PubMed:12421953 JSONTXT

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    FSU-PRGE

    {"project":"FSU-PRGE","denotations":[{"id":"T1","span":{"begin":44,"end":57},"obj":"protein"},{"id":"T2","span":{"begin":62,"end":120},"obj":"protein"},{"id":"T3","span":{"begin":122,"end":130},"obj":"protein"},{"id":"T4","span":{"begin":146,"end":153},"obj":"protein"},{"id":"T5","span":{"begin":167,"end":175},"obj":"protein"},{"id":"T6","span":{"begin":187,"end":197},"obj":"protein"},{"id":"T7","span":{"begin":298,"end":311},"obj":"protein"},{"id":"T8","span":{"begin":328,"end":383},"obj":"protein"},{"id":"T9","span":{"begin":385,"end":398},"obj":"protein"},{"id":"T10","span":{"begin":404,"end":429},"obj":"protein"},{"id":"T11","span":{"begin":431,"end":436},"obj":"protein"},{"id":"T12","span":{"begin":572,"end":585},"obj":"protein"},{"id":"T13","span":{"begin":657,"end":660},"obj":"protein"},{"id":"T14","span":{"begin":661,"end":664},"obj":"protein"},{"id":"T15","span":{"begin":666,"end":670},"obj":"protein"},{"id":"T16","span":{"begin":676,"end":704},"obj":"protein"},{"id":"T17","span":{"begin":706,"end":729},"obj":"protein"},{"id":"T18","span":{"begin":731,"end":734},"obj":"protein"},{"id":"T19","span":{"begin":750,"end":753},"obj":"protein"},{"id":"T20","span":{"begin":768,"end":773},"obj":"protein"},{"id":"T21","span":{"begin":794,"end":807},"obj":"protein"},{"id":"T22","span":{"begin":897,"end":906},"obj":"protein"},{"id":"T23","span":{"begin":922,"end":925},"obj":"protein"},{"id":"T24","span":{"begin":959,"end":965},"obj":"protein"},{"id":"T25","span":{"begin":989,"end":995},"obj":"protein"},{"id":"T26","span":{"begin":1061,"end":1064},"obj":"protein"},{"id":"T27","span":{"begin":1103,"end":1109},"obj":"protein"},{"id":"T28","span":{"begin":1111,"end":1117},"obj":"protein"},{"id":"T29","span":{"begin":1123,"end":1128},"obj":"protein"},{"id":"T30","span":{"begin":1229,"end":1232},"obj":"protein"},{"id":"T31","span":{"begin":1305,"end":1311},"obj":"protein"},{"id":"T32","span":{"begin":1313,"end":1319},"obj":"protein"},{"id":"T33","span":{"begin":1325,"end":1331},"obj":"protein"},{"id":"T34","span":{"begin":1337,"end":1340},"obj":"protein"},{"id":"T35","span":{"begin":1421,"end":1427},"obj":"protein"},{"id":"T36","span":{"begin":1432,"end":1438},"obj":"protein"},{"id":"T37","span":{"begin":1489,"end":1492},"obj":"protein"},{"id":"T38","span":{"begin":1547,"end":1550},"obj":"protein"},{"id":"T39","span":{"begin":1645,"end":1648},"obj":"protein"},{"id":"T40","span":{"begin":1682,"end":1685},"obj":"protein"},{"id":"T41","span":{"begin":1690,"end":1703},"obj":"protein"},{"id":"T42","span":{"begin":1772,"end":1777},"obj":"protein"},{"id":"T43","span":{"begin":1800,"end":1805},"obj":"protein"},{"id":"T44","span":{"begin":1819,"end":1822},"obj":"protein"},{"id":"T45","span":{"begin":1867,"end":1880},"obj":"protein"},{"id":"T46","span":{"begin":1920,"end":1927},"obj":"protein"},{"id":"T47","span":{"begin":1971,"end":1976},"obj":"protein"}],"text":"Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2.\nFicolins are oligomeric lectins comprising a collagen-like and a fibrinogen-like domain, with a binding specificity for N-acetylglucosamine. It has been reported recently that L-ficolin/P35 associates with mannan-binding lectin (MBL)-associated serine proteases (MASP-1 and -2) and MBL-associated protein 19 (MAp19) in serum and forms complexes able to activate complement. Using surface plasmon resonance spectroscopy we have shown that recombinant MASP-1 and -2, their N-terminal CUB1 (module originally found in complement proteins C1r/C1s, Uegf, and bone morphogenetic protein-1)-epidermal growth factor (EGF)-CUB2 and CUB1-EGF segments, and MAp19 bind to immobilized L-ficolin/P35 in the presence of Ca(2+) ions. Comparable K(d) values were obtained for the full-length proteases and their CUB1-EGF-CUB2 segments (9.2 and 10 nM for MASP-1 and 4.6 and 5.4 nM for MASP-2, respectively), whereas higher values were obtained for the CUB1-EGF segments (26.7, 15.6, and 14.3 nM for MASP-1, MASP-2, and MAp19). These values are in the same range as those determined for the interaction of these proteins with MBL. Binding was Ca(2+) dependent and was only partly sensitive to EDTA for MASP-1, MASP-2, and MASP-2 CUB1-EGF-CUB2. Half-maximal binding was obtained at comparable Ca(2+) concentrations for MASP-1 and MASP-2 (0.45 and 0.47 micro M, respectively), their CUB1-EGF-CUB2 segments (0.37 and 0.72 micro M), and their CUB1-EGF segments (0.31 and 0.79 micro M). These values are lower than those determined in the case of MBL, indicating a difference between MBL and L-ficolin/P35 with respect to the Ca(2+) dependence of their interaction with the MASPs. Preincubation of the MASPs with soluble MBL inhibited subsequent binding to immobilized L-ficolin/P35 and, conversely, suggesting that these lectins compete with each other for binding to the MASPs in vivo."}

    PIR-corpus2

    {"project":"PIR-corpus2","denotations":[{"id":"T1","span":{"begin":44,"end":53},"obj":"protein"},{"id":"T2","span":{"begin":54,"end":57},"obj":"protein"},{"id":"T3","span":{"begin":62,"end":113},"obj":"protein"},{"id":"T4","span":{"begin":122,"end":130},"obj":"protein"},{"id":"T5","span":{"begin":135,"end":153},"obj":"protein"},{"id":"T6","span":{"begin":167,"end":175},"obj":"protein"},{"id":"T7","span":{"begin":187,"end":197},"obj":"protein"},{"id":"T8","span":{"begin":298,"end":307},"obj":"protein"},{"id":"T9","span":{"begin":308,"end":311},"obj":"protein"},{"id":"T10","span":{"begin":328,"end":383},"obj":"protein"},{"id":"T11","span":{"begin":385,"end":391},"obj":"protein"},{"id":"T12","span":{"begin":404,"end":437},"obj":"protein"},{"id":"T13","span":{"begin":484,"end":494},"obj":"protein"},{"id":"T14","span":{"begin":572,"end":578},"obj":"protein"},{"id":"T15","span":{"begin":637,"end":660},"obj":"protein"},{"id":"T16","span":{"begin":661,"end":664},"obj":"protein"},{"id":"T17","span":{"begin":666,"end":670},"obj":"protein"},{"id":"T18","span":{"begin":676,"end":704},"obj":"protein"},{"id":"T19","span":{"begin":706,"end":735},"obj":"protein"},{"id":"T20","span":{"begin":750,"end":753},"obj":"protein"},{"id":"T21","span":{"begin":768,"end":773},"obj":"protein"},{"id":"T22","span":{"begin":796,"end":803},"obj":"protein"},{"id":"T23","span":{"begin":804,"end":807},"obj":"protein"},{"id":"T24","span":{"begin":897,"end":906},"obj":"protein"},{"id":"T25","span":{"begin":922,"end":925},"obj":"protein"},{"id":"T26","span":{"begin":959,"end":965},"obj":"protein"},{"id":"T27","span":{"begin":989,"end":995},"obj":"protein"},{"id":"T28","span":{"begin":1061,"end":1064},"obj":"protein"},{"id":"T29","span":{"begin":1103,"end":1109},"obj":"protein"},{"id":"T30","span":{"begin":1111,"end":1117},"obj":"protein"},{"id":"T31","span":{"begin":1123,"end":1128},"obj":"protein"},{"id":"T32","span":{"begin":1229,"end":1232},"obj":"protein"},{"id":"T33","span":{"begin":1305,"end":1311},"obj":"protein"},{"id":"T34","span":{"begin":1313,"end":1319},"obj":"protein"},{"id":"T35","span":{"begin":1325,"end":1331},"obj":"protein"},{"id":"T36","span":{"begin":1337,"end":1340},"obj":"protein"},{"id":"T37","span":{"begin":1421,"end":1427},"obj":"protein"},{"id":"T38","span":{"begin":1432,"end":1438},"obj":"protein"},{"id":"T39","span":{"begin":1489,"end":1492},"obj":"protein"},{"id":"T40","span":{"begin":1547,"end":1550},"obj":"protein"},{"id":"T41","span":{"begin":1645,"end":1648},"obj":"protein"},{"id":"T42","span":{"begin":1682,"end":1685},"obj":"protein"},{"id":"T43","span":{"begin":1690,"end":1699},"obj":"protein"},{"id":"T44","span":{"begin":1700,"end":1703},"obj":"protein"},{"id":"T45","span":{"begin":1772,"end":1777},"obj":"protein"},{"id":"T46","span":{"begin":1800,"end":1805},"obj":"protein"},{"id":"T47","span":{"begin":1819,"end":1822},"obj":"protein"},{"id":"T48","span":{"begin":1867,"end":1876},"obj":"protein"},{"id":"T49","span":{"begin":1877,"end":1880},"obj":"protein"},{"id":"T50","span":{"begin":1920,"end":1927},"obj":"protein"},{"id":"T51","span":{"begin":1971,"end":1976},"obj":"protein"},{"id":"T54","span":{"begin":62,"end":120},"obj":"long_form"},{"id":"T64","span":{"begin":572,"end":585},"obj":"long_form"}],"text":"Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2.\nFicolins are oligomeric lectins comprising a collagen-like and a fibrinogen-like domain, with a binding specificity for N-acetylglucosamine. It has been reported recently that L-ficolin/P35 associates with mannan-binding lectin (MBL)-associated serine proteases (MASP-1 and -2) and MBL-associated protein 19 (MAp19) in serum and forms complexes able to activate complement. Using surface plasmon resonance spectroscopy we have shown that recombinant MASP-1 and -2, their N-terminal CUB1 (module originally found in complement proteins C1r/C1s, Uegf, and bone morphogenetic protein-1)-epidermal growth factor (EGF)-CUB2 and CUB1-EGF segments, and MAp19 bind to immobilized L-ficolin/P35 in the presence of Ca(2+) ions. Comparable K(d) values were obtained for the full-length proteases and their CUB1-EGF-CUB2 segments (9.2 and 10 nM for MASP-1 and 4.6 and 5.4 nM for MASP-2, respectively), whereas higher values were obtained for the CUB1-EGF segments (26.7, 15.6, and 14.3 nM for MASP-1, MASP-2, and MAp19). These values are in the same range as those determined for the interaction of these proteins with MBL. Binding was Ca(2+) dependent and was only partly sensitive to EDTA for MASP-1, MASP-2, and MASP-2 CUB1-EGF-CUB2. Half-maximal binding was obtained at comparable Ca(2+) concentrations for MASP-1 and MASP-2 (0.45 and 0.47 micro M, respectively), their CUB1-EGF-CUB2 segments (0.37 and 0.72 micro M), and their CUB1-EGF segments (0.31 and 0.79 micro M). These values are lower than those determined in the case of MBL, indicating a difference between MBL and L-ficolin/P35 with respect to the Ca(2+) dependence of their interaction with the MASPs. Preincubation of the MASPs with soluble MBL inhibited subsequent binding to immobilized L-ficolin/P35 and, conversely, suggesting that these lectins compete with each other for binding to the MASPs in vivo."}

    PIR-corpus1

    {"project":"PIR-corpus1","denotations":[{"id":"T1","span":{"begin":44,"end":57},"obj":"protein"},{"id":"T2","span":{"begin":62,"end":120},"obj":"compound-protein"},{"id":"T3","span":{"begin":122,"end":130},"obj":"protein"},{"id":"T4","span":{"begin":146,"end":153},"obj":"protein"},{"id":"T5","span":{"begin":298,"end":311},"obj":"protein"},{"id":"T6","span":{"begin":328,"end":383},"obj":"protein"},{"id":"T7","span":{"begin":385,"end":398},"obj":"compound-protein"},{"id":"T8","span":{"begin":404,"end":429},"obj":"protein"},{"id":"T9","span":{"begin":431,"end":436},"obj":"acronym"},{"id":"T10","span":{"begin":457,"end":466},"obj":"protein"},{"id":"T11","span":{"begin":572,"end":585},"obj":"compound-protein"},{"id":"T12","span":{"begin":637,"end":656},"obj":"protein"},{"id":"T13","span":{"begin":657,"end":664},"obj":"protein"},{"id":"T14","span":{"begin":666,"end":670},"obj":"protein"},{"id":"T15","span":{"begin":676,"end":704},"obj":"protein"},{"id":"T16","span":{"begin":768,"end":773},"obj":"protein"},{"id":"T17","span":{"begin":794,"end":807},"obj":"protein"},{"id":"T18","span":{"begin":897,"end":906},"obj":"protein"},{"id":"T19","span":{"begin":959,"end":965},"obj":"protein"},{"id":"T20","span":{"begin":989,"end":995},"obj":"protein"},{"id":"T21","span":{"begin":1103,"end":1109},"obj":"protein"},{"id":"T22","span":{"begin":1111,"end":1117},"obj":"protein"},{"id":"T23","span":{"begin":1123,"end":1128},"obj":"protein"},{"id":"T24","span":{"begin":1215,"end":1223},"obj":"protein"},{"id":"T25","span":{"begin":1421,"end":1427},"obj":"protein"},{"id":"T26","span":{"begin":1432,"end":1438},"obj":"protein"},{"id":"T27","span":{"begin":1690,"end":1703},"obj":"protein"},{"id":"T28","span":{"begin":1772,"end":1777},"obj":"protein"},{"id":"T29","span":{"begin":1800,"end":1805},"obj":"protein"},{"id":"T30","span":{"begin":1867,"end":1880},"obj":"protein"},{"id":"T31","span":{"begin":1920,"end":1927},"obj":"protein"},{"id":"T32","span":{"begin":1971,"end":1976},"obj":"protein"}],"text":"Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2.\nFicolins are oligomeric lectins comprising a collagen-like and a fibrinogen-like domain, with a binding specificity for N-acetylglucosamine. It has been reported recently that L-ficolin/P35 associates with mannan-binding lectin (MBL)-associated serine proteases (MASP-1 and -2) and MBL-associated protein 19 (MAp19) in serum and forms complexes able to activate complement. Using surface plasmon resonance spectroscopy we have shown that recombinant MASP-1 and -2, their N-terminal CUB1 (module originally found in complement proteins C1r/C1s, Uegf, and bone morphogenetic protein-1)-epidermal growth factor (EGF)-CUB2 and CUB1-EGF segments, and MAp19 bind to immobilized L-ficolin/P35 in the presence of Ca(2+) ions. Comparable K(d) values were obtained for the full-length proteases and their CUB1-EGF-CUB2 segments (9.2 and 10 nM for MASP-1 and 4.6 and 5.4 nM for MASP-2, respectively), whereas higher values were obtained for the CUB1-EGF segments (26.7, 15.6, and 14.3 nM for MASP-1, MASP-2, and MAp19). These values are in the same range as those determined for the interaction of these proteins with MBL. Binding was Ca(2+) dependent and was only partly sensitive to EDTA for MASP-1, MASP-2, and MASP-2 CUB1-EGF-CUB2. Half-maximal binding was obtained at comparable Ca(2+) concentrations for MASP-1 and MASP-2 (0.45 and 0.47 micro M, respectively), their CUB1-EGF-CUB2 segments (0.37 and 0.72 micro M), and their CUB1-EGF segments (0.31 and 0.79 micro M). These values are lower than those determined in the case of MBL, indicating a difference between MBL and L-ficolin/P35 with respect to the Ca(2+) dependence of their interaction with the MASPs. Preincubation of the MASPs with soluble MBL inhibited subsequent binding to immobilized L-ficolin/P35 and, conversely, suggesting that these lectins compete with each other for binding to the MASPs in vivo."}