Abstract
Human stefin B is a protease inhibitor from the family of cystatins. It was reported that it forms oligomers in cells. We have shown that it has a role in cell’s response to misfolded proteins. We also have shown that its oligomers bind amyloid-beta (Aβ). Here, we discuss ways, how stefin B could reduce build-up of protein aggregates by other proteins and consequently reduces ROS and, how this might be connected to autophagy. When overexpressed, stefin B forms protein aggregates itself and these protein aggregates induce autophagy. Similarly, cystatin C was shown to bind Aβ and to induce autophagy. It is also suggested how more knowledge about the role of stefin B in a cell’s response to misfolded proteins could be used to modulate progressive myoclonus epilepsy of type 1 EPM1 disease.
Highlights
Human stefin B is a protease inhibitor, belonging to the family of cystatins
It was reported that stefin-B knock-out KO cells are more sensitive to oxidative stress [19] and we have found ourselves that mural stefin B KO astrocytes bear more protein aggregates and have impaired autophagy [20]
Our previous studies showed that the R68X fragment was natively unfolded and that it transformed into amyloid fibrils already at neutral pH [40]
Summary
Human stefin B is a protease inhibitor, belonging to the family of cystatins. Human cystatins are of three types: cystatins of type 1 and 2 and kininogens. The fact that this protein aggregates, as many other proteins do, can be used mainly as a model for amyloidogenic proteins. Stefin B expression in cells and properties of the intracellular missense EPM1 mutants aggregates are relevant and represent possible modulating factors of the course of the disease (gain in toxic function).
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