Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-57 |
Sentence |
denotes |
In vivo glycosylation of MUC1 in airway epithelial cells. |
TextSentencer_T2 |
58-257 |
Sentence |
denotes |
The O-glycans that decorate mucin glycoproteins contribute to the biophysical and biochemical properties of these molecules and hence their function as a barrier and lubricant on epithelial surfaces. |
TextSentencer_T3 |
258-343 |
Sentence |
denotes |
Alterations in mucin O-glycosylation in certain diseases may contribute to pathology. |
TextSentencer_T4 |
344-494 |
Sentence |
denotes |
It is known that both the host cell type and the amino acid sequence of the mucin tandem repeat contribute to the O-glycosylation of a mucin molecule. |
TextSentencer_T5 |
495-773 |
Sentence |
denotes |
We expressed an epitope-tagged MUC1 mucin cDNA construct in the airway cell line 16HBE14o- and the colon carcinoma cell line Caco2 and used Fast Atom Bombardment Mass Spectrometry to evaluate the contribution of the host cell to differences in O-glycosylation of a single mucin. |
TextSentencer_T6 |
774-905 |
Sentence |
denotes |
Many of the glycans detected on the MUC1 mucin were common to both cell types, as would be predicted from biosynthetic constraints. |
TextSentencer_T7 |
906-1115 |
Sentence |
denotes |
However, MUC1 synthesized in the airway cell line showed comparatively low levels of sialylation but carried a range of oligo-N-acetyllactosamine structures that were not seen in the colon carcinoma cell line. |
T1 |
0-57 |
Sentence |
denotes |
In vivo glycosylation of MUC1 in airway epithelial cells. |
T2 |
58-257 |
Sentence |
denotes |
The O-glycans that decorate mucin glycoproteins contribute to the biophysical and biochemical properties of these molecules and hence their function as a barrier and lubricant on epithelial surfaces. |
T3 |
258-343 |
Sentence |
denotes |
Alterations in mucin O-glycosylation in certain diseases may contribute to pathology. |
T4 |
344-494 |
Sentence |
denotes |
It is known that both the host cell type and the amino acid sequence of the mucin tandem repeat contribute to the O-glycosylation of a mucin molecule. |
T5 |
495-773 |
Sentence |
denotes |
We expressed an epitope-tagged MUC1 mucin cDNA construct in the airway cell line 16HBE14o- and the colon carcinoma cell line Caco2 and used Fast Atom Bombardment Mass Spectrometry to evaluate the contribution of the host cell to differences in O-glycosylation of a single mucin. |
T6 |
774-905 |
Sentence |
denotes |
Many of the glycans detected on the MUC1 mucin were common to both cell types, as would be predicted from biosynthetic constraints. |
T7 |
906-1115 |
Sentence |
denotes |
However, MUC1 synthesized in the airway cell line showed comparatively low levels of sialylation but carried a range of oligo-N-acetyllactosamine structures that were not seen in the colon carcinoma cell line. |