Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent l-lysine-containing domains.
Journal Article (Journal Article)
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.
Full Text
Duke Authors
Cited Authors
- Gonzalez-Gronow, M; Fiedler, JL; Farias Gomez, C; Wang, F; Ray, R; Ferrell, PD; Pizzo, SV
Published Date
- August 26, 2017
Published In
Volume / Issue
- 490 / 3
Start / End Page
- 855 - 860
PubMed ID
- 28648598
Electronic International Standard Serial Number (EISSN)
- 1090-2104
Digital Object Identifier (DOI)
- 10.1016/j.bbrc.2017.06.131
Language
- eng
Conference Location
- United States