Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent L-lysine-containing domains
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2017Metadata
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Gonzàlez Gronow, Mario
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Myelin basic protein stimulates plasminogen activation via tissue plasminogen activator following binding to independent L-lysine-containing domains
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Abstract
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.
Patrocinador
Fondo Nacional de
Desarrollo Cientίfico y Tecnolόgico de Chile, FONDECYT No 1130451
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URI: https://repositorio.uchile.cl/handle/2250/149113
DOI: http://dx.doi.org/10.1016/j.bbrc.2017.06.131
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Biochemical and Biophysical Research Communications 490 (2017) 855-860
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Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile
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