{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T12:54:10Z","timestamp":1791204850986,"version":"4.1.0"},"reference-count":36,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2013,10,6]],"date-time":"2013-10-06T00:00:00Z","timestamp":1381017600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,10,6]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Mannan binding lectin (MBL)-associated serine protease type 1 (MASP-1) has a central role in the lectin pathway of complement activation and is required for the formation of C3 convertase. The activity of MASP-1 in the peripheral blood has been identified previously as a highly significant predictor of the severity of liver fibrosis in hepatitis C virus (HCV) infection, but not in liver disease of other aetiologies. In this study we tested the hypotheses that expression of MASP-1 may promote disease progression in HCV disease by direct activation of hepatic stellate cells (HSCs) and may additionally be up-regulated by HCV. In order to do so, we utilized a model for the maintenance of primary human HSC in the quiescent state by culture on basement membrane substrate prior to stimulation. In comparison to controls, recombinant MASP-1 stimulated quiescent human HSCs to differentiate to the activated state as assessed by both morphology and up-regulation of HSC activation markers \u03b1-smooth muscle actin and tissue inhibitor of metalloproteinase 1. Further, the expression of MASP-1 was up-regulated significantly by HCV infection in hepatocyte cell lines. These observations suggest a new role for MASP-1 and provide a possible mechanistic link between high levels of MASP-1 and the severity of disease in HCV infection. Taken together with previous clinical observations, our new findings suggest that the balance of MASP-1 activity may be proinflammatory and act to accelerate fibrosis progression in HCV liver disease.<\/jats:p>","DOI":"10.1111\/cei.12174","type":"journal-article","created":{"date-parts":[[2013,7,11]],"date-time":"2013-07-11T09:22:34Z","timestamp":1373534554000},"page":"265-273","source":"Crossref","is-referenced-by-count":25,"title":["Mannan binding lectin-associated serine protease 1 is induced by hepatitis C virus infection and activates human hepatic stellate cells"],"prefix":"10.1093","volume":"174","author":[{"given":"A","family":"Saeed","sequence":"first","affiliation":[{"name":"School of Molecular Medical Sciences, University of Nottingham, Leicester, UK"},{"name":"School of Pharmacy, University of Nottingham, Leicester, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"K","family":"Baloch","sequence":"additional","affiliation":[{"name":"School of Molecular Medical Sciences, University of Nottingham, Leicester, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R J P","family":"Brown","sequence":"additional","affiliation":[{"name":"School of Molecular Medical Sciences, University of Nottingham, Leicester, UK"},{"name":"Division of Experimental Virology, Twincore, Medical School Hannover and Helmholtz Centre for Infection Research, Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R","family":"Wallis","sequence":"additional","affiliation":[{"name":"Departments of Infection, Immunity and Inflammation and Biochemistry, University of Leicester, Leicester, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L","family":"Chen","sequence":"additional","affiliation":[{"name":"School of Molecular Medical Sciences, University of Nottingham, Leicester, UK"},{"name":"School of Pharmacy, University of Nottingham, Leicester, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L","family":"Dexter","sequence":"additional","affiliation":[{"name":"School of Molecular Medical Sciences, University of Nottingham, Leicester, UK"},{"name":"School of Pharmacy, University of Nottingham, Leicester, UK"},{"name":"Microbiology Laboratory, University Hospital of Wales, Cardiff, CF14 4XW, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C P","family":"McClure","sequence":"additional","affiliation":[{"name":"School of Molecular Medical Sciences, University of Nottingham, Leicester, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"K","family":"Shakesheff","sequence":"additional","affiliation":[{"name":"School of Pharmacy, University of Nottingham, Leicester, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B J","family":"Thomson","sequence":"additional","affiliation":[{"name":"School of Molecular Medical Sciences, University of Nottingham, Leicester, 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