Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-137 |
Sentence |
denotes |
The natural mutation Y248C of human angiotensinogen leads to abnormal glycosylation and altered immunological recognition of the protein. |
T2 |
138-237 |
Sentence |
denotes |
Common molecular variants of the angiotensinogen gene have been associated with human hypertension. |
T3 |
238-337 |
Sentence |
denotes |
The rare Tyr to Cys change at residue 248 of mature angiotensinogen was identified in one pedigree. |
T4 |
338-487 |
Sentence |
denotes |
Heterozygous individuals (Y248C) had a 40% decrease in plasma angiotensinogen concentration and a 35% reduction of the angiotensin I production rate. |
T5 |
488-603 |
Sentence |
denotes |
Recombinant wild-type (Tyr-248) and mutant (Cys-248) proteins were stably expressed in Chinese hamster ovary cells. |
T6 |
604-796 |
Sentence |
denotes |
Angiotensinogen monoclonal antibodies revealed marked differences in the epitope recognition of the mutant protein and allowed the demonstration of its presence in plasma of Y248C individuals. |
T7 |
797-900 |
Sentence |
denotes |
Similar kinetic constants of angiotensin I production with human renin were observed for both proteins. |
T8 |
901-1061 |
Sentence |
denotes |
Western blot analysis showed similar heterogeneities; however, a 3-kDa increase in molecular mass for the Cys-248 protein was observed after immunopurification. |
T9 |
1062-1267 |
Sentence |
denotes |
Metabolic labeling of the intracellular Cys-248 protein showed a 61-kDa band in addition to the 55.5- and 58-kDa bands observed for the Tyr-248 protein, with all bands being sensitive to endoglycosidase H. |
T10 |
1268-1368 |
Sentence |
denotes |
In addition, pulse-chase studies revealed a slower intracellular processing for the Cys-248 protein. |
T11 |
1369-1600 |
Sentence |
denotes |
In conclusion, the Cys-248 mutation alters the structure, glycosylation, and secretion of angiotensinogen in Chinese hamster ovary cells and is accompanied by a decrease in plasma angiotensinogen concentration in Y248C individuals. |
T1 |
0-137 |
Sentence |
denotes |
The natural mutation Y248C of human angiotensinogen leads to abnormal glycosylation and altered immunological recognition of the protein. |
T2 |
138-237 |
Sentence |
denotes |
Common molecular variants of the angiotensinogen gene have been associated with human hypertension. |
T3 |
238-337 |
Sentence |
denotes |
The rare Tyr to Cys change at residue 248 of mature angiotensinogen was identified in one pedigree. |
T4 |
338-487 |
Sentence |
denotes |
Heterozygous individuals (Y248C) had a 40% decrease in plasma angiotensinogen concentration and a 35% reduction of the angiotensin I production rate. |
T5 |
488-603 |
Sentence |
denotes |
Recombinant wild-type (Tyr-248) and mutant (Cys-248) proteins were stably expressed in Chinese hamster ovary cells. |
T6 |
604-796 |
Sentence |
denotes |
Angiotensinogen monoclonal antibodies revealed marked differences in the epitope recognition of the mutant protein and allowed the demonstration of its presence in plasma of Y248C individuals. |
T7 |
797-900 |
Sentence |
denotes |
Similar kinetic constants of angiotensin I production with human renin were observed for both proteins. |
T8 |
901-1061 |
Sentence |
denotes |
Western blot analysis showed similar heterogeneities; however, a 3-kDa increase in molecular mass for the Cys-248 protein was observed after immunopurification. |
T9 |
1062-1267 |
Sentence |
denotes |
Metabolic labeling of the intracellular Cys-248 protein showed a 61-kDa band in addition to the 55.5- and 58-kDa bands observed for the Tyr-248 protein, with all bands being sensitive to endoglycosidase H. |
T10 |
1268-1368 |
Sentence |
denotes |
In addition, pulse-chase studies revealed a slower intracellular processing for the Cys-248 protein. |
T11 |
1369-1600 |
Sentence |
denotes |
In conclusion, the Cys-248 mutation alters the structure, glycosylation, and secretion of angiotensinogen in Chinese hamster ovary cells and is accompanied by a decrease in plasma angiotensinogen concentration in Y248C individuals. |