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Severe fibrosis in hepatitis C virus‐infected patients is associated with increased activity of the mannan‐binding lectin (MBL)/MBL‐associated serine protease 1 (MASP‐1) complex
Author(s) -
Brown K. S.,
Keogh M. J.,
Tagiuri N.,
Grainge M. J.,
Presanis J. S.,
Ryder S. D.,
Irving W. L.,
Ball J. K.,
Sim R. B.,
Hickling T. P.
Publication year - 2007
Publication title -
clinical & experimental immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 135
eISSN - 1365-2249
pISSN - 0009-9104
DOI - 10.1111/j.1365-2249.2006.03264.x
Subject(s) - mannan binding lectin , immunology , lectin , hepatitis c virus , virology , biology , serine protease , fibrosis , protease , medicine , virus , enzyme , biochemistry
Summary Mannan‐binding lectin (MBL) binds microorganisms via interactions with glycans on the target surface. Bound MBL subsequently activates MBL‐associated serine protease proenzymes (MASPs). A role for MBL in hepatitis C virus (HCV) infection had been indicated by previous studies examining MBL levels and polymorphisms in relation to disease progression and response to treatment. We undertook this study to investigate a possible relationship between disease progression and functional MBL/MASP‐1 complex activity. A functional assay for MBL/MASP‐1 complex activity was employed to examine serum samples from patients with chronic HCV infection, non‐HCV liver disease and healthy controls. Intrapatient consistency of MBL/MASP‐1 complex activity levels was assessed in sequential samples from a subgroup of patients. Median values of MBL/MASP‐1 complex activity were higher in sera from patients with liver disease compared with healthy controls. MBL/MASP‐1 complex activity levels correlate with severity of fibrosis after adjusting for confounding factors ( P  = 0·003). MBL/MASP‐1 complex activity was associated more significantly with fibrosis than was MBL concentration. The potential role of MBL/MASP‐1 complex activity in disease progression is worthy of further study to investigate possible mechanistic links.

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