File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: The mouse C2C12 myoblast cell surface N-linked glycoproteome: Identification, glycosite occupancy, and membrane orientation

TitleThe mouse C2C12 myoblast cell surface N-linked glycoproteome: Identification, glycosite occupancy, and membrane orientation
Authors
Issue Date2009
Citation
Molecular and Cellular Proteomics, 2009, v. 8 n. 11, p. 2555-2569 How to Cite?
AbstractEndogenous regeneration and repair mechanisms are responsible for replacing dead and damaged cells to maintain or enhance tissue and organ function, and one of the best examples of endogenous repair mechanisms involves skeletal muscle. Although the molecular mechanisms that regulate the differentiation of satellite cells and myoblasts toward myofibers are not fully understood, cell surface proteins that sense and respond to their environment play an important role. The cell surface capturing technology was used here to uncover the cell surface N-linked glycoprotein subproteome of myoblasts and to identify potential markers of myoblast differentiation. 128 bona fide cell surface-exposed N-linked glycoproteins, including 117 transmembrane, four glycosylphosphatidylinositol-anchored, five extracellular matrix, and two membrane-associated proteins were identified from mouse C2C12 myoblasts. The data set revealed 36 cluster of differentiation-annotated proteins and confirmed the occupancy for 235 N-linked glycosylation sites. The identification of the N-glycosylation sites on the extracellular domain of the proteins allowed for the determination of the orientation of the identified proteins within the plasma membrane. One glycoprotein transmembrane orientation was found to be inconsistent with Swiss-Prot annotations, whereas ambiguous annotations for 14 other proteins were resolved. Several of the identified N-linked glycoproteins, including aquaporin-1 and β-sarcoglycan, were found in validation experiments to change in overall abundance as the myoblasts differentiate toward myotubes. Therefore, the strategy and data presented shed new light on the complexity of the myoblast cell surface subproteome and reveal new targets for the clinically important characterization of cell intermediates during myoblast differentiation into myotubes.
Persistent Identifierhttp://hdl.handle.net/10722/195201
ISSN
2015 Impact Factor: 5.912
2015 SCImago Journal Rankings: 3.213
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorGundry, RL-
dc.contributor.authorRaginski, K-
dc.contributor.authorTarasova, Y-
dc.contributor.authorTchernyshyov, I-
dc.contributor.authorBausch-Fluck, D-
dc.contributor.authorElliott, ST-
dc.contributor.authorBoheler, KR-
dc.contributor.authorVan Eyk, JE-
dc.contributor.authorWollscheid, B-
dc.date.accessioned2014-02-25T01:40:18Z-
dc.date.available2014-02-25T01:40:18Z-
dc.date.issued2009-
dc.identifier.citationMolecular and Cellular Proteomics, 2009, v. 8 n. 11, p. 2555-2569-
dc.identifier.issn1535-9476-
dc.identifier.urihttp://hdl.handle.net/10722/195201-
dc.description.abstractEndogenous regeneration and repair mechanisms are responsible for replacing dead and damaged cells to maintain or enhance tissue and organ function, and one of the best examples of endogenous repair mechanisms involves skeletal muscle. Although the molecular mechanisms that regulate the differentiation of satellite cells and myoblasts toward myofibers are not fully understood, cell surface proteins that sense and respond to their environment play an important role. The cell surface capturing technology was used here to uncover the cell surface N-linked glycoprotein subproteome of myoblasts and to identify potential markers of myoblast differentiation. 128 bona fide cell surface-exposed N-linked glycoproteins, including 117 transmembrane, four glycosylphosphatidylinositol-anchored, five extracellular matrix, and two membrane-associated proteins were identified from mouse C2C12 myoblasts. The data set revealed 36 cluster of differentiation-annotated proteins and confirmed the occupancy for 235 N-linked glycosylation sites. The identification of the N-glycosylation sites on the extracellular domain of the proteins allowed for the determination of the orientation of the identified proteins within the plasma membrane. One glycoprotein transmembrane orientation was found to be inconsistent with Swiss-Prot annotations, whereas ambiguous annotations for 14 other proteins were resolved. Several of the identified N-linked glycoproteins, including aquaporin-1 and β-sarcoglycan, were found in validation experiments to change in overall abundance as the myoblasts differentiate toward myotubes. Therefore, the strategy and data presented shed new light on the complexity of the myoblast cell surface subproteome and reveal new targets for the clinically important characterization of cell intermediates during myoblast differentiation into myotubes.-
dc.languageeng-
dc.relation.ispartofMolecular and Cellular Proteomics-
dc.titleThe mouse C2C12 myoblast cell surface N-linked glycoproteome: Identification, glycosite occupancy, and membrane orientation-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1074/mcp.M900195-MCP200-
dc.identifier.pmid19656770-
dc.identifier.scopuseid_2-s2.0-72149120326-
dc.identifier.volume8-
dc.identifier.issue11-
dc.identifier.spage2555-
dc.identifier.epage2569-
dc.identifier.isiWOS:000271615200012-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats