| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-155 |
Sentence |
denotes |
Glycosylation of α-dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases. |
| T2 |
156-608 |
Sentence |
denotes |
O-Linked glycosylation is a functionally and structurally diverse type of protein modification present in many tissues and across many species. α-Dystroglycan (α-DG), a protein linked to the extracellular matrix, whose glycosylation status is associated with human muscular dystrophies, displays two predominant types of O-glycosylation, O-linked mannose (O-Man) and O-linked N-acetylgalactosamine (O-GalNAc), in its highly conserved mucin-like domain. |
| T3 |
609-690 |
Sentence |
denotes |
The O-Man is installed by an enzyme complex present in the endoplasmic reticulum. |
| T4 |
691-849 |
Sentence |
denotes |
O-GalNAc modifications are initiated subsequently in the Golgi apparatus by the UDP-GalNAc polypeptide N-acetylgalactosaminyltransferase (ppGalNAc-T) enzymes. |
| T5 |
850-1021 |
Sentence |
denotes |
How the presence and position of O-Man influences the action of the ppGalNAc-Ts on α-DG and the distribution of the two forms of glycosylation in this domain is not known. |
| T6 |
1022-1230 |
Sentence |
denotes |
Here, we investigated the interplay between O-Man and the addition of O-GalNAc by examining the activity of the ppGalNAc-Ts on peptides and O-Man-containing glycopeptides mimicking those found in native α-DG. |
| T7 |
1231-1347 |
Sentence |
denotes |
These synthetic glycopeptides emulate intermediate structures, not otherwise readily available from natural sources. |
| T8 |
1348-1629 |
Sentence |
denotes |
Through enzymatic and mass spectrometric methods, we demonstrate that the presence and specific location of O-Man can impact either the regional exclusion or the site of O-GalNAc addition on α-DG, elucidating the factors contributing to the glycosylation patterns observed in vivo. |
| T9 |
1630-1950 |
Sentence |
denotes |
These results provide evidence that one form of glycosylation can influence another form of glycosylation in α-DG and suggest that in the absence of proper O-mannosylation, as is associated with certain forms of muscular dystrophy, aberrant O-GalNAc modifications may occur and could play a role in disease presentation. |
