ref11 doi: 10.1152/ajpregu.91038.2008 – ident: ref16 doi: 10.1101/cshperspect.a004556 – ident: ref1 doi: 10.1016/0166-2236(92)90191-A – ident: ref27 doi: 10.1113/jphysiol.2004.071068 – ident: ref22 doi: 10.1161/CIRCRESAHA.108.175877 – ident: ref6 doi: 10.1042/BJ20051628 – ident: ref12 doi: 10.1016/j.ejphar.2007.03.056 – ident: ref20 doi: 10.1152/physrev.1981.61.2.296 – ident: ref24 doi: 10.1073/pnas.87.16.6445 – ident: ref15 doi: 10.1016/j.cellsig.2013.12.011 – ident: ref26 doi: 10.1152/jn.1994.72.6.2563 – ident: ref25 doi: 10.1111/j.1749-6632.1989.tb25165.x – ident: ref2 doi: 10.1016/S0896-6273(01)00535-9 – ident: ref21 doi: 10.3389/fphys.2014.00043 – ident: ref4 doi: 10.1523/JNEUROSCI.13-11-04690.1993 – ident: ref13 doi: 10.1016/j.brainres.2008.10.061 – ident: ref10 doi: 10.1016/j.bbrc.2004.05.217 – ident: ref17 doi: 10.1161/01.STR.0000106910.42815.C2 – ident: ref23 doi: 10.1074/jbc.274.29.20206 – ident: ref3 doi: 10.1016/0896-6273(93)90183-R – ident: ref7 doi: 10.1523/JNEUROSCI.14-03-01352.1994 – ident: ref18 doi: 10.1073/pnas.1312982110 – ident: ref19 doi: 10.1111/j.1471-4159.2008.05355.x – ident: ref8 doi: 10.1074/jbc.M413015200 – ident: ref9 doi: 10.1074/jbc.M114.555284 – ident: ref14 doi: 10.1002/jnr.22818 – ident: ref5 doi: 10.1074/jbc.M304400200 – reference: 10400637 - J Biol Chem. 1999 Jul 16;274(29):20206-14 – reference: 1279865 - Trends Neurosci. 1992 Oct;15(10):396-402 – reference: 24378530 - Cell Signal. 2014 Apr;26(4):697-704 – reference: 16831126 - Biochem J. 2006 Nov 1;399(3):493-501 – reference: 8102533 - Neuron. 1993 Aug;11(2):267-77 – reference: 17482160 - Eur J Pharmacol. 2007 Jul 12;567(1-2):131-8 – reference: 19022230 - Brain Res. 2009 Jan 12;1248:22-30 – reference: 1696732 - Proc Natl Acad Sci U S A. 1990 Aug;87(16):6445-9 – reference: 24592239 - Front Physiol. 2014 Feb 13;5:43 – reference: 12791686 - J Biol Chem. 2003 Aug 22;278(34):31676-84 – reference: 23940334 - Proc Natl Acad Sci U S A. 2013 Aug 27;110(35):14426-31 – reference: 15550467 - J Physiol. 2005 Jan 15;562(Pt 2):455-75 – reference: 8120630 - J Neurosci. 1994 Mar;14(3 Pt 1):1352-7 – reference: 21628429 - Cold Spring Harb Perspect Biol. 2011 Jul 01;3(7):null – reference: 18363831 - J Neurochem. 2008 Jul;106(1):231-43 – reference: 22420041 - J Neurosci Res. 2012 Apr;90(4):860-9 – reference: 14671239 - Stroke. 2004 Jan;35(1):185-90 – reference: 18757828 - Circ Res. 2008 Oct 10;103(8):881-90 – reference: 2483875 - Ann N Y Acad Sci. 1989;574:287-93 – reference: 7901350 - J Neurosci. 1993 Nov;13(11):4690-9 – reference: 15240117 - Biochem Biophys Res Commun. 2004 Jul 30;320(3):789-94 – reference: 7012859 - Physiol Rev. 1981 Apr;61(2):296-434 – reference: 15840586 - J Biol Chem. 2005 Jun 24;280(25):24135-42 – reference: 24936055 - J Biol Chem. 2014 Jul 25;289(30):20879-97 – reference: 19710385 - Am J Physiol Regul Integr Comp Physiol. 2009 Nov;297(5):R1409-20 – reference: 11754841 - Neuron. 2001 Dec 20;32(6):1107-17 – reference: 7897473 - J Neurophysiol. 1994 Dec;72(6):2563-9 |
| SSID | ssj0067156 |
| Score | 2.162288 |
| Snippet | The Na⁺/H⁺ exchanger-1 (NHE-1) is a ubiquitously expressed pH-regulatory membrane protein that functions in the brain, heart, and other organs. It is increased... The Na+/H+ exchanger-1 (NHE-1) is a ubiquitously expressed pH-regulatory membrane protein that functions in the brain, heart, and other organs. It is increased... |
| SourceID | nrf unpaywall pubmedcentral proquest pubmed crossref |
| SourceType | Open Website Open Access Repository Aggregation Database Index Database Enrichment Source |
| StartPage | 593 |
| SubjectTerms | Original 약학 |
| SummonAdditionalLinks | – databaseName: Unpaywall dbid: UNPAY link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3db9MwELdY9wAvbIiPhY_JIN6GO8dO4uSxQhsdEhUSqzSeLCe2t6hVMrWp2PbXc5e03aoBGk-JlIs_zufc72L7d4R8jAFyhAnPmc2sZVEoEpaJUDKvZOalz7zzeMD52ygZjqOvZ_HZLU3OneV78DTiEM-g11OEQrgLS_V5mG6R7SQG3N0j2-PR98HPdtlYQRVhmyqrpdaEmEN2FEN_K2XDDW1VM_8nhHl_o-TjRXVprn-Z6fSOFzre6dIZzVvyQtx8Mukvmrxf3NyndnxAB3fJ0yUYpYPOep6RR656TtyP7kyVs_QE24O_9nGvKh0Upa3n5ZyeQkR_DrCRQoF0ZA4OhwdHV8UFsmGwEMRWGdNoWdEvYNkGULGjIAJfj6a-KuF6_YKMj49OPw_ZMhkDKwCzNMxJ49HZc5VxbiOXhVZKH6YWMVNu0iKBWNMal4aFUzaxgBwAnXjupQPQ5I18SXpVXbk9Qi3AvMQqVeTcRJECBynS3LsYmXgktyIgYjU2ulgylWPCjKmGiAW1pm-1plFrGrQWkE_rly47oo5_i3-AQdeTotRIsI3X81pPZhrCiBMNcXAsYmjI-5VNaJh1qG9TuXox1wCjMoE8SSogrzobWdcqUlxqljwgasN61gJY4eaTqrxomb3jJI1BGQFhazt7SGde_6f8G_IEb7sjlW9Jr5kt3DvAVk2-v5xUvwHITCK3 priority: 102 providerName: Unpaywall |
| Title | Sustained Intracellular Acidosis Triggers the Na + /H + Exchager-1 Activation in Glutamate Excitotoxicity |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/28605830 https://www.proquest.com/docview/1909207817 https://pubmed.ncbi.nlm.nih.gov/PMC5685428 http://doi.org/10.4062/biomolther.2017.018 https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART002280018 |
| UnpaywallVersion | submittedVersion |
| Volume | 25 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| ispartofPNX | Biomolecules & Therapeutics, 2017, 25(6), , pp.593-598 |
| journalDatabaseRights | – providerCode: PRVAFT databaseName: Open Access Digital Library customDbUrl: eissn: 1976-9148 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0067156 issn: 1976-9148 databaseCode: KQ8 dateStart: 20120101 isFulltext: true titleUrlDefault: http://grweb.coalliance.org/oadl/oadl.html providerName: Colorado Alliance of Research Libraries – providerCode: PRVBFR databaseName: Free Medical Journals customDbUrl: eissn: 1976-9148 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0067156 issn: 1976-9148 databaseCode: DIK dateStart: 20080101 isFulltext: true titleUrlDefault: http://www.freemedicaljournals.com providerName: Flying Publisher – providerCode: PRVERR databaseName: KoreaMed Open Access customDbUrl: eissn: 1976-9148 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0067156 issn: 1976-9148 databaseCode: 5-W dateStart: 20130101 isFulltext: true titleUrlDefault: https://koreamed.org/journals providerName: Korean Association of Medical Journal Editors – providerCode: PRVAQN databaseName: PubMed Central customDbUrl: eissn: 1976-9148 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0067156 issn: 1976-9148 databaseCode: RPM dateStart: 20120101 isFulltext: true titleUrlDefault: https://www.ncbi.nlm.nih.gov/pmc/ providerName: National Library of Medicine – providerCode: PRVFZP databaseName: Scholars Portal Journals: Open Access customDbUrl: eissn: 1976-9148 dateEnd: 20250930 omitProxy: true ssIdentifier: ssj0067156 issn: 1976-9148 databaseCode: M48 dateStart: 20120101 isFulltext: true titleUrlDefault: http://journals.scholarsportal.info providerName: Scholars Portal |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB71cYALAvEKlMogbiXbOE7i5IRWqGWL1BUSXamcLCe226hRUvah7v57Zjab0IqCEKcc4tjOPDLfxPY3AO9jhBw8CXLfZMb4EQ8TPwu58J0UmRMuc9bRAefTcTKaRF_O4_Mt6KqibgQ4uze1o3pSk2k1WP5YfUSHR_w6wHAUHtJB9aYivERbteQg4Ok27GKoyqiWw2nULyskkq_LuXKMwejlUdrSEP2pEyIKTmnZkLZI34pa2_XU3QdIf99X-WBRX-vVja6qW0Hr-DE82qBNNmzN4wls2fopuG_toSlr2An1QP_uaTMqGxalaWbljJ1hyn6BuJDhRNlYHxyODtjRsrgkvgufY7uuJhora_YZbVcj7rXUBL8P82ZZ4nX1DCbHR2efRv6m3IJfICqZ-1ZoR-E8kFkQmMhm3AjheGoIFeU6LRLMJo22KS-sNIlBbID4wwVOWIRFTovnsFM3tX0JzCCQS4yURR7oKJIYAsM0dzYmrh0RmNCDsBOnKjZc5FQSo1KYk5A61C91KFKHQnV48KF_6Lql4vh783eoJ3VVlIootOl60airqcJE4URhphuHMU7kbadGhX5FAte1bRYzhUApC4kJSXrwolVrP2pnFR7IOwrvG9CAd-_U5eWauztO0hiF4YHfm8a_vMyr_x7pNTykTtrjk3uwM58u7BvEUfN8f-0b-7A7GX8dfv8JueYglw |
| linkProvider | Scholars Portal |
| linkToUnpaywall | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3db9MwELdY9wAvbIiPhY_JIN6GO8dO4uSxQhsdEhUSqzSeLCe2t6hVMrWp2PbXc5e03aoBGk-JlIs_zufc72L7d4R8jAFyhAnPmc2sZVEoEpaJUDKvZOalz7zzeMD52ygZjqOvZ_HZLU3OneV78DTiEM-g11OEQrgLS_V5mG6R7SQG3N0j2-PR98HPdtlYQRVhmyqrpdaEmEN2FEN_K2XDDW1VM_8nhHl_o-TjRXVprn-Z6fSOFzre6dIZzVvyQtx8Mukvmrxf3NyndnxAB3fJ0yUYpYPOep6RR656TtyP7kyVs_QE24O_9nGvKh0Upa3n5ZyeQkR_DrCRQoF0ZA4OhwdHV8UFsmGwEMRWGdNoWdEvYNkGULGjIAJfj6a-KuF6_YKMj49OPw_ZMhkDKwCzNMxJ49HZc5VxbiOXhVZKH6YWMVNu0iKBWNMal4aFUzaxgBwAnXjupQPQ5I18SXpVXbk9Qi3AvMQqVeTcRJECBynS3LsYmXgktyIgYjU2ulgylWPCjKmGiAW1pm-1plFrGrQWkE_rly47oo5_i3-AQdeTotRIsI3X81pPZhrCiBMNcXAsYmjI-5VNaJh1qG9TuXox1wCjMoE8SSogrzobWdcqUlxqljwgasN61gJY4eaTqrxomb3jJI1BGQFhazt7SGde_6f8G_IEb7sjlW9Jr5kt3DvAVk2-v5xUvwHITCK3 |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Sustained+Intracellular+Acidosis+Triggers+the+Na%2B%2FH%2B+Exchager-1+Activation+in+Glutamate+Excitotoxicity&rft.jtitle=Biomolecules+%26+therapeutics&rft.au=Lee%2C+Bo+Kyung&rft.au=Jung%2C+Yi-Sook&rft.date=2017-11-01&rft.pub=The+Korean+Society+of+Applied+Pharmacology&rft.issn=1976-9148&rft.eissn=2005-4483&rft.volume=25&rft.issue=6&rft.spage=593&rft.epage=598&rft_id=info:doi/10.4062%2Fbiomolther.2017.018&rft_id=info%3Apmid%2F28605830&rft.externalDocID=PMC5685428 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2005-4483&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2005-4483&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2005-4483&client=summon |