Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-100 |
Sentence |
denotes |
Comparative proteome analysis of saccular intracranial aneurysms with iTRAQ quantitative proteomics. |
T2 |
101-111 |
Sentence |
denotes |
OBJECTIVE: |
T3 |
112-386 |
Sentence |
denotes |
To screen differentially expressed proteins of saccular intracranial aneurysms and superficial temporal artery by the proteomics analysis using isobaric tags for relative and absolute quantification (iTRAQ) combined with reverse phase high-performance liquid chromatography. |
T4 |
387-395 |
Sentence |
denotes |
METHODS: |
T5 |
396-536 |
Sentence |
denotes |
Collecting 17 samples from intracranial aneurysm patients undergoing aneurysmectomy as experiment group and 17 matched STA as control group. |
T6 |
537-661 |
Sentence |
denotes |
After quantification and enzymolysis of the protein, the iTRAQ were used to label the peptides of the 2 groups respectively. |
T7 |
662-796 |
Sentence |
denotes |
Then, the mixture of the peptides was fractioned by RP-HPLC and analyzed by LC-MS/MS to identify the differential expression proteins. |
T8 |
797-805 |
Sentence |
denotes |
RESULTS: |
T9 |
806-937 |
Sentence |
denotes |
A total of 1699 proteins were identified from the ProteinPilot 4.5 software (AB SCIEX) using the Paragon database search algorithm. |
T10 |
938-1089 |
Sentence |
denotes |
Comparing with STA, 54 proteins were significantly up-regulated (115:114<0.5-fold) and 37 were significantly down-regulated in sIAs (115:114>2.0-fold). |
T11 |
1090-1385 |
Sentence |
denotes |
Furthermore, Integrin β3, Secreted frizzled-related protein 2 were significantly up-regulated (2.3 fold and 2.1 fold, respectively), whereas MyosinIIb, Alpha-actinin-1, Laminin β2, and Carboxypeptidase A3 were down-regulated (3.01 fold, 2.1 fold, 2.07 fold, and 2.01 fold, respectively) in sIAs. |
T12 |
1386-1729 |
Sentence |
denotes |
GO Ontology analysis showed that most differential proteins expressed in cytoskeletal; up-regulated proteins in sIAs play an important role in inflammatory reaction, enzymatic hydrolysis, cell adhesion and invasion, and cellular immune reaction; down-regulated proteins in sIAs involved in cytoskeletal protein, enzyme, and structural protein. |
T13 |
1730-1813 |
Sentence |
denotes |
ITGB3, ACTN1 and MYL2 play a role in aneurysm formation via focal adhesion pathway. |
T14 |
1814-1911 |
Sentence |
denotes |
The results of Western-blot assay were consistent with the proteomic changes of those 6 proteins. |
T15 |
1912-1923 |
Sentence |
denotes |
CONCLUSION: |
T16 |
1924-2071 |
Sentence |
denotes |
The differentially expressed proteins in sIAs that showed aneurysm formation are related to cytoskeleton abnormal and extracellular matrix changes. |
T17 |
2072-2190 |
Sentence |
denotes |
The iTRAQ technology provides scientific foundation for the further study to explore the pathogenic mechanism of sIAs. |
T1 |
0-100 |
Sentence |
denotes |
Comparative proteome analysis of saccular intracranial aneurysms with iTRAQ quantitative proteomics. |
T2 |
101-111 |
Sentence |
denotes |
OBJECTIVE: |
T3 |
112-386 |
Sentence |
denotes |
To screen differentially expressed proteins of saccular intracranial aneurysms and superficial temporal artery by the proteomics analysis using isobaric tags for relative and absolute quantification (iTRAQ) combined with reverse phase high-performance liquid chromatography. |
T4 |
387-395 |
Sentence |
denotes |
METHODS: |
T5 |
396-536 |
Sentence |
denotes |
Collecting 17 samples from intracranial aneurysm patients undergoing aneurysmectomy as experiment group and 17 matched STA as control group. |
T6 |
537-661 |
Sentence |
denotes |
After quantification and enzymolysis of the protein, the iTRAQ were used to label the peptides of the 2 groups respectively. |
T7 |
662-796 |
Sentence |
denotes |
Then, the mixture of the peptides was fractioned by RP-HPLC and analyzed by LC-MS/MS to identify the differential expression proteins. |
T8 |
797-805 |
Sentence |
denotes |
RESULTS: |
T9 |
806-937 |
Sentence |
denotes |
A total of 1699 proteins were identified from the ProteinPilot 4.5 software (AB SCIEX) using the Paragon database search algorithm. |
T10 |
938-1089 |
Sentence |
denotes |
Comparing with STA, 54 proteins were significantly up-regulated (115:114<0.5-fold) and 37 were significantly down-regulated in sIAs (115:114>2.0-fold). |
T11 |
1090-1385 |
Sentence |
denotes |
Furthermore, Integrin β3, Secreted frizzled-related protein 2 were significantly up-regulated (2.3 fold and 2.1 fold, respectively), whereas MyosinIIb, Alpha-actinin-1, Laminin β2, and Carboxypeptidase A3 were down-regulated (3.01 fold, 2.1 fold, 2.07 fold, and 2.01 fold, respectively) in sIAs. |
T12 |
1386-1729 |
Sentence |
denotes |
GO Ontology analysis showed that most differential proteins expressed in cytoskeletal; up-regulated proteins in sIAs play an important role in inflammatory reaction, enzymatic hydrolysis, cell adhesion and invasion, and cellular immune reaction; down-regulated proteins in sIAs involved in cytoskeletal protein, enzyme, and structural protein. |
T13 |
1730-1813 |
Sentence |
denotes |
ITGB3, ACTN1 and MYL2 play a role in aneurysm formation via focal adhesion pathway. |
T14 |
1814-1911 |
Sentence |
denotes |
The results of Western-blot assay were consistent with the proteomic changes of those 6 proteins. |
T15 |
1912-1923 |
Sentence |
denotes |
CONCLUSION: |
T16 |
1924-2071 |
Sentence |
denotes |
The differentially expressed proteins in sIAs that showed aneurysm formation are related to cytoskeleton abnormal and extracellular matrix changes. |
T17 |
2072-2190 |
Sentence |
denotes |
The iTRAQ technology provides scientific foundation for the further study to explore the pathogenic mechanism of sIAs. |