Scholars@Duke publication: Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent l-lysine-containing domains.

Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent l-lysine-containing domains.

Publication , Journal Article

Gonzalez-Gronow, M; Fiedler, JL; Farias Gomez, C; Wang, F; Ray, R; Ferrell, PD; Pizzo, SV

Published in: Biochem Biophys Res Commun

August 26, 2017

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

Author Mario Gonzalez-Gronow Pathology

Author Salvatore Vincent Pizzo Pathology

Published In

Biochem Biophys Res Commun

DOI

10.1016/j.bbrc.2017.06.131

EISSN

1090-2104

Publication Date

August 26, 2017

Volume

490

Issue

Start / End Page

855 / 860

Location

United States

Related Subject Headings

Tissue Plasminogen Activator
Proteolysis
Protein Domains
Protein Binding
Plasminogen
Myelin Basic Protein
Lysine
Kinetics
Humans
Enzyme Activation

Citation

APA

Chicago

ICMJE

MLA

NLM

Gonzalez-Gronow, M., Fiedler, J. L., Farias Gomez, C., Wang, F., Ray, R., Ferrell, P. D., & Pizzo, S. V. (2017). Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent l-lysine-containing domains. Biochem Biophys Res Commun, 490(3), 855–860. https://doi.org/10.1016/j.bbrc.2017.06.131

Gonzalez-Gronow, Mario, Jenny L. Fiedler, Cristian Farias Gomez, Fang Wang, Rupa Ray, Paul D. Ferrell, and Salvatore V. Pizzo. “Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent l-lysine-containing domains.” Biochem Biophys Res Commun 490, no. 3 (August 26, 2017): 855–60. https://doi.org/10.1016/j.bbrc.2017.06.131.

Gonzalez-Gronow M, Fiedler JL, Farias Gomez C, Wang F, Ray R, Ferrell PD, et al. Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent l-lysine-containing domains. Biochem Biophys Res Commun. 2017 Aug 26;490(3):855–60.

Gonzalez-Gronow, Mario, et al. “Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent l-lysine-containing domains.” Biochem Biophys Res Commun, vol. 490, no. 3, Aug. 2017, pp. 855–60. Pubmed, doi:10.1016/j.bbrc.2017.06.131.

Gonzalez-Gronow M, Fiedler JL, Farias Gomez C, Wang F, Ray R, Ferrell PD, Pizzo SV. Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent l-lysine-containing domains. Biochem Biophys Res Commun. 2017 Aug 26;490(3):855–860.