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In this study, we sought to investigate the detrimental effects of H<jats:sub>2<\/jats:sub>S during <jats:styled-content style=\"fixed-case\">AP<\/jats:styled-content> specifically with regard to its regulation on the impaired autophagy. The incubated levels of H<jats:sub>2<\/jats:sub>S were artificially intervened by an administration of sodium hydrosulphide (Na<jats:styled-content style=\"fixed-case\">HS<\/jats:styled-content>) or <jats:styled-content style=\"fixed-case\">DL<\/jats:styled-content>\u2010propargylglycine (<jats:styled-content style=\"fixed-case\">PAG<\/jats:styled-content>) after <jats:styled-content style=\"fixed-case\">AP<\/jats:styled-content> induction. Accumulation of autophagic vacuoles and pre\u2010mature activation of trypsinogen within acini, which indicate the impairment of autophagy during <jats:styled-content style=\"fixed-case\">AP<\/jats:styled-content>, were both exacerbated by treatment with Na<jats:styled-content style=\"fixed-case\">HS<\/jats:styled-content> but attenuated by treatment with <jats:styled-content style=\"fixed-case\">PAG<\/jats:styled-content>. The regulation that H<jats:sub>2<\/jats:sub>S exerted on the impaired autophagy during <jats:styled-content style=\"fixed-case\">AP<\/jats:styled-content> was further attributed to over\u2010activation of autophagy rather than hampered autophagosome\u2013lysosome fusion. To elucidate the molecular mechanism that underlies H<jats:sub>2<\/jats:sub>S\u2010mediated over\u2010activation of autophagy during <jats:styled-content style=\"fixed-case\">AP<\/jats:styled-content>, we evaluated phosphorylations of AMP\u2010activated protein kinase (<jats:styled-content style=\"fixed-case\">AMPK<\/jats:styled-content>), <jats:styled-content style=\"fixed-case\">AKT<\/jats:styled-content> and mammalian target of rapamycin (<jats:styled-content style=\"fixed-case\">mTOR<\/jats:styled-content>). Furthermore, Compound C (<jats:styled-content style=\"fixed-case\">CC<\/jats:styled-content>) was introduced to determine the involvement of <jats:styled-content style=\"fixed-case\">mTOR<\/jats:styled-content> signalling by evaluating phosphorylations of downstream effecters including p70 S6 kinase (P70S6k) and <jats:styled-content style=\"fixed-case\">UNC<\/jats:styled-content>\u201051\u2010Like kinase 1 (<jats:styled-content style=\"fixed-case\">ULK<\/jats:styled-content>1). Our findings suggested that H<jats:sub>2<\/jats:sub>S exacerbated taurocholate\u2010induced <jats:styled-content style=\"fixed-case\">AP<\/jats:styled-content> by over\u2010activating autophagy <jats:italic>via<\/jats:italic> activation of <jats:styled-content style=\"fixed-case\">AMPK<\/jats:styled-content> and subsequently, inhibition of <jats:styled-content style=\"fixed-case\">mTOR<\/jats:styled-content>. Thus, an active suppression of H<jats:sub>2<\/jats:sub>S to restore over\u2010activated autophagy might be a promising therapeutic approach against <jats:styled-content style=\"fixed-case\">AP<\/jats:styled-content>\u2010related injuries.<\/jats:p>","DOI":"10.1111\/jcmm.12928","type":"journal-article","created":{"date-parts":[[2016,7,15]],"date-time":"2016-07-15T16:14:14Z","timestamp":1468599254000},"page":"2349-2361","source":"Crossref","is-referenced-by-count":52,"title":["Hydrogen sulphide exacerbates acute pancreatitis by over\u2010activating autophagy <i>via<\/i><scp>AMPK<\/scp>\/<scp>mTOR<\/scp> pathway"],"prefix":"10.1111","volume":"20","author":[{"given":"Liang","family":"Ji","sequence":"first","affiliation":[{"name":"Department of General Surgery The First Affiliated Hospital of Harbin Medical University Harbin China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Le","family":"Li","sequence":"additional","affiliation":[{"name":"Department of General Surgery 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