IndraLab

Statements


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reach
"The reasons for this are not known, but it could be that there are additional regulatory components in the native myocytes that are regulating the interaction of SNTA1 and SCN5A."

No evidence text available

No evidence text available

sparser
"Moreover, the functional studies for the complex SCN5A-SNTA1 (lacking both nNOS and PMCA4b) or SCN5A-SNTA1-nNOS complex (lacking PMCA4b) suggest that the three SNTA1 mutations do not cause increased late I Na by a direct interaction between SNTA1 and SCN5A or between SNTA1 and nNOS."

sparser
"A257G) which precipitated a marked increase in peak I Na and altered Nav1.5 channel kinetics in both HEK293 cells and cardiomyocytes through direct interaction of mutant SNTA1 with SCN5A. xref All these findings suggest that SNTA1 is a crucial Nav1.5 channel interacting protein (ChIP) involved in maintaining the normal function of the cardiac sodium channel."

reach
"Moreover, the functional studies for the complex SCN5A and SNTA1 (lacking both nNOS and PMCA4b) or SCN5A, SNTA1, and nNOS complex (lacking PMCA4b) suggest that the three SNTA1 mutations do not cause increased late I Na by a direct interaction between SNTA1 and SCN5A or between SNTA1 and nNOS."

reach
"By using a GST-fusion protein of the C terminus of SCN5A, we showed that WT-SNTA1 interacted with SCN5A, nNOS, and PMCA4b."

reach
"Additionally, alpha1-syntrophin interacts with SCN5A and nNOS and PMCA4b complex in cardiomyocytes."

No evidence text available

sparser
"The reasons for this are not known, but it could be that there are additional regulatory components in the native myocytes that are regulating the interaction of SNTA1 and SCN5A. Alternatively, the stoichiometry of the transfected/infected components may be different between the two systems."