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Pannexin1 drives multicellular aggregate compaction via a signaling cascade that remodels the actin cytoskeleton

Brian A Bao1, Charles P Lai, Christian C Naus

  • 1Department of Molecular Pharmacology, Physiology, and Biotechnology, Center for Biomedical Engineering, Brown University, Providence, Rhode Island 02912, USA.

The Journal of Biological Chemistry
|January 24, 2012
PubMed

Insights

Pannexin 1 (Panx1) channels release ATP, activating purinergic signaling and actomyosin function to promote cancer cell aggregate assembly. This study reveals Panx1

Area of Science:

  • Biochemistry
  • Cell Biology
  • Cancer Research

Background:

  • Pannexin 1 (Panx1) is a gap junction protein with identified tumor-suppressive roles.
  • The role of Panx1 in the tumor's biomechanical microenvironment remains unclear.

Purpose of the Study:

  • To investigate the role of Panx1 channels in modulating the dynamic assembly of multicellular C6 glioma aggregates.
  • To elucidate the underlying molecular mechanisms, including purinergic signaling and cytoskeletal regulation.

Main Methods:

  • Utilized pharmacological inhibitors (carbenoxolone, probenecid) to block Panx1 channels.
  • Investigated the effects of exogenous ATP and purinergic antagonists (suramin).
  • Examined the F-actin microfilament network and employed a 3D scaffold-free method to quantify multicellular interactions.

Main Results:

  • Panx1 channel blockade inhibited glioma aggregate assembly.
  • Exogenous ATP reversed the inhibitory effects of Panx1 blockers.
  • Aggregate compaction was sensitive to purinergic antagonism.
  • Panx1 channels facilitate ATP release, activating the P(2)X(7) receptor and up-regulating actomyosin function.

Conclusions:

  • Panx1 channels are crucial regulators of intercellular biomechanical interactions in C6 glioma aggregates.
  • Panx1-mediated ATP release and purinergic signaling are pivotal in controlling aggregate assembly and cancer progression.

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