| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-146 |
Sentence |
denotes |
Endocytosis of alpha 1-acid glycoprotein variants and of neoglycoproteins containing mannose derivatives by a mouse hybridoma cell line (2C11-12). |
| TextSentencer_T2 |
147-192 |
Sentence |
denotes |
Comparison with mouse peritoneal macrophages. |
| TextSentencer_T3 |
193-328 |
Sentence |
denotes |
Macrophages from various origins are known to express membrane lectins that mediate the endocytosis of mannose-bearing glycoconjugates. |
| TextSentencer_T4 |
329-382 |
Sentence |
denotes |
Most macrophage tumor cell-lines lack such receptors. |
| TextSentencer_T5 |
383-675 |
Sentence |
denotes |
In this paper we show by flow cytometry analysis that a newly generated macrophage hybridoma (2C11-12), which displays several macrophage characteristics, also expresses mannose membrane lectins, resulting in the internalization of fluoresceinylated neoglycoproteins into acidic compartments. |
| TextSentencer_T6 |
676-941 |
Sentence |
denotes |
Thioglycolate elicited mouse peritoneal macrophages and the 2C11-12 hybridomas were compared by flow cytometry with regard to the binding and endocytosis of alpha 1-acid glycoprotein (AGP) variants separated by affinity chromatography on immobilized concanavalin A. |
| TextSentencer_T7 |
942-1109 |
Sentence |
denotes |
AGP C eluted specifically with methyl alpha-mannopyranoside, which contains two bi-antennary oligosaccharides, was endocytosed as mannosylated serum albumin (Man-BSA). |
| TextSentencer_T8 |
1110-1296 |
Sentence |
denotes |
In both types of macrophages, the fluoresceinylated ligands were internalized in acidic compartments as demonstrated by the fluorescence intensity increase upon monensin post-incubation. |
| TextSentencer_T9 |
1297-1379 |
Sentence |
denotes |
However the behaviour of the internalized ligands was found to be quite different. |
| TextSentencer_T10 |
1380-1588 |
Sentence |
denotes |
AGP C and Man-BSA were rapidly degraded by thioglycolate elicited peritoneal macrophages and excreted in the medium as small peptide fragments; conversely they remained a longer time in the 2C11-12 hybridoma. |
| T1 |
0-146 |
Sentence |
denotes |
Endocytosis of alpha 1-acid glycoprotein variants and of neoglycoproteins containing mannose derivatives by a mouse hybridoma cell line (2C11-12). |
| T2 |
147-192 |
Sentence |
denotes |
Comparison with mouse peritoneal macrophages. |
| T3 |
193-328 |
Sentence |
denotes |
Macrophages from various origins are known to express membrane lectins that mediate the endocytosis of mannose-bearing glycoconjugates. |
| T4 |
329-382 |
Sentence |
denotes |
Most macrophage tumor cell-lines lack such receptors. |
| T5 |
383-675 |
Sentence |
denotes |
In this paper we show by flow cytometry analysis that a newly generated macrophage hybridoma (2C11-12), which displays several macrophage characteristics, also expresses mannose membrane lectins, resulting in the internalization of fluoresceinylated neoglycoproteins into acidic compartments. |
| T6 |
676-941 |
Sentence |
denotes |
Thioglycolate elicited mouse peritoneal macrophages and the 2C11-12 hybridomas were compared by flow cytometry with regard to the binding and endocytosis of alpha 1-acid glycoprotein (AGP) variants separated by affinity chromatography on immobilized concanavalin A. |
| T7 |
942-1109 |
Sentence |
denotes |
AGP C eluted specifically with methyl alpha-mannopyranoside, which contains two bi-antennary oligosaccharides, was endocytosed as mannosylated serum albumin (Man-BSA). |
| T8 |
1110-1296 |
Sentence |
denotes |
In both types of macrophages, the fluoresceinylated ligands were internalized in acidic compartments as demonstrated by the fluorescence intensity increase upon monensin post-incubation. |
| T9 |
1297-1379 |
Sentence |
denotes |
However the behaviour of the internalized ligands was found to be quite different. |
| T10 |
1380-1588 |
Sentence |
denotes |
AGP C and Man-BSA were rapidly degraded by thioglycolate elicited peritoneal macrophages and excreted in the medium as small peptide fragments; conversely they remained a longer time in the 2C11-12 hybridoma. |
