Search
Clear search
Close search
Main menu
Google apps
2 datasets found
  1. f

    Data_Sheet_1_The Endothelial Mechanotransduction Protein Platelet...

    • frontiersin.figshare.com
    docx
    Updated Jun 1, 2023
    Share
    FacebookFacebook
    TwitterTwitter
    Email
    Click to copy link
    Link copied
    Close
    Cite
    Lasse Gliemann; Nicolai Rytter; Peter Piil; Jannik Nilton; Thomas Lind; Michael Nyberg; Matthew Cocks; Ylva Hellsten (2023). Data_Sheet_1_The Endothelial Mechanotransduction Protein Platelet Endothelial Cell Adhesion Molecule-1 Is Influenced by Aging and Exercise Training in Human Skeletal Muscle.docx [Dataset]. http://doi.org/10.3389/fphys.2018.01807.s001
    Explore at:
    docxAvailable download formats
    Dataset updated
    Jun 1, 2023
    Dataset provided by
    Frontiers
    Authors
    Lasse Gliemann; Nicolai Rytter; Peter Piil; Jannik Nilton; Thomas Lind; Michael Nyberg; Matthew Cocks; Ylva Hellsten
    License

    Attribution 4.0 (CC BY 4.0)https://creativecommons.org/licenses/by/4.0/
    License information was derived automatically

    Description

    Aim: The aim was to determine the role of aging and exercise training on endothelial mechanosensor proteins and the hyperemic response to shear stress by passive leg movement.Methods: We examined the expression of mechanosensor proteins and vascular function in young (n = 14, 25 ± 3 years) and old (n = 14, 72 ± 5 years) healthy male subjects with eight weeks of aerobic exercise training. Before and after training, the hyperaemic response to passive leg movement was determined and a thigh muscle biopsy was obtained before and after passive leg movement to assess the acute effect of increased shear stress. Biopsies were analyzed for protein amount and phosphorylation of mechanosensor proteins; Platelet endothelial cell adhesion molecule-1 (PECAM-1), Vascular endothelial cadherin, Vascular endothelial growth factor receptor-2 and endothelial nitric oxide synthase (eNOS).Results: Before training, the old group presented a lower hyperaemic response to passive leg movement and a 35% lower (P < 0.05) relative basal phosphorylation level of PECAM-1 whereas there was no difference for the other mechanosensor proteins. After training, the eNOS protein amount, the amount of PECAM-1 protein and the passive leg movement-induced phosphorylation of PECAM-1 were higher in both groups. The hyperaemic response to passive leg movement was higher after training in the young group only.Conclusion: Aged individuals have a lower hyperaemic response to passive leg movement and a lower relative basal phosphorylation of PECAM-1 than young. The higher PECAM-1 phosphorylation despite a similar hyperemic level in the aged observed after training, suggests that training improved shear stress responsiveness of this mechanotransduction protein.

  2. t

    BIOGRID CURATED DATA FOR PUBLICATION: Cellular mechanotransduction relies on...

    • thebiogrid.org
    zip
    Updated Mar 4, 2013
    Share
    FacebookFacebook
    TwitterTwitter
    Email
    Click to copy link
    Link copied
    Close
    Cite
    BioGRID Project (2013). BIOGRID CURATED DATA FOR PUBLICATION: Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. [Dataset]. https://thebiogrid.org/151657/publication/cellular-mechanotransduction-relies-on-tension-induced-and-chaperone-assisted-autophagy.html
    Explore at:
    zipAvailable download formats
    Dataset updated
    Mar 4, 2013
    Dataset authored and provided by
    BioGRID Project
    License

    MIT Licensehttps://opensource.org/licenses/MIT
    License information was derived automatically

    Description

    Protein-Protein, Genetic, and Chemical Interactions for Ulbricht A (2013):Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. curated by BioGRID (https://thebiogrid.org); ABSTRACT: Mechanical tension is an ever-present physiological stimulus essential for the development and homeostasis of locomotory, cardiovascular, respiratory, and urogenital systems [1, 2]. Tension sensing contributes to stem cell differentiation, immune cell recruitment, and tumorigenesis [3, 4]. Yet, how mechanical signals are transduced inside cells remains poorly understood. Here, we identify chaperone-assisted selective autophagy (CASA) as a tension-induced autophagy pathway essential for mechanotransduction in muscle and immune cells. The CASA complex, comprised of the molecular chaperones Hsc70 and HspB8 and the cochaperone BAG3, senses the mechanical unfolding of the actin-crosslinking protein filamin. Together with the chaperone-associated ubiquitin ligase CHIP, the complex initiates the ubiquitin-dependent autophagic sorting of damaged filamin to lysosomes for degradation. Autophagosome formation during CASA depends on an interaction of BAG3 with synaptopodin-2 (SYNPO2). This interaction is mediated by the BAG3 WW domain and facilitates cooperation with an autophagosome membrane fusion complex. BAG3 also utilizes its WW domain to engage in YAP/TAZ signaling. Via this pathway, BAG3 stimulates filamin transcription to maintain actin anchoring and crosslinking under mechanical tension. By integrating tension sensing, autophagosome formation, and transcription regulation during mechanotransduction, the CASA machinery ensures tissue homeostasis and regulates fundamental cellular processes such as adhesion, migration, and proliferation.

  3. Not seeing a result you expected?
    Learn how you can add new datasets to our index.

Share
FacebookFacebook
TwitterTwitter
Email
Click to copy link
Link copied
Close
Cite
BioGRID Project (2013). BIOGRID CURATED DATA FOR PUBLICATION: Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. [Dataset]. https://thebiogrid.org/151657/publication/cellular-mechanotransduction-relies-on-tension-induced-and-chaperone-assisted-autophagy.html

BIOGRID CURATED DATA FOR PUBLICATION: Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy.

Related Article
Explore at:
zipAvailable download formats
Dataset updated
Mar 4, 2013
Dataset authored and provided by
BioGRID Project
License

MIT Licensehttps://opensource.org/licenses/MIT
License information was derived automatically

Description

Protein-Protein, Genetic, and Chemical Interactions for Ulbricht A (2013):Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. curated by BioGRID (https://thebiogrid.org); ABSTRACT: Mechanical tension is an ever-present physiological stimulus essential for the development and homeostasis of locomotory, cardiovascular, respiratory, and urogenital systems [1, 2]. Tension sensing contributes to stem cell differentiation, immune cell recruitment, and tumorigenesis [3, 4]. Yet, how mechanical signals are transduced inside cells remains poorly understood. Here, we identify chaperone-assisted selective autophagy (CASA) as a tension-induced autophagy pathway essential for mechanotransduction in muscle and immune cells. The CASA complex, comprised of the molecular chaperones Hsc70 and HspB8 and the cochaperone BAG3, senses the mechanical unfolding of the actin-crosslinking protein filamin. Together with the chaperone-associated ubiquitin ligase CHIP, the complex initiates the ubiquitin-dependent autophagic sorting of damaged filamin to lysosomes for degradation. Autophagosome formation during CASA depends on an interaction of BAG3 with synaptopodin-2 (SYNPO2). This interaction is mediated by the BAG3 WW domain and facilitates cooperation with an autophagosome membrane fusion complex. BAG3 also utilizes its WW domain to engage in YAP/TAZ signaling. Via this pathway, BAG3 stimulates filamin transcription to maintain actin anchoring and crosslinking under mechanical tension. By integrating tension sensing, autophagosome formation, and transcription regulation during mechanotransduction, the CASA machinery ensures tissue homeostasis and regulates fundamental cellular processes such as adhesion, migration, and proliferation.