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Identification of Mediators of T-cell Receptor Signaling via the Screening of Chemical Inhibitor Libraries
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Identification of fibrinogen as a natural inhibitor of MMP-2

Hassan Sarker1, Eugenio Hardy1,2, Ayman Haimour1

  • 1Department of Biochemistry, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada.

Scientific Reports
|March 15, 2019
PubMed

Insights

Human fibrinogen (FBG) acts as a selective inhibitor of matrix metalloproteinase-2 (MMP-2). Elevated FBG levels may cause MMP-2 insufficiency, a condition linked to various pathologies.

Area of Science:

  • Biochemistry
  • Enzymology

Background:

  • Non-genetic MMP-2 insufficiency is poorly understood.
  • Potential causes include overexpression of MMP-2 inhibitors like TIMPs and alpha-2-macroglobulin.
  • Human fibrinogen (FBG) is an acute phase reactant with potential inhibitory roles.

Purpose of the Study:

  • To investigate the hypothesis that human fibrinogen (FBG) inhibits human MMP-2.
  • To explore the mechanism and domains of FBG involved in MMP-2 inhibition.

Main Methods:

  • Enzyme kinetics assays measuring MMP-2 activity with varying FBG concentrations.
  • Gelatin zymography to assess MMP-2 and MMP-9 binding to gelatin.
  • In silico analyses and antibody neutralization studies to identify inhibitory domains of FBG.

Main Results:

  • Human FBG concentration-dependently inhibited proMMP-2 and MMP-2 binding to gelatin.
  • FBG selectively inhibited MMP-2 (not MMP-9) cleavage of gelatin in a mixed-type inhibition pattern.
  • Domains D and E of FBG were implicated in MMP-2 inhibition.

Conclusions:

  • Human fibrinogen is a natural, selective inhibitor of MMP-2.
  • Pathological elevation of FBG may lead to MMP-2 insufficiency in humans.

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