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'Patchiness' and basic cancer research: unravelling the proteases.

Authors
  • Soond, Surinder M1
  • Kozhevnikova, Maria V1
  • Zamyatnin, Andrey A Jr1, 2
  • 1 a Institute of Molecular Medicine , Sechenov First Moscow State Medical University , Moscow , Russian Federation. , (Russia)
  • 2 b Belozersky Institute of Physico-Chemical Biology , Lomonosov Moscow State University , Moscow , Russian Federation. , (Russia)
Type
Published Article
Journal
Cell Cycle
Publisher
Landes Bioscience
Publication Date
Aug 01, 2019
Volume
18
Issue
15
Pages
1687–1701
Identifiers
DOI: 10.1080/15384101.2019.1632639
PMID: 31213124
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

The recent developments in Cathepsin protease research have unveiled a number of key observations which are fundamental to further our understanding of normal cellular homeostasis and disease. By far, the most interesting and promising area of Cathepsin biology stems from how these proteins are linked to the fate of living cells through the phenomenon of Lysosomal Leakage and Lysosomal Membrane Permeabilisation. While extracellular Cathepsins are generally believed to be of central importance in tumour progression, through their ability to modulate the architecture of the Extracellular Matrix, intracellular Cathepsins have been established as being of extreme significance in mediating cell death through Apoptosis. With these two juxtaposed key research areas in mind, the focus of this review highlights recent advancements in how this fast-paced area of Cathepsin research has recently evolved in the context of their mechanistic regulation in cancer research. Abbreviations : ECM, Extracellular Matrix; MMP, Matrix Metalloproteases; LL, Lysosomal Leakage; LMP, Lysosomal Membrane Permeabilisation; LMA, Lysosomorphic Agents; BC, Breast Cancer; ASM, Acid Sphingomyelinase; TNF-α, Tumor Necrosis Factor-alpha; LAMP, Lysosomal Associated membrane Protein; PCD, Programmed Cell Death; PDAC, Pancreatic Ductal Adenocarcinoma; ROS, Reactive Oxygen Species; aa, amino acids.

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