Pub. Date : 2022 Apr 13
PMID : 35418571
14 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | In this study, we show that the lipophilic cyclic peptide, cyclosporin A (CsA), interacted with, and likely induced aggregation, of polymeric, gel-forming mucins (MUC2, MUC5AC and MUC5B) which underpin the mucus gel-networks in the gastrointestinal tract. | Cyclosporine | mucin 2, oligomeric mucus/gel-forming | Homo sapiens |
| 2 | In this study, we show that the lipophilic cyclic peptide, cyclosporin A (CsA), interacted with, and likely induced aggregation, of polymeric, gel-forming mucins (MUC2, MUC5AC and MUC5B) which underpin the mucus gel-networks in the gastrointestinal tract. | Cyclosporine | mucin 5AC, oligomeric mucus/gel-forming | Homo sapiens |
| 3 | In this study, we show that the lipophilic cyclic peptide, cyclosporin A (CsA), interacted with, and likely induced aggregation, of polymeric, gel-forming mucins (MUC2, MUC5AC and MUC5B) which underpin the mucus gel-networks in the gastrointestinal tract. | Cyclosporine | mucin 5B, oligomeric mucus/gel-forming | Homo sapiens |
| 4 | Using rate-zonal centrifugation, purified MUC2, MUC5AC and MUC5B mucins sedimented faster in the presence of CsA, with a significant increase in mucins in the pellet fraction. | Cyclosporine | mucin 2, oligomeric mucus/gel-forming | Homo sapiens |
| 5 | Using rate-zonal centrifugation, purified MUC2, MUC5AC and MUC5B mucins sedimented faster in the presence of CsA, with a significant increase in mucins in the pellet fraction. | Cyclosporine | mucin 5AC, oligomeric mucus/gel-forming | Homo sapiens |
| 6 | Using rate-zonal centrifugation, purified MUC2, MUC5AC and MUC5B mucins sedimented faster in the presence of CsA, with a significant increase in mucins in the pellet fraction. | Cyclosporine | mucin 5B, oligomeric mucus/gel-forming | Homo sapiens |
| 7 | CsA increased MUC5B sedimentation was concentration-dependent, and sedimentation studies using recombinant mucin protein domains suggests CsA most likely causes aggregation of the relatively non-O-glycosylated N-terminal and C-terminal regions of MUC5B. | Cyclosporine | mucin 5B, oligomeric mucus/gel-forming | Homo sapiens |
| 8 | CsA increased MUC5B sedimentation was concentration-dependent, and sedimentation studies using recombinant mucin protein domains suggests CsA most likely causes aggregation of the relatively non-O-glycosylated N-terminal and C-terminal regions of MUC5B. | Cyclosporine | LOC100508689 | Homo sapiens |
| 9 | CsA increased MUC5B sedimentation was concentration-dependent, and sedimentation studies using recombinant mucin protein domains suggests CsA most likely causes aggregation of the relatively non-O-glycosylated N-terminal and C-terminal regions of MUC5B. | Cyclosporine | mucin 5B, oligomeric mucus/gel-forming | Homo sapiens |
| 10 | CsA increased MUC5B sedimentation was concentration-dependent, and sedimentation studies using recombinant mucin protein domains suggests CsA most likely causes aggregation of the relatively non-O-glycosylated N-terminal and C-terminal regions of MUC5B. | Cyclosporine | mucin 5B, oligomeric mucus/gel-forming | Homo sapiens |
| 11 | CsA increased MUC5B sedimentation was concentration-dependent, and sedimentation studies using recombinant mucin protein domains suggests CsA most likely causes aggregation of the relatively non-O-glycosylated N-terminal and C-terminal regions of MUC5B. | Cyclosporine | LOC100508689 | Homo sapiens |
| 12 | CsA increased MUC5B sedimentation was concentration-dependent, and sedimentation studies using recombinant mucin protein domains suggests CsA most likely causes aggregation of the relatively non-O-glycosylated N-terminal and C-terminal regions of MUC5B. | Cyclosporine | mucin 5B, oligomeric mucus/gel-forming | Homo sapiens |
| 13 | CsA has partially N-methylated amide groups, this unique molecular structure, not present in daptomycin and polymyxin B, may potentially be involved in interaction with gel-forming mucin. | Cyclosporine | LOC100508689 | Homo sapiens |
| 14 | Taken together, our results indicate that the interaction of gel-forming mucins with the cyclic peptide CsA is mediated at the N- and C-terminal domains of mucin polymers under physiological conditions. | Cyclosporine | LOC100508689 | Homo sapiens |