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Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to

Mario Gonzalez-Gronow1, Jenny L Fiedler2, Cristian Farias Gomez3

  • 1Department of Biological Sciences, Laboratory of Environmental Neurotoxicology, Faculty of Medicine, Universidad Católica del Norte, Coquimbo, Chile; Department of Pathology, Duke University Medical Center, Durham, NC, USA.

Biochemical and Biophysical Research Communications
|June 27, 2017
PubMed

Insights

Myelin basic protein (MBP) enhances plasminogen activation by tissue-type plasminogen activator (t-PA). This interaction, crucial for myelin physiology, involves specific binding sites on MBP.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Myelin basic protein (MBP) is essential for the structure and function of myelin, the insulating sheath around neuronal axons.
  • Plasminogen (Pg) and tissue-type plasminogen activator (t-PA) are key components of the fibrinolytic system, involved in blood clot breakdown.

Purpose of the Study:

  • To investigate the interaction and kinetics between MBP, Pg, and t-PA.
  • To elucidate the molecular mechanisms underlying Pg activation by t-PA in the presence of MBP.

Main Methods:

  • Utilized immobilized MBP to study binding kinetics.
  • Analyzed the specific binding sites and mechanisms of t-PA and Pg on MBP.

Main Results:

  • MBP significantly stimulates Pg activation by t-PA.
  • t-PA binds to MBP via a lysine-dependent mechanism at Lys91 (residues Asp82-Pro99).
  • Pg binds to MBP via a lysine-dependent mechanism at Lys122 (residues Leu109-Gly126).

Conclusions:

  • MBP acts as a mimic of fibrin in the context of plasminogen activation.
  • These findings suggest a direct role for the plasminogen activation system in myelin basic protein physiology.
Keywords:
Myelin basic proteinPlasminogenPlasminogen receptorTissue plasminogen activator (tPA)

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