IndraLab

Statements


SCN5A binds SNTA1, NOS1, and PMCA4b. 4 / 4
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"XREF_BIBR The other three variants (G54R, P56S, and T262P), while considered functionally insignificant in the modification of SCN5A channel biology and now classified as a functional insignificant variant, may have helped nevertheless to elucidate which functional domains of SNTA1 are most important in maintaining integrity and proper function of the SCN5A, nNOS, SNTA1, and PMCA4b complex."

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"In conclusion, this study implicates SNTA1 as a novel SIDS-susceptibility gene, whereby mutant SNTA1 disturbs the nNOS, SNTA1, PMCA4b, and SCN5A complex, releasing inhibition of associated nNOS by PMCA4b and resulting in increased peak and late I Na via the up-regulated endogenous NO."

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"For the SCN5A, SNTA1, nNOS, and PMCA4b complex it was shown that the SNTA1 mutation disrupted the nNOS suppressor PMCA4b from the complex [XREF_BIBR; XREF_BIBR]; in contrast, Cav3-F97C remains in the complex, but apparently has lost the ability to suppress nNOS."

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"In order to observe the effect of NOS inhibitor on the PMCA4b, nNOS, SNTA1, and SCN5A complex, L-NMMA (100 muM) was introduced into the HEK293 cell culture medium 12 hours prior to testing."