ArticleActa histochemica et cytochemica2010
VAMP2 marks quiescent satellite cells and myotubes, but not activated myoblasts.
Article in Acta histochemica et cytochemica, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Suppression of VAMP2 Alters Morphology of the Tegument and Affects Glucose uptake, Development and Reproduction of Schistosoma japonicum.Scientific reports · 2017Article
- Characterization of VAMP2 in Schistosoma japonicum and the Evaluation of Protective Efficacy Induced by Recombinant SjVAMP2 in Mice.PloS one · 2015Article
- Vesicular transport system in myotubes: ultrastructural study and signposting with vesicle-associated membrane proteins.Histochemistry and cell biology · 2014Article
- The localization of VAMP5 in skeletal and cardiac muscle.Histochemistry and cell biology · 2013Article
- Magnetically enhanced nucleic acid delivery. Ten years of magnetofection-progress and prospects.Advanced drug delivery reviews · 2011Review
- Immunohistochemical Analysis of Histone H3 Modifications in Germ Cells during Mouse Spermatogenesis.Acta histochemica et cytochemica · 2011Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We examined the expression and intracellular localization of vesicle-associated membrane protein 2 (VAMP2) during the differentiation of skeletal muscle cells by immunofluorescence microscopy. In isolated single myofibers, VAMP2 was expressed in quiescent satellite cells, downregulated in proliferating myoblastic cells, and re-expressed with differentiation. In the myoblastic cell line C2C12, VAMP2 was expressed at a low level in the proliferating stage, and then increased after differentiation into myotubes. Based on these results, we propose that VAMP2 can be used as a molecular marker for both quiescent satellite cells and myotubes, but not for proliferating myoblasts. We also found the partial colocalization of VAMP2 with transferrin- or Rab11-labeled vesicles in myotubes, suggesting a role of VAMP2 in the trafficking of recycling endosomes.
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Registered trials
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