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Article: Regulation of Na/H + exchanger isoform 1 (NHE1) by calmodulin-binding sites: Role of angiotensin II

TitleRegulation of Na/H + exchanger isoform 1 (NHE1) by calmodulin-binding sites: Role of angiotensin II
Authors
KeywordsAngiotensin II
Calmodulin
NHE1
Issue Date2010
PublisherS Karger AG. The Journal's web site is located at http://www.karger.com/CPB
Citation
Cellular Physiology And Biochemistry, 2010, v. 26 n. 4-5, p. 541-552 How to Cite?
AbstractWe examined the effect of Angiotensin II (Ang II) on the interaction between the Ca 2+/CaM complex and hNHE1. Considering that calmodulin binds to NHE1 at two sites (A and B), amino acids at both sites were modified and two mutants were constructed: SA 1K3R/4E and SB 1K3R/4E. Wild type and mutants were transfected into PS120 cells and their activity was examined by H + flux (J H+). The basal J H+ of wild type was 4.71 ± 0.57 (mM/min), and it was similar in both mutants. However, the mutations partially impaired the binding of CaM to hNHE1. Ang II (10 -12 and 10 -9 M) increased the J H+ in wild type and SB. Ang II (10 -6 M) increased this parameter only in SA. Ang II (10 -9 M) maintained the expression of calmodulin in wild type or mutants, and Ang II (10 -6 M) decreased it in wild type or SA, but not in SB. Dimethyl-Bapta-AM (10 -7 M), a calcium chelator, suppressed the effect of Ang II (10 -9 M) in wild type. With Ang II (10 -6 M), Bapta failed to affect wild type or SA, but it increased the J H+ in SB. W13 or calmidazolium chloride (10 -5 M), two distinct calmodulin inhibitors, decreased the effect of Ang II (10 -9 M) in wild type or SB. With Ang II (10 -6 M), W13 or calmidazolium chloride decreased the J H+ in wild type or SA and increased it in SB. Thus, with Ang II (10 -12 and 10 -9 M), site A seems to be responsible for the stimulation of hNHE1 and with Ang II (10 -6 M), site B is important to maintain its basal activity. © 2010 S. Karger AG Basel.
Persistent Identifierhttp://hdl.handle.net/10722/137488
ISSN
2015 Impact Factor: 4.652
2015 SCImago Journal Rankings: 1.139
ISI Accession Number ID
Funding AgencyGrant Number
Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
Conselho Nacional de Pesquisas (CNPq)
Funding Information:

We thank Dr. Gerhard Malnic and Dr. Luciene Regina Carraro Lacroix for providing some of the drugs used here and for careful reading of the manuscript; Dr. Carlos Menck for providing the pEGFP vector; Dr. Chung Ming Tse for providing the PS120 cells; and Elida Adalgisa Neri for participation during the nucleic acid sequencing process. This study was supported by Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) and Conselho Nacional de Pesquisas (CNPq).

References

 

DC FieldValueLanguage
dc.contributor.authorEguti, DMNen_HK
dc.contributor.authorThieme, Ken_HK
dc.contributor.authorLeung, GPen_HK
dc.contributor.authorMelloAires, Men_HK
dc.contributor.authorOliveiraSouza, Men_HK
dc.date.accessioned2011-08-26T14:26:06Z-
dc.date.available2011-08-26T14:26:06Z-
dc.date.issued2010en_HK
dc.identifier.citationCellular Physiology And Biochemistry, 2010, v. 26 n. 4-5, p. 541-552en_HK
dc.identifier.issn1015-8987en_HK
dc.identifier.urihttp://hdl.handle.net/10722/137488-
dc.description.abstractWe examined the effect of Angiotensin II (Ang II) on the interaction between the Ca 2+/CaM complex and hNHE1. Considering that calmodulin binds to NHE1 at two sites (A and B), amino acids at both sites were modified and two mutants were constructed: SA 1K3R/4E and SB 1K3R/4E. Wild type and mutants were transfected into PS120 cells and their activity was examined by H + flux (J H+). The basal J H+ of wild type was 4.71 ± 0.57 (mM/min), and it was similar in both mutants. However, the mutations partially impaired the binding of CaM to hNHE1. Ang II (10 -12 and 10 -9 M) increased the J H+ in wild type and SB. Ang II (10 -6 M) increased this parameter only in SA. Ang II (10 -9 M) maintained the expression of calmodulin in wild type or mutants, and Ang II (10 -6 M) decreased it in wild type or SA, but not in SB. Dimethyl-Bapta-AM (10 -7 M), a calcium chelator, suppressed the effect of Ang II (10 -9 M) in wild type. With Ang II (10 -6 M), Bapta failed to affect wild type or SA, but it increased the J H+ in SB. W13 or calmidazolium chloride (10 -5 M), two distinct calmodulin inhibitors, decreased the effect of Ang II (10 -9 M) in wild type or SB. With Ang II (10 -6 M), W13 or calmidazolium chloride decreased the J H+ in wild type or SA and increased it in SB. Thus, with Ang II (10 -12 and 10 -9 M), site A seems to be responsible for the stimulation of hNHE1 and with Ang II (10 -6 M), site B is important to maintain its basal activity. © 2010 S. Karger AG Basel.en_HK
dc.languageengen_US
dc.publisherS Karger AG. The Journal's web site is located at http://www.karger.com/CPBen_HK
dc.relation.ispartofCellular Physiology and Biochemistryen_HK
dc.rightsCellular Physiology and Biochemistry. Copyright © S Karger AG.-
dc.subjectAngiotensin IIen_HK
dc.subjectCalmodulinen_HK
dc.subjectNHE1en_HK
dc.subject.meshAmino Acid Substitution-
dc.subject.meshAngiotensin II - pharmacology - physiology-
dc.subject.meshBinding Sites-
dc.subject.meshCalmodulin - antagonists and inhibitors - metabolism-
dc.subject.meshSodium-Hydrogen Antiporter - genetics - metabolism-
dc.titleRegulation of Na/H + exchanger isoform 1 (NHE1) by calmodulin-binding sites: Role of angiotensin IIen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1015-8987&volume=26&issue=4-5&spage=541&epage=552&date=2010&atitle=Regulation+of+Na+/H++exchanger+isoform+1+(NHE1)+by+calmodulin-binding+sites:+role+of+angiotensin+II-
dc.identifier.emailLeung, GP: gphleung@hkucc.hku.hken_HK
dc.identifier.authorityLeung, GP=rp00234en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1159/000322322en_HK
dc.identifier.pmid21063092-
dc.identifier.scopuseid_2-s2.0-78149425568en_HK
dc.identifier.hkuros189214en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-78149425568&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume26en_HK
dc.identifier.issue4-5en_HK
dc.identifier.spage541en_HK
dc.identifier.epage552en_HK
dc.identifier.isiWOS:000283859000006-
dc.publisher.placeSwitzerlanden_HK
dc.identifier.scopusauthoridEguti, DMN=25029486400en_HK
dc.identifier.scopusauthoridThieme, K=25029529000en_HK
dc.identifier.scopusauthoridLeung, GP=35963668200en_HK
dc.identifier.scopusauthoridMelloAires, M=6603767427en_HK
dc.identifier.scopusauthoridOliveiraSouza, M=6603142419en_HK

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