Cysteine cathepsins in extracellular matrix remodeling: Extracellular matrix degradation and beyond.

Autor: Vizovišek M; Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute, Jamova cesta 39, SI-1000 Ljubljana, Slovenia., Fonović M; Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute, Jamova cesta 39, SI-1000 Ljubljana, Slovenia., Turk B; Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute, Jamova cesta 39, SI-1000 Ljubljana, Slovenia; Faculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, Slovenia. Electronic address: boris.turk@ijs.si.
Jazyk: angličtina
Zdroj: Matrix biology : journal of the International Society for Matrix Biology [Matrix Biol] 2019 Jan; Vol. 75-76, pp. 141-159. Date of Electronic Publication: 2018 Feb 01.
DOI: 10.1016/j.matbio.2018.01.024
Abstrakt: Cysteine cathepsins have been for a long time considered to execute mainly nonspecific bulk proteolysis in the endolysosomal system. However, this view has been changing profoundly over the last decade as cathepsins were found in the cytoplasm, nucleus and in the extracellular milieu. Cathepsins are currently gaining increased attention largely because of their extracellular roles associated with disease development and progression. While kept under tight control under physiological conditions, their dysregulated and elevated activity in the extracellular milieu are distinctive hallmarks of numerous diseases such as various cancers, inflammatory disorders, rheumatoid arthritis, bone disorders and heart diseases. In this review, we discuss cysteine cathepsins with a major focus on their extracellular roles and extracellular proteolytic targets beyond degradation of the extracellular matrix. We further highlight the perspectives of cathepsin research and novel avenues in cathepsin-based diagnostic and therapeutic applications.
(Copyright © 2018. Published by Elsevier B.V.)
Databáze: MEDLINE
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