IndraLab

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Spadin inhibits KCNK2. 4 / 4
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"Our findings revealed a significant upregulation of PPARγ and C/EBPα expression upon inhibition of TREK-1 by Spadin treatment, indicating a potential regulatory role of TREK-1 in these adipogenic markers (Fig. 3C, D)."

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"We observed that the inhibition of TREK-1 by Spadin treatment significantly increased lipid droplet formation during adipogenic differentiation (Fig. 2H, I)."

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"We first performed recordings in control ACSF and then in the presence of acidification (pH6.2) and Spadin (500 nM, referred to by pH6.2/Spadin-application) to specifically block KCNK2 channels (42–45)."

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"Spadin, which is a 17-amino acid peptide derived from the endogenous peptide sortilin, induces a decrease in TREK1 currents by promoting the internalization of the channel (Mazella et al., 2010)."