| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-151 |
Sentence |
denotes |
Role of interaction of mannan-binding protein with meprins at the initial step of complement activation in ischemia/reperfusion injury to mouse kidney. |
| T1 |
0-151 |
Sentence |
denotes |
Role of interaction of mannan-binding protein with meprins at the initial step of complement activation in ischemia/reperfusion injury to mouse kidney. |
| T1 |
0-151 |
Sentence |
denotes |
Role of interaction of mannan-binding protein with meprins at the initial step of complement activation in ischemia/reperfusion injury to mouse kidney. |
| TextSentencer_T2 |
152-224 |
Sentence |
denotes |
Ischemia/reperfusion (I/R) is an important cause of acute renal failure. |
| T2 |
152-224 |
Sentence |
denotes |
Ischemia/reperfusion (I/R) is an important cause of acute renal failure. |
| T2 |
152-224 |
Sentence |
denotes |
Ischemia/reperfusion (I/R) is an important cause of acute renal failure. |
| TextSentencer_T3 |
225-491 |
Sentence |
denotes |
Recent studies have shown that the complement system mediated by the mannan-binding protein (MBP), which is a C-type serum lectin recognizing mannose, fucose and N-acetylglucosamine residues, plays a critical role in the pathogenesis of ischemic acute renal failure. |
| T3 |
225-491 |
Sentence |
denotes |
Recent studies have shown that the complement system mediated by the mannan-binding protein (MBP), which is a C-type serum lectin recognizing mannose, fucose and N-acetylglucosamine residues, plays a critical role in the pathogenesis of ischemic acute renal failure. |
| T3 |
225-491 |
Sentence |
denotes |
Recent studies have shown that the complement system mediated by the mannan-binding protein (MBP), which is a C-type serum lectin recognizing mannose, fucose and N-acetylglucosamine residues, plays a critical role in the pathogenesis of ischemic acute renal failure. |
| TextSentencer_T4 |
492-699 |
Sentence |
denotes |
MBP causes complement activation through the MBP lectin pathway and a resulting complement component, C3b, is accumulated on the brush borders of kidney proximal tubules in a renal I/R-operated mouse kidney. |
| T4 |
492-699 |
Sentence |
denotes |
MBP causes complement activation through the MBP lectin pathway and a resulting complement component, C3b, is accumulated on the brush borders of kidney proximal tubules in a renal I/R-operated mouse kidney. |
| T4 |
492-699 |
Sentence |
denotes |
MBP causes complement activation through the MBP lectin pathway and a resulting complement component, C3b, is accumulated on the brush borders of kidney proximal tubules in a renal I/R-operated mouse kidney. |
| TextSentencer_T5 |
700-788 |
Sentence |
denotes |
However, the initial step of the complement activation has not been studied extensively. |
| T5 |
700-788 |
Sentence |
denotes |
However, the initial step of the complement activation has not been studied extensively. |
| T5 |
700-788 |
Sentence |
denotes |
However, the initial step of the complement activation has not been studied extensively. |
| TextSentencer_T6 |
789-942 |
Sentence |
denotes |
We previously identified both meprins α and β, highly glycosylated zinc metalloproteases, localized on kidney proximal tubules as endogenous MBP ligands. |
| T6 |
789-942 |
Sentence |
denotes |
We previously identified both meprins α and β, highly glycosylated zinc metalloproteases, localized on kidney proximal tubules as endogenous MBP ligands. |
| T6 |
789-942 |
Sentence |
denotes |
We previously identified both meprins α and β, highly glycosylated zinc metalloproteases, localized on kidney proximal tubules as endogenous MBP ligands. |
| TextSentencer_T7 |
943-1122 |
Sentence |
denotes |
In the present study, we demonstrated that serum-type MBP (S-MBP) and C3b were co-localized with meprins on both the cortex and the medulla in the renal I/R-operated mouse kidney. |
| T7 |
943-1122 |
Sentence |
denotes |
In the present study, we demonstrated that serum-type MBP (S-MBP) and C3b were co-localized with meprins on both the cortex and the medulla in the renal I/R-operated mouse kidney. |
| T7 |
943-1122 |
Sentence |
denotes |
In the present study, we demonstrated that serum-type MBP (S-MBP) and C3b were co-localized with meprins on both the cortex and the medulla in the renal I/R-operated mouse kidney. |
| TextSentencer_T8 |
1123-1307 |
Sentence |
denotes |
S-MBP was indicated to interact with meprins in vivo in the I/R-operated mouse kidney and was shown to initiate the complement activation through the interaction with meprins in vitro. |
| T8 |
1123-1307 |
Sentence |
denotes |
S-MBP was indicated to interact with meprins in vivo in the I/R-operated mouse kidney and was shown to initiate the complement activation through the interaction with meprins in vitro. |
| T8 |
1123-1307 |
Sentence |
denotes |
S-MBP was indicated to interact with meprins in vivo in the I/R-operated mouse kidney and was shown to initiate the complement activation through the interaction with meprins in vitro. |
| TextSentencer_T9 |
1308-1557 |
Sentence |
denotes |
Taken together, the present study strongly suggested that the binding of S-MBP to meprins triggers the complement activation through the lectin pathway and may cause the acute renal failure due to I/R on kidney transplantation and hemorrhagic shock. |
| T9 |
1308-1557 |
Sentence |
denotes |
Taken together, the present study strongly suggested that the binding of S-MBP to meprins triggers the complement activation through the lectin pathway and may cause the acute renal failure due to I/R on kidney transplantation and hemorrhagic shock. |
| T9 |
1308-1557 |
Sentence |
denotes |
Taken together, the present study strongly suggested that the binding of S-MBP to meprins triggers the complement activation through the lectin pathway and may cause the acute renal failure due to I/R on kidney transplantation and hemorrhagic shock. |