Mateusz Michalski1, Anna S Świerzko2, Sambor Sawicki3, Andrzej Kałużyński4, Jolanta Łukasiewicz5, Anna Maciejewska5, Dariusz Wydra3, Maciej Cedzyński1. 1. Laboratory of Immunobiology of Infections, Institute of Medical Biology, Polish Academy of Sciences, Lodz, Poland. 2. Laboratory of Immunobiology of Infections, Institute of Medical Biology, Polish Academy of Sciences, Lodz, Poland. Electronic address: aswierzko@cbm.pan.pl. 3. Department of Gynaecology, Oncologic Gynaecology and Gynaecologic Endocrinology, Medical University of Gdansk, Gdansk, Poland. 4. Department of Clinical Pathomorphology, Polish Mother's Memorial Hospital Research Institute, Lodz, Poland. 5. Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wroclaw, Poland.
Abstract
BACKGROUND: Ficolin-3 is a pattern-recognition molecule with the ability to activate the lectin pathway of complement. It is found in lung, liver and blood, but its physiological role is unclear. We have investigated interaction of recombinant ficolin-3 with malignant cells and tissues. MATERIAL AND METHODS: Cells of various lines of human origin as well as ovarian tissue sections have been studied with the use of flow cytometry and immunohistochemistry. RESULTS: Recombinant (but not serum-derived) ficolin-3 was found to bind strongly to the ovarian cancer cell lines, SKOV-3, OVCAR-3 and ES-2, at concentrations of 2.5 μg/ml and above. Moreover, His-tagged recombinant ficolin-3 (10 μg/ml) preferentially stained ovarian tissue sections from patients with malignant tumours compared with those from patients without. Binding to cell lines was inhibited by EDTA and specific carbohydrate ligands, indicating involvement of the fibrinogen-like domain. Binding was enhanced under mildly acidic conditions and at physiological pH after pre-incubation of cells with mildly acidic buffer. CONCLUSION: Basing on data concerning recombinant protein, it may be suggested that ficolin-3 is involved in immune response in ovarian cancer. However, unidentified serum factor(s) seem(s) to protect cancer cells from recognition by natural or rficolin-3.
BACKGROUND:Ficolin-3 is a pattern-recognition molecule with the ability to activate the lectin pathway of complement. It is found in lung, liver and blood, but its physiological role is unclear. We have investigated interaction of recombinant ficolin-3 with malignant cells and tissues. MATERIAL AND METHODS: Cells of various lines of human origin as well as ovarian tissue sections have been studied with the use of flow cytometry and immunohistochemistry. RESULTS: Recombinant (but not serum-derived) ficolin-3 was found to bind strongly to the ovarian cancer cell lines, SKOV-3, OVCAR-3 and ES-2, at concentrations of 2.5 μg/ml and above. Moreover, His-tagged recombinant ficolin-3 (10 μg/ml) preferentially stained ovarian tissue sections from patients with malignant tumours compared with those from patients without. Binding to cell lines was inhibited by EDTA and specific carbohydrate ligands, indicating involvement of the fibrinogen-like domain. Binding was enhanced under mildly acidic conditions and at physiological pH after pre-incubation of cells with mildly acidic buffer. CONCLUSION: Basing on data concerning recombinant protein, it may be suggested that ficolin-3 is involved in immune response in ovarian cancer. However, unidentified serum factor(s) seem(s) to protect cancer cells from recognition by natural or rficolin-3.
Authors: Anna Sokołowska; Anna S Świerzko; Gabriela Gajek; Aleksandra Gołos; Mateusz Michalski; Mateusz Nowicki; Agnieszka Szala-Poździej; Anna Wolska-Washer; Olga Brzezińska; Agnieszka Wierzbowska; Krzysztof Jamroziak; Marek L Kowalski; Steffen Thiel; Misao Matsushita; Jens C Jensenius; Maciej Cedzyński Journal: Sci Rep Date: 2020-06-29 Impact factor: 4.379