CTSS

Case study 1: Svenja Memmert, 2018

Cathepsin S is a cysteine protease, which is expressed in human periodontal ligament (PDL) cells under inflammatory and infectious conditions. This in vitro study was established to investigate the effect of cathepsin S on PDL cell wound closure. An in vitro wound healing assay was used to monitor wound closure in wounded PDL cell monolayers for 72 h in the presence and absence of cathepsin S. In addition, the effects of cathepsin S on specific markers for apoptosis and proliferation were studied at transcriptional level. Changes in the proliferation rate due to cathepsin S stimulation were analyzed by an XTT assay, and the actions of cathepsin S on cell migration were investigated via live cell tracking. Additionally, PDL cell monolayers were treated with a toll-like receptor 2 agonist in the presence and absence of a cathepsin inhibitor to examine if periodontal bacteria can alter wound closure via cathepsins. Cathepsin S enhanced significantly the in vitro wound healing rate by inducing proliferation and by increasing the speed of cell migration, but had no effect on apoptosis. Moreover, the toll-like receptor 2 agonist enhanced significantly the wound closure and this stimulatory effect was dependent on cathepsins.

Fig1. Wound closure of PDL cell monolayers in the presence or absence of CTSS (1 ng/μl) over 72 h.

Fig2. PDL cell proliferation in the presence or absence of CTSS (1 ng/μl) at 4 h and 24 h. Mean ± SEM (n = 24), * significant (p < 0.05) difference between groups.

Case study 2: Min-Chieh Hsin, 2017

Hispolon, a phenolic compound isolated from Phellinus igniarius, induces apoptosis and anti-tumor effects in cancers. However, the molecular mechanism involved in hispolon-mediated tumor-suppressing activities observed in cervical cancer is poorly characterized. Here, the researchers demonstrated that treatment with hispolon inhibited cell metastasis in two cervical cancer cell lines. In addition, the downregulation of the lysosomal protease Cathepsin S (CTSS) was critical for hispolon-mediated suppression of tumor cell metastasis in both in vitro and in vivo models. Moreover, hispolon induced autophagy, which increased LC3 conversion and acidic vesicular organelle formation. Mechanistically, hispolon inhibited the cell motility of cervical cells through the extracellular signal-regulated kinase (ERK) pathway, and blocking of the ERK pathway reversed autophagy-mediated cell motility and CTSS inhibition. The results indicate that autophagy is essential for decreasing CTSS activity to inhibit tumor metastasis by hispolon treatment in cervical cancer; this finding provides a new perspective on molecular regulation.

Fig3. HeLa cells transfected with pCMV3-CTSS-His plasmid 5 μg for 6 h and treated with hispolon for 24 h, then analyzed by Western blot and migration assay.

Fig4. The interaction between Cathepsin S, LC3 and Ubiquitin. After treating the cells with hispolon, detecting that LC3 interacted with CTSS by Co-IP.

Fig1. Role of cathepsin S (CatS) in the immune-suppressive milieu of the tumor microenvironment (TME). (Natalie Fuchs, 2020)

Fig2. The schematic representation of anti-metastasis effects of hispolon in human cervical cancer cell. (Min-Chieh Hsin, 2017)

CTSS involved in several pathways and played different roles in them. We selected most pathways CTSS participated on our site, such as Adaptive Immune System, Antigen processing and presentation, Antigen processing-Cross presentation, which may be useful for your reference. Also, other proteins which involved in the same pathway with CTSS were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

CTSS has several biochemical functions, for example, collagen binding, cysteine-type endopeptidase activity, fibronectin binding. Some of the functions are cooperated with other proteins, some of the functions could acted by CTSS itself. We selected most functions CTSS had, and list some proteins which have the same functions with CTSS. You can find most of the proteins on our site.

CTSS has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with CTSS here. Most of them are supplied by our site. Hope this information will be useful for your research of CTSS.

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