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Inflammaging

Id Subject Object Predicate Lexical cue
T1 0-111 Sentence denotes Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
T2 112-250 Sentence denotes We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
T3 251-654 Sentence denotes Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
T4 655-813 Sentence denotes Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation.
T5 814-1005 Sentence denotes FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
T6 1006-1080 Sentence denotes Western blot analysis indicated that both N-linked sites are glycosylated.
T7 1081-1195 Sentence denotes In functional studies, hPAR(2)N30A displayed a selective and significant increase in sensitivity towards tryptase.
T8 1196-1291 Sentence denotes Interestingly, hPAR(2)N222A displayed a loss in sensitivity towards all PAR(2) agonists tested.
T9 1292-1757 Sentence denotes However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists. hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
T10 1758-1991 Sentence denotes Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
T11 1992-2104 Sentence denotes We conclude that hPAR(2) N-linked glycosylation and sialylation regulates receptor expression and/or signalling.
T1 0-111 Sentence denotes Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
T2 112-250 Sentence denotes We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
T3 251-654 Sentence denotes Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
T4 655-813 Sentence denotes Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation.
T5 814-1005 Sentence denotes FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
T6 1006-1080 Sentence denotes Western blot analysis indicated that both N-linked sites are glycosylated.
T7 1081-1195 Sentence denotes In functional studies, hPAR(2)N30A displayed a selective and significant increase in sensitivity towards tryptase.
T8 1196-1291 Sentence denotes Interestingly, hPAR(2)N222A displayed a loss in sensitivity towards all PAR(2) agonists tested.
T9 1292-1757 Sentence denotes However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists. hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
T10 1758-1991 Sentence denotes Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
T11 1992-2104 Sentence denotes We conclude that hPAR(2) N-linked glycosylation and sialylation regulates receptor expression and/or signalling.

bionlp-st-epi-2011-training

Id Subject Object Predicate Lexical cue
T1 23-54 Protein denotes proteinase-activated receptor-2
T2 57-61 Protein denotes PAR2
T3 184-215 Protein denotes proteinase-activated receptor-2
T4 218-224 Protein denotes PAR(2)
T5 277-283 Protein denotes PAR(2)
T6 289-295 Protein denotes PAR(2)
T7 301-307 Protein denotes PAR(2)
T8 407-413 Protein denotes PAR(2)
T9 465-471 Protein denotes PAR(2)
T10 498-504 Protein denotes PAR(2)
T11 538-544 Protein denotes PAR(2)
T12 559-565 Protein denotes PAR(2)
T13 684-690 Protein denotes PAR(2)
T14 709-715 Protein denotes PAR(2)
T15 780-796 Protein denotes N -glycosidase F
T16 863-869 Protein denotes PAR(2)
T17 874-880 Protein denotes PAR(2)
T18 973-979 Protein denotes PAR(2)
T19 1105-1111 Protein denotes PAR(2)
T20 1212-1218 Protein denotes PAR(2)
T21 1268-1274 Protein denotes PAR(2)
T22 1424-1430 Protein denotes PAR(2)
T23 1471-1477 Protein denotes PAR(2)
T24 1489-1495 Protein denotes PAR(2)
T25 1807-1813 Protein denotes PAR(2)
T26 2010-2016 Protein denotes PAR(2)