• LOGIN
    Login with username and password
Repository logo

BORIS Portal

Bern Open Repository and Information System

  • Publications
  • Theses
  • Research Data
  • Projects
  • Organizations
  • Researchers
  • More
  • Collections
  • Statistics
  • LOGIN
    Login with username and password
Repository logo
Unibern.ch
  1. Home
  2. Publications
  3. Syntrophin mutation associated with long QT syndrome through activation of the nNOS-SCN5A macromolecular complex.
 

Syntrophin mutation associated with long QT syndrome through activation of the nNOS-SCN5A macromolecular complex.

Options
  • Details
Publisher DOI
10.1073/pnas.0801294105
PubMed ID
18591664
Description
Mutations in 11 genes that encode ion channels or their associated proteins cause inherited long QT syndrome (LQTS) and account for approximately 75-80% of cases (LQT1-11). Direct sequencing of SNTA1, the gene encoding alpha1-syntrophin, was performed in a cohort of LQTS patients that were negative for mutations in the 11 known LQTS-susceptibility genes. A missense mutation (A390V-SNTA1) was found in a patient with recurrent syncope and markedly prolonged QT interval (QTc, 530 ms). SNTA1 links neuronal nitric oxide synthase (nNOS) to the nNOS inhibitor plasma membrane Ca-ATPase subtype 4b (PMCA4b); SNTA1 also is known to associate with the cardiac sodium channel SCN5A. By using a GST-fusion protein of the C terminus of SCN5A, we showed that WT-SNTA1 interacted with SCN5A, nNOS, and PMCA4b. In contrast, A390V-SNTA1 selectively disrupted association of PMCA4b with this complex and increased direct nitrosylation of SCN5A. A390V-SNTA1 expressed with SCN5A, nNOS, and PMCA4b in heterologous cells increased peak and late sodium current compared with WT-SNTA1, and the increase was partially inhibited by NOS blockers. Expression of A390V-SNTA1 in cardiac myocytes also increased late sodium current. We conclude that the A390V mutation disrupted binding with PMCA4b, released inhibition of nNOS, caused S-nitrosylation of SCN5A, and was associated with increased late sodium current, which is the characteristic biophysical dysfunction for sodium-channel-mediated LQTS (LQT3). These results establish an SNTA1-based nNOS complex attached to SCN5A as a key regulator of sodium current and suggest that SNTA1 be considered a rare LQTS-susceptibility gene.
Date of Publication
2008-07-08
Publication Type
Article
Subject(s)
600 Technology > 610 Medicine & health
Language(s)
en
Contributor(s)
Ueda, Kazuo
Valdivia, Carmen
Medeiros Domingo, Argelia
Universitätsklinik für Kardiologie
Tester, David J.
Vatta, Matteo
Farrugia, Gianrico
Ackerman, Michael J.
Makielski, Jonathan C.
Additional Credits
Universitätsklinik für Kardiologie
Series
Proceedings of the National Academy of Sciences of the United States of America - PNAS
Publisher
National Academy of Sciences NAS
ISSN
0027-8424
Access(Rights)
metadata.only
Show full item
BORIS Portal
Bern Open Repository and Information System
Build: dd892c [ 9.04. 8:30]
Explore
  • Projects
  • Funding
  • Publications
  • Research Data
  • Organizations
  • Researchers
  • Audiovisual Material
  • Software & other digital items
  • Events
More
  • About BORIS Portal
  • Send Feedback
  • Cookie settings
  • Service Policy
Follow us on
  • Mastodon
  • YouTube
  • LinkedIn
UniBe logo