Title : Melatonin reduces endoplasmic reticulum stress and corneal dystrophy-associated TGFBIp through activation of endoplasmic reticulum-associated protein degradation.

Pub. Date : 2017 Oct

PMID : 28580641






2 Functional Relationships(s)
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1 Under ER stress, melatonin significantly suppressed the induction of immunoglobulin heavy-chain-binding protein (BiP) and activation of inositol-requiring enzyme 1alpha (IRE1alpha), and their downstream target, alternative splicing of X-box binding protein 1(XBP1). Melatonin endoplasmic reticulum to nucleus signaling 1 Homo sapiens
2 Notably, the reduction in BiP and IRE1alpha by melatonin was suppressed by the ubiquitin-proteasome inhibitor, MG132, but not by the autophagy inhibitor, bafilomycin A1, indicating involvement of the ER-associated protein degradation (ERAD) system. Melatonin endoplasmic reticulum to nucleus signaling 1 Homo sapiens