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Wearable Sensors for Blood Perfusion Monitoring in Patients with Diabetes Mellitus
Published in Andrey V. Dunaev, Valery V. Tuchin, Biomedical Photonics for Diabetes Research, 2023
Evgenii A. Zherebtsov, Elena V. Zharkikh, Yulia I. Loktionova, Angelina I. Zherebtsova, Viktor V. Sidorov, Alexander I. Krupatkin, Andrey V. Dunaev
The progression of increased endothelial permeability is thought to be associated with cathepsin S. Сathepsin S secreted by the invading macrophages activates protease-activated receptor-2 on endothelial cells, resulting in the increase in microvascular permeability manifesting as albuminuria; administration of inhibitors of either cathepsin S or protease-activated receptor-2 prevented ultrastructural and functional endothelial abnormalities and attenuated albuminuria and glomerulosclerosis [22,23].
Osteoporosis
Published in Peter V. Giannoudis, Thomas A. Einhorn, Surgical and Medical Treatment of Osteoporosis, 2020
Ippokratis Pountos, Peter V. Giannoudis
Cathepsin K is a catalytic enzyme of collagen type I expressed in osteoclasts. A small amount of cathepsin K is released in the circulation but is degraded quickly by other enzymes like cathepsin S. There is some evidence to suggest that cathepsin K is increased in postmenopausal women with osteoporosis, but its clinical relevance should be further elucidated as this molecule is involved in pathologies like osteoarthritis, atherosclerosis, and cardiovascular diseases (39).
Major Histocompatibility Complex and Autoimmune Disease
Published in Richard K. Burt, Alberto M. Marmont, Stem Cell Therapy for Autoimmune Disease, 2019
Ursula Holzer, Gerald T. Nepom
The two main proteases involved in the degradation of the Ii chain are cathepsin L and S, which are differently distributed in tissues. Whereas cathepsin L is expressed in cortical thymic epithelial cells (cTEC), which present endogenous peptides to maturing thymocytes, cathepsin S is found in bone marrow-derived APCs like dendritic cells, macrophages or B-cells.20 Interestingly, cathepsin S deficient mice exhibit significantly diminished susceptibility to collagen-induced arthritis, the mouse model for human rheumatoid arthritis,21 thus suggesting that the proteolytic pathway involving antigen and the Ii chain are involved in processing and recognition of target antigens in this model of induced autoimmunity.
The cellular prion protein and its derived fragments in human prion diseases and their role as potential biomarkers
Published in Expert Review of Molecular Diagnostics, 2019
Katrin Thüne, Matthias Schmitz, Anna Villar-Piqué, Hermann Clemens Altmeppen, Markus Schlomm, Saima Zafar, Markus Glatzel, Franc Llorens, Inga Zerr
In sCJD brains, excessive Ca2+ levels were found to accompany activation of calpains 1/2 and cathepsin S, which was demonstrated to be linked to cleavage of different cellular substrates, impaired autophagy, and lysosomal damage [134]. Activation of calpains and cathepsins was found to be an upstream event in experimental prion models [130,134,135]. Calpains are non-lysosomal cysteine proteases that mediate regulatory as well as katabolic functions through their proteolytic activity in order to feature important physiological processes including signal transduction, synaptic plasticity, learning and memory, or apoptosis. Through cleavage of their substrates at specific sites, calpains are able to generate large, often bioactive fragments with modified properties. Similarly, cathepsin S and some aspartyl protease cathepsins have been observed to carry out their distinct functions by limited proteolysis of proteins [136].
Epithelial damage in the cystic fibrosis lung: the role of host and microbial factors
Published in Expert Review of Respiratory Medicine, 2022
Arlene M. A. Glasgow, Catherine M. Greene
Cysteine cathepsins are a group of cysteine proteases that are located in lysosomes and work most effectively at acidic pH, with the exception of cathepsin S and cathepsin C which can function at neutral to alkaline pH [91]. Although they have many intracellular functions such as lysosomal degradation of pathogen proteins and antigen presentation, they can also be released extracellularly from a range of cell types including macrophages, neutrophils, mast cells, fibroblasts, and lung epithelial and endothelial cells. Here, they can potently degrade ECM proteins such as elastin, collagen, fibronectin, and laminin [91].
Emerging treatment for Sjögren’s disease: a review of recent phase II and III trials
Published in Expert Opinion on Emerging Drugs, 2023
Robert I. Fox, Carla M. Fox, Sara S. McCoy
Amongst the lysosomal cysteine cathepsin family of proteases, cathepsin-S (CTSS) holds particular interest due to distinctive properties, including a normally restricted expression profile, inducible upregulation, and activity at a broad pH range. Consequently, while CTSS is well established as a member of the proteolytic cocktail within the lysosome degrading unwanted and damaged proteins, it has increasingly been shown to mediate several distinct, more selective roles, including antigen processing and antigen presentation and cleavage of substrates both intra and extracellular.