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With the notable exception of antibodies, the liver produces most of the circulatory glycoproteins, including the acute phase proteins released as a function of the inflammatory response. Among these proteins is \u03b2-galactoside \u03b12,6-sialyltransferase (ST6Gal1), an enzyme required for \u03b12,6-linked sialylation of glycoproteins. Here, we describe a hepatocyte-specific conditional knockout of ST6Gal1 (H-cKO) using albumin promoter-driven Cre-lox recombination. We confirm the loss of circulatory glycoprotein \u03b12,6 sialylation and note no obvious dysfunction or pathology in young H-cKO mice, yet these mice show robust changes in plasma glycoprotein fucosylation, branching and the abundance of bisecting GlcNAc and marked changes in a number of metabolic pathways. As H-cKO mice aged, they spontaneously developed fatty liver disease characterized by the buildup of fat droplets in the liver, inflammatory cytokine production and a shift in liver leukocyte phenotype away from anti-inflammatory Kupffer cells and towards proinflammatory M1 macrophages. These findings connect hepatocyte and circulatory glycoprotein sialylation to the regulation of metabolism and inflammation, potentially identifying the glycome as a new target for liver-driven disease.<\/jats:p>","DOI":"10.1093\/glycob\/cwz096","type":"journal-article","created":{"date-parts":[[2019,11,11]],"date-time":"2019-11-11T20:11:55Z","timestamp":1573503115000},"page":"346-359","source":"Crossref","is-referenced-by-count":28,"title":["Modulation of hepatocyte sialylation drives spontaneous fatty liver disease and inflammation"],"prefix":"10.1093","volume":"30","author":[{"given":"Douglas M","family":"Oswald","sequence":"first","affiliation":[{"name":"Department of Pathology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark B","family":"Jones","sequence":"first","affiliation":[{"name":"Department of Pathology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1055-2530","authenticated-orcid":false,"given":"Brian A","family":"Cobb","sequence":"first","affiliation":[{"name":"Department of Pathology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2019,11,29]]},"reference":[{"issue":"9","key":"2020050203585107700_ref1","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1016\/j.bbagen.2011.12.001","article-title":"Glycans as cancer biomarkers","volume":"1820","author":"Adamczyk","year":"2012","journal-title":"Biochim Biophys Acta - Gen Subj."},{"issue":"15","key":"2020050203585107700_ref2","doi-asserted-by":"crossref","first-page":"7085","DOI":"10.1073\/pnas.89.15.7085","article-title":"A family of erythrocyte binding proteins of malaria 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