
Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent l-lysine-containing domains.
Myelin basic protein (MBP) is a key component of myelin, the specialized lipid membrane that encases the axons of all neurons. Both plasminogen (Pg) and tissue-type plasminogen activator (t-PA) bind to MBP with high affinity. We investigated the kinetics and mechanisms involved in this process using immobilized MBP and found that Pg activation by t-PA is significantly stimulated by MBP. This mechanism involves the binding of t-PA via a lysine-dependent mechanism to the Lys91 residue of the MBP NH2-terminal region Asp82 -Pro99, and the binding of Pg via a lysine-dependent mechanism to the Lys122 residue of the MBP COOH-terminal region Leu109-Gly126. In this context, MBP mimics fibrin and because MBP is a plasmin substrate, our results suggest direct participation of the Pg activation system on MBP physiology.
Duke Scholars
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Related Subject Headings
- Tissue Plasminogen Activator
- Proteolysis
- Protein Domains
- Protein Binding
- Plasminogen
- Myelin Basic Protein
- Lysine
- Kinetics
- Humans
- Enzyme Activation
Citation

Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Tissue Plasminogen Activator
- Proteolysis
- Protein Domains
- Protein Binding
- Plasminogen
- Myelin Basic Protein
- Lysine
- Kinetics
- Humans
- Enzyme Activation