PubMed:12732622
Annnotations
sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 0-132 | Sentence | denotes | Prion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support S-nitroso-dependent autocleavage of glypican-1 heparan sulfate. |
| T2 | 133-218 | Sentence | denotes | Copper are generally bound to proteins, e.g. the prion and the amyloid beta proteins. |
| T3 | 219-380 | Sentence | denotes | We have previously shown that copper ions are required to nitrosylate thiol groups in the core protein of glypican-1, a heparan sulfate-substituted proteoglycan. |
| T4 | 381-643 | Sentence | denotes | When S-nitrosylated glypican-1 is then exposed to an appropriate reducing agent, such as ascorbate, nitric oxide is released and autocatalyzes deaminative cleavage of the glypican-1 heparan sulfate side chains at sites where the glucosamines are N-unsubstituted. |
| T5 | 644-814 | Sentence | denotes | These processes take place in a stepwise manner, whereas glypican-1 recycles via a caveolin-1-associated pathway where copper ions could be provided by the prion protein. |
| T6 | 815-1536 | Sentence | denotes | Here we show, by using both biochemical and microscopic techniques, that (a) the glypican-1 core protein binds copper(II) ions, reduces them to copper(I) when the thiols are nitrosylated and reoxidizes copper(I) to copper(II) when ascorbate releases nitric oxide; (b) maximally S-nitrosylated glypican-1 can cleave its own heparan sulfate chains at all available sites in a nitroxyl ion-dependent reaction; (c) free zinc(II) ions, which are redox inert, also support autocleavage of glypican-1 heparan sulfate, probably via transnitrosation, whereas they inhibit copper(II)-supported degradation; and (d) copper(II)-loaded but not zinc(II)-loaded prion protein or amyloid beta peptide support heparan sulfate degradation. |
| T7 | 1537-1835 | Sentence | denotes | As glypican-1 in prion null cells is poorly S-nitrosylated and as ectopic expression of cellular prion protein restores S-nitrosylation of glypican-1 in these cells, we propose that one function of the cellular prion protein is to deliver copper(II) for the S-nitrosylation of recycling glypican-1. |
Glycosmos6-GlycoEpitope
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 116-131 | http://www.glycoepitope.jp/epitopes/EP0086 | denotes | heparan sulfate |
| T2 | 339-354 | http://www.glycoepitope.jp/epitopes/EP0086 | denotes | heparan sulfate |
| T3 | 563-578 | http://www.glycoepitope.jp/epitopes/EP0086 | denotes | heparan sulfate |
| T4 | 1138-1153 | http://www.glycoepitope.jp/epitopes/EP0086 | denotes | heparan sulfate |
| T5 | 1309-1324 | http://www.glycoepitope.jp/epitopes/EP0086 | denotes | heparan sulfate |
| T6 | 1508-1523 | http://www.glycoepitope.jp/epitopes/EP0086 | denotes | heparan sulfate |
mondo_disease
| Id | Subject | Object | Predicate | Lexical cue | mondo_id |
|---|---|---|---|---|---|
| T1 | 7-14 | Disease | denotes | amyloid | http://purl.obolibrary.org/obo/MONDO_0019065 |
| T2 | 196-203 | Disease | denotes | amyloid | http://purl.obolibrary.org/obo/MONDO_0019065 |
| T3 | 1479-1486 | Disease | denotes | amyloid | http://purl.obolibrary.org/obo/MONDO_0019065 |
GlyCosmos15-Sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 0-132 | Sentence | denotes | Prion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support S-nitroso-dependent autocleavage of glypican-1 heparan sulfate. |
| T2 | 133-218 | Sentence | denotes | Copper are generally bound to proteins, e.g. the prion and the amyloid beta proteins. |
| T3 | 219-380 | Sentence | denotes | We have previously shown that copper ions are required to nitrosylate thiol groups in the core protein of glypican-1, a heparan sulfate-substituted proteoglycan. |
| T4 | 381-643 | Sentence | denotes | When S-nitrosylated glypican-1 is then exposed to an appropriate reducing agent, such as ascorbate, nitric oxide is released and autocatalyzes deaminative cleavage of the glypican-1 heparan sulfate side chains at sites where the glucosamines are N-unsubstituted. |
| T5 | 644-814 | Sentence | denotes | These processes take place in a stepwise manner, whereas glypican-1 recycles via a caveolin-1-associated pathway where copper ions could be provided by the prion protein. |
| T6 | 815-1536 | Sentence | denotes | Here we show, by using both biochemical and microscopic techniques, that (a) the glypican-1 core protein binds copper(II) ions, reduces them to copper(I) when the thiols are nitrosylated and reoxidizes copper(I) to copper(II) when ascorbate releases nitric oxide; (b) maximally S-nitrosylated glypican-1 can cleave its own heparan sulfate chains at all available sites in a nitroxyl ion-dependent reaction; (c) free zinc(II) ions, which are redox inert, also support autocleavage of glypican-1 heparan sulfate, probably via transnitrosation, whereas they inhibit copper(II)-supported degradation; and (d) copper(II)-loaded but not zinc(II)-loaded prion protein or amyloid beta peptide support heparan sulfate degradation. |
| T7 | 1537-1835 | Sentence | denotes | As glypican-1 in prion null cells is poorly S-nitrosylated and as ectopic expression of cellular prion protein restores S-nitrosylation of glypican-1 in these cells, we propose that one function of the cellular prion protein is to deliver copper(II) for the S-nitrosylation of recycling glypican-1. |
GlyCosmos15-MONDO
| Id | Subject | Object | Predicate | Lexical cue | mondo_id |
|---|---|---|---|---|---|
| T1 | 7-14 | Disease | denotes | amyloid | MONDO:0019065 |
| T2 | 196-203 | Disease | denotes | amyloid | MONDO:0019065 |
| T3 | 1479-1486 | Disease | denotes | amyloid | MONDO:0019065 |
GlyCosmos15-GlycoEpitope
| Id | Subject | Object | Predicate | Lexical cue | glycoepitope_id |
|---|---|---|---|---|---|
| T1 | 116-131 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | heparan sulfate | http://www.glycoepitope.jp/epitopes/EP0086 |
| T2 | 339-354 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | heparan sulfate | http://www.glycoepitope.jp/epitopes/EP0086 |
| T3 | 563-578 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | heparan sulfate | http://www.glycoepitope.jp/epitopes/EP0086 |
| T4 | 1138-1153 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | heparan sulfate | http://www.glycoepitope.jp/epitopes/EP0086 |
| T5 | 1309-1324 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | heparan sulfate | http://www.glycoepitope.jp/epitopes/EP0086 |
| T6 | 1508-1523 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | heparan sulfate | http://www.glycoepitope.jp/epitopes/EP0086 |
CL-cell
| Id | Subject | Object | Predicate | Lexical cue | cl_id |
|---|---|---|---|---|---|
| T1 | 1560-1570 | Cell | denotes | null cells | http://purl.obolibrary.org/obo/CL:0000623|http://purl.obolibrary.org/obo/CL:0000825 |