Cystatin C regulates Cathepsin B activity within pancreatic zymogen granules and prevents pancreatic protease activation

Objectives. The aim of the study was to evaluate the activity of cathepsin B, collagenases, trypsin, and plasmin and concentration of cystatin C in serum of healthy pregnant women in peripartum period.Study Design. The study group included 45 women in uncomplicated pregnancies. Blood samples were collected in four time points. Enzyme activity was measured by spectrofluorometric method. The level of cystatin C was measured using immunonephelometric method.Results. Mean activity of cathepsin B and the level of serum cystatin C were significantly higher in the study group. Collagenase activity was significantly lower in the study group than the control group. No differences in collagenase, plasmin, and trypsin activity on each day of the peripartum period were found.Conclusion. High activity of cathepsin B and increased level of cystatin C are typical for women in late pregnancy. Those levels significantly decrease after delivery which can be associated with potential role of those markers in placental separation. The insignificant changes of cystatin C level in the peripartum period seem to exclude the possibility of using cystatin C as a marker for renal insufficiency in the peripartum period but additional research is necessary to investigate the matter further.

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Cathepsin B, Cathepsin H, Cathepsin X and Cystatin C in Sera of Patients with Early-Stage and Inflammatory Breast Cancer

The International Journal of Biological Markers ◽

10.1177/172460080802300305 ◽

2008 ◽

Vol 23 (3) ◽

pp. 161-168 ◽

Cited By ~ 36

Author(s):

J. Decock ◽

N. Obermajer ◽

S. Vozelj ◽

W. Hendrickx ◽

R. Paridaens ◽

...

Keyword(s):

Breast Cancer ◽

Cystatin C ◽

Inflammatory Breast Cancer ◽

Tumor Size ◽

Cathepsin B ◽

Early Stage ◽

Menopausal Status ◽

Preoperative Serum ◽

Cathepsin H ◽

Cathepsin X

Numerous studies have linked cathepsins and their inhibitor cystatin C to tumor invasion and metastasis. We examined whether cathepsin B, cathepsin H, cathepsin X and cystatin C could be detected in sera from women with early-stage or inflammatory breast cancer and whether they correlated with clinicopathological characteristics. Preoperative serum was obtained from 176 patients with early-stage breast cancer (tumor size <5 cm, negative lymph nodes) and 31 patients with inflammatory breast cancer. Cathepsin and cystatin C levels were measured by ELISA. The patient and tumor characteristics under study were age at diagnosis, menopausal status, tumor size, tumor grade, and steroid hormone receptor status. Serum cathepsin B levels were significantly lower in patients with poorly differentiated tumors. High cystatin C levels were associated with tumor size, postmenopausal status and patient age. Interestingly, significantly lower levels of cathepsin X and H were found in patients with inflammatory breast cancer, a trend also observed for cathepsin B and cystatin C. In conclusion, our results show a limited association of cathepsins B, H, X and cystatin C with established prognostic parameters. These data are promising and encourage future analysis of the clinical outcome of our patients in order to examine the potential prognostic value of these biomarkers. Further, this study indicates a role for cathepsin X and H in inflammatory breast cancer.

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The Role of Cathepsin B in Peritoneal Fibrosis due to Peritoneal Dialysis

International Journal of Nephrology ◽

10.1155/2019/4150656 ◽

2019 ◽

Vol 2019 ◽

pp. 1-7 ◽

Cited By ~ 1

Author(s):

Su Ah Sung ◽

Dong Hee Kim ◽

Kook-Hwan Oh ◽

Sang Youb Han ◽

Kum Hyun Han

Keyword(s):

Peritoneal Dialysis ◽

Cystatin C ◽

Cathepsin B ◽

Ca 125 ◽

Peritoneal Fibrosis ◽

Peritoneal Mesothelial Cells ◽

Type Plasminogen Activator ◽

Lysosomal Cysteine Protease ◽

Human Peritoneal Mesothelial Cells

Glucose-containing peritoneal dialysis (PD) solution causes peritoneal fibrosis (PF) characterized by accumulation of extracellular matrix (ECM) in the submesothelial layer. Cathepsin B is a lysosomal cysteine protease that degrades ECM, but its role in the PF remains unclear. Thus, we investigated the role of cathepsin B in PF. Procathepsin B was measured in the 73 PD effluents of 68 patients. Procathepsin B and cathepsin B after exposure of glucose and the effects of cathepsin B on the expression of matrix metalloproteinases (MMPs), tissue inhibitor of metalloproteinases (TIMPs), and urokinase-type plasminogen activator (uPA) were measured in the supernatant of cultured human peritoneal mesothelial cells (HPMCs). The effect of cathepsin B and its inhibitor, cystatin C, on PF was investigated in the murine model. Procathepsin B was measured at 3.6 μg/L in serum and 5.4 μg/L in PD effluent and positively correlated to the cancer antigen (CA) 125. The treatment with 4.25% glucose increased procathepsin B by 3.1-fold and cathepsin B by 5.9-fold in the HPMCs. Cathepsin B induced the secretion of MMP-1, -2, and -3 and TIMP-1 in the HPMCs, but uPA was not excreted. In the PF murine models, cathepsin B reduced the thickness of the submesothelial layer and cystatin C attenuated the effect of cathepsin B. HPMCs secrete cathepsin B with exposure of PD solution, and cathepsin B might help protect against PF.

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