1998
DOI: 10.1016/s0161-5890(98)00052-2
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Human complement factor I: its expression by insect cells and its biochemical and structural characterisation

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Cited by 17 publications
(14 citation statements)
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“…The expression of FI may face difficulties in cells other than hepatocytes due to insufficient cellular machinery for posttranslational processing, resulting in secretion of a precursor devoid of proteolytic activity [32]. Herein, we showed for the first time that breast Beside an obvious pro-tumor activity of endogenous complement inhibitors, there are also reports showing tumor-sustaining events driven by complement activation, such as mobilization of immune suppressor cells [6] and angiogenesis [7].…”
Section: High Expression Of Fi In Tumor Cells Is Associated With Poormentioning
confidence: 82%
“…The expression of FI may face difficulties in cells other than hepatocytes due to insufficient cellular machinery for posttranslational processing, resulting in secretion of a precursor devoid of proteolytic activity [32]. Herein, we showed for the first time that breast Beside an obvious pro-tumor activity of endogenous complement inhibitors, there are also reports showing tumor-sustaining events driven by complement activation, such as mobilization of immune suppressor cells [6] and angiogenesis [7].…”
Section: High Expression Of Fi In Tumor Cells Is Associated With Poormentioning
confidence: 82%
“…Once the protein is secreted, the signal peptide of 18 residues is cleaved off. FI can be expressed recombinantly in mammalian or insect cells but only partial proteolytic processing of the single chain FI precursor occurs under such conditions and only the processed protein has catalytic activity (Nilsson et al, 2007;Ullman et al, 1998;Wong et al, 1995). Mature FI is made up of an unique sequence of domains some of which share sequence similarity with domains found in complement and non-complement proteins.…”
Section: Fimentioning
confidence: 99%
“…Haemolytically inactive C3 (C3u) was prepared by incubating native C3 in 200 mM hydrazine at 37°C for 1 h. 54 Protein concentrations were determined from absorption coefficients of 16.7 for FH, 12 for factor I and 9.4 for C3u (1%; 280 nm; 1 cm path length). 31,55,56 Proteins were dialysed into Hepes buffer for experiments, and their integrity was routinely checked by SDS-PAGE before and after scattering, ultracentrifugation and assays. Fig.…”
Section: Protein Purificationmentioning
confidence: 99%