ArticleHistochemistry and cell biology2013
The localization of VAMP5 in skeletal and cardiac muscle.
Article in Histochemistry and cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Targeting VAMP5 suppresses PLK1-driven growth of gliomas with high NDRG4 expression.Journal of neuro-oncology · 2026Article
- Picalm coordinates clathrin-mediated endocytosis and actin remodeling during myogenesis.Molecular metabolism · 2026Article
- A PTPRO-Related Five-Gene Blood Transcriptional Signature with Diagnostic Potential for Tuberculosis.Biomedicines · 2026Article
- VAMP proteins: molecular architects in disease pathogenesis and therapeutic innovation.Medical oncology (Northwood, London, England) · 2025Review
- VAMP5 promotes Fcγ receptor-mediated phagocytosis and regulates phagosome maturation in macrophages.Molecular biology of the cell · 2024Article
- Correlative microscopy and block-face imaging (CoMBI): a 3D imaging method with wide applicability in the field of biological science.Anatomical science international · 2023Review
- Release of VAMP5-positive extracellular vesicles by retinal Müller glia in vivo.Journal of extracellular vesicles · 2022Article
- Article
- Vesicular transport system in myotubes: ultrastructural study and signposting with vesicle-associated membrane proteins.Histochemistry and cell biology · 2014Article
- The Histochem Cell Biol conspectus: the year 2013 in review.Histochemistry and cell biology · 2014Review
- Long non-coding RNA expression profiling in the lungs of pulmonary arterial hypertension rats with acute inflammation.Pulmonary circulationArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vesicle-associated membrane protein 5 (VAMP5) is a member of the SNARE protein family, which is generally thought to regulate the docking and fusion of vesicles with their target membranes. This study investigated the expression and localization of the VAMP5 protein. Immunoblotting analyses detected the VAMP5 protein in skeletal muscle, heart, spleen, lung, liver, and kidney tissue, but not in brain or small intestine tissue. Through the immunofluorescence microscopy of skeletal muscle, we found that the expression level of VAMP5 varies among fibers. Most of the fibers with high expression levels of VAMP5 were categorized as type IIa fibers on the basis of their myosin heavy chain subtypes. In addition, the expression patterns of VAMP5 and glucose transporter 4 (GLUT4) were similar. In cardiac muscle, we determined that VAMP5 was localized to the vicinity of intercalated discs. These results suggest that VAMP5 plays local roles in membrane trafficking in skeletal and cardiac muscle.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.