4.8 Article

Distribution and partial characterisation of IgG Fc binding protein in various mucin producing cells and body fluids

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GUT
卷 51, 期 2, 页码 169-176

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BMJ PUBLISHING GROUP
DOI: 10.1136/gut.51.2.169

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Background and aims: Mucus released from goblet cells is important in intestinal mucosal defence, and mucin glycoproteins are thought to be major components of mucus. Recently, we identified and cloned another component of human colonic mucus, IgG Fc binding protein (FcgammaBP). FcgammaBP is immunologically distinct from known Fcgamma receptors and its structure contains repeated cysteine rich unit sequences resembling those present in mucins. In this work, we assessed the tissue distribution of FcgammaBP, its binding activity in various body fluids, and its ability to inhibit complement mediated haemolysis. Methods: Immunohistochemical localisation of FcgammaBP, using monoclonal antibodies against FcgammaBP (K9 or K17) and labelled IgG, was conducted in various mucin producing tissues: colon, small intestine, stomach, gall bladder, cystic duct, choledochus, bronchus, submandibular gland, conjunctiva, and cervix uteri. The binding activity of FcgammaBP in mucus extracted from colon, gastric juice, bile, nasal discharges, saliva, sputum, and tears was also examined by immunodotblot and immunoprecipitation using these monoclonal antibodies. Inhibition of complement mediated haemolysis by FcgammaBP was investigated using sheep red blood cells (SRBC) and anti-SRBC IgG. Results: The immunohistochemical study revealed that mucin secreting cells in the colon, small intestine, gall bladder, cystic duct, choledochus, bronchus, submandibular gland, and cervix uteri contained FcgammaBP, and immunodotblot and immunoprecipitation analysis using IgG and monoclonal antibodies demonstrated that the fluids secreted by these cells were capable of binding IgG. Mucin producing cells of the conjunctiva did not express FcgammaBP molecules or bind to 19G. The surface mucus cells in the stomach were variably positive for FcgammaBP. Perhaps because of proteolytic degradation, FcgammaBP in gut lavage fluid did not have IgG binding activity, although this activity was present in the Conclusions: FcgammaBP is widely expressed on mucosal surfaces and in external secretions. It is functionally intact in several fluids. These findings lend support to the concept that FcgammaBP is an important component of mucosal immunological defences.

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