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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cellular Plasticity

Background:

  • Structural plasticity of dendritic spines underlies learning and memory.
  • This plasticity depends on brain-derived neurotrophic factor (BDNF) and its receptor TrkB.
  • Mature BDNF requires proteolytic cleavage from its precursor, proBDNF, to bind TrkB.

Purpose of the Study:

  • To investigate the role of matrix metalloproteinase-9 (MMP-9) in BDNF maturation and TrkB activation.
  • To determine if MMP-9 is involved in the structural plasticity of dendritic spines.

Main Methods:

  • Utilized two-photon microscopy for real-time observation.
  • Employed single-spine stimulation via glutamate uncaging.
  • Assessed MMP-9 release and proteolytic activity post-stimulation.
  • Investigated MMP-9's direct cleavage of proBDNF.

Main Results:

  • MMP-9 is rapidly released upon synaptic stimulation, with activity localized to activated spines within 2 minutes.
  • MMP-9 activity is essential for tropomyosin receptor kinase B (TrkB) activation.
  • MMP-9 directly cleaves pro-brain-derived neurotrophic factor (proBDNF) into mature BDNF.
  • MMP-9 is required for activity-dependent structural plasticity of dendritic spines.

Conclusions:

  • Matrix metalloproteinase-9 (MMP-9) plays a critical role in processing brain-derived neurotrophic factor (BDNF).
  • MMP-9 directly facilitates the maturation of BDNF, enabling TrkB receptor activation.
  • This MMP-9-BDNF interaction is essential for regulating dendritic spine structural plasticity, impacting learning and memory mechanisms.