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1

Inhibition of cathepsin B acivity in human breast cancer tissue by cysteine peptidase inhibitor isolated from human placenta: immunohistochemical and biochemical studies

100%
Saleh Y., Siewinski M., Sebzda T., Jelen M., Ziolkowski P., Gutowicz J., Grybos M., Pawelec M.
Folia Histochemica et Cytobiologica
|
2003
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tom 41
|
nr 3
2

The activities and subcellular localization of cathepsin B and cysteine proteinase inhibitors in human ovarian carcinoma

100%
Haczynska H., Gerber J., Osada J., Warwas M.
Acta Biochimica Polonica
|
1997
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tom 44
|
nr 1
Ovarian carcinomas exhibited a higher cathepsin B activity than did normal ovaries. The plasma membrane fractions of ovarian cancers were enriched in the activities of both cathepsin and cysteine proteinase inhibitors. The ratio of cathepsin to the inhibitors in these fractions was higher at stage IV than at stage III of the disease, classified according to the Federation of International Gynecology and Obstetrics.
3

The expression of matrix metalloproteinase 9 and cathepsin B in gastric carcinoma is associated with lymph node metastasis, but not with postoperative survival

84%
Czyzewska J., Guzinska-Ustymowicz K., Kemona A., Bandurski R.
Folia Histochemica et Cytobiologica
|
2008
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tom 46
|
nr 1
57-64
4
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One session of exercise regulates cathepsin B activity in the livers of trained and untrained rats

84%
Wyczalkowska-Tomasik A., Czarkowska-Paczek B., Piekarczyk-Persa J., Zendzian-Piotrowska M.
Journal of Physiology and Pharmacology
|
2017
|
tom 68
|
nr 5
5
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Distribution and amount of cathepsin B in gentamicin-induced acute kidney injury in rats

84%
Svara T., Pogacnik M., Juntes P.
Polish Journal of Veterinary Sciences
|
2010
|
tom 13
|
nr 1
75-82
The aim of our study was to investigate how the distribution and amount of cathepsin B change during acute kidney injury. The research was done on a rat model of acute kidney injury that was induced by nephrotoxic antibiotic gentamicin. Gentamicin was injected at a dose of 40 mg/kg body weight (the first treated group) and 80 mg/kg body weight (the second treated group) for 14 days. Control groups received injections of physiological saline only. One day after the last injection, animals were euthanized, dissected and kidney samples were taken and fixed in 10% buffered formalin. Tissue sections were stained with haematoxylin and eosin, periodic Acid Schiff (PAS) and Oil-red-O. Immunohistochemistry was used for the demonstration of cathepsin B. Vacuolar degeneration of the proximal convoluted tubules was the most prominent pathologic lesion found in the first treated group, while necrosis prevailed in the second treated group in the same localisation. In both treated groups significantly weaker immunohistochemical reaction for cathepsin B was noticed in the proximal convoluted tubules in comparison to the control groups (P < 0.05). The decrease of positive reaction was the largest in the proximal convoluted tubules of the outer renal cortex. Stronger positive reaction for cathepsin B, although not statistically significant, was found in the proximal straight tubules (P > 0.05), as well. However, more numerous cathepsin B-positive large granules appeared in the proximal straight tubules of the second treated group then in the second control group (P < 0.05). We can conclude that the amount of cathepsin B in the affected proximal convoluted tubules significantly decreases along the increased severity of the histopathological lesions of the proximal convoluted tubuls, the amount of enzyme in the well preserved proximal straight tubules increases and more cathepsin B-positive large granules appear in the cytoplasm.
6
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Missorting of cathepsin B into the secretory compartment of CI-MPR/IGFII-deficient mice does not induce spontaneous trypsinogen activation but leads to enhanced trypsin activity during experimental pancreatitis - without affecting disease severity

84%
Meister T., Niehues R., Hahn D., Domschke W., Sendler M., Lerch M. M., Schnekenburger J.
Journal of Physiology and Pharmacology
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2010
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tom 61
|
nr 5
7

A possible application of cathepsin B activity determination for estimating the spread of the cervix uteri carcinoma

84%
Makarewicz R., Drewa G.
Acta Biochimica Polonica
|
1996
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tom 43
|
nr 3
The value of cathcpsin B activity determination for evaluation of the extent of disease was investigated in 98 patients with the cervix uteri carcinoma and 25 women with cervix uteri dysplasia. The measurements were performed before treatment. Cathepsin B activity was estimated in serum using Z-Phe-Arg-NMec, and in tumor tissue using Z-Arg-Arg-pNA • HC1 as substrates. The mean activity of the enzyme increased both in serum and tumor tissue with progression of neoplastic disease and was dependent on the clinical stage of cervical carcinoma. It should be stressed, however, that among the patients with the clinically observed early stage of the disease, higher cathepsin B activity was observed in those in whom metastases to pelvic lymph nodes were detected than in those in whom the disease was limited to cervix uteri.
8

Interaction of cysteine proteinase inhibitor with liposomes. II. Effect on the inhibition of cathepsin

84%
Gutowicz J., Saleh J., Pola A., Siewinski M.
Cellular and Molecular Biology Letters
|
1999
|
tom 04
|
nr 2
9
Content available remote

Strong association between fibronectin accumulation and lowered cathepsin B activity in glomeruli of diabetic rats

67%
Wyczalkowska-Tomasik A., Bartolomiejczyk I., Gornicka B., Paczek L.
Journal of Physiology and Pharmacology
|
2012
|
tom 63
|
nr 5
10

Control of active B and L cathepsins in tissues of colorectal cancer using cystatins isolated from chicken egg proteins: in vitro studies

67%
Hap A., Kielan W., Grzebieniak Z., Siewinski M., Rudnicki J., Tarnawa R., Rudno-Rudzinska J., Agrawal A. K.
Folia Histochemica et Cytobiologica
|
2011
|
tom 49
|
nr 4
11

Fluorogenic peptide substrates for carboxydipeptidase activity of cathepsin B

67%
Stachowiak K., Tokmina M., Karpinska A., Sosnowska R., Wiczk W.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 1
Cathepsin B is a lysosomal cysteine protease exhibiting mainly dipeptidyl carboxypeptidase activity, which decreases dramatically above pH 5.5, when the en­zyme starts acting as an endopeptidase. Since the common cathepsin B assays are performed at pH 6 and do not distinguish between these activities, we synthesized a series of peptide substrates specifically designed for the carboxydipeptidase activity of cathepsin B. The amino-acid sequences of the P5-P1 part of these substrates were based on the binding fragments of cystatin C and cystatin SA, the natural reversible inhibitors of papain-like cysteine protease. The sequences of the P'1-P'2 dipeptide fragments of the substrates were chosen on the basis of the specificity of the S'1-S'2 sites of the cathepsin B catalytic cleft. The rates of hydrolysis by cathepsin B and papain, the archetypal cysteine protease, were monitored by a continuous fluores­cence assay based on internal resonance energy transfer from an Edans to a Dabcyl group. The fluorescence energy donor and acceptor were attached to the C- and the N-terminal amino-acid residues, respectively. The kinetics of hydrolysis followed the Michaelis-Menten model. Out of all the examined peptides Dabcyl-R-L-V-G-FE(Edans) turned out to be a very good substrate for both papain and cathepsin B at both pH 6 and pH 5. The replacement of Glu by Asp turned this peptide into an exclusive substrate for cathepsin B not hydrolyzed by papain. The substitution of Phe by Nal in the original substrate caused an increase of the specificity constant for cathepsin B at pH 5, and a significant decrease at pH 6. The results of kinetic studies also suggest that Arg in position P4 is not important for the exopeptidase activity of cathepsin B, and that introducing Glu in place of Val in position P2 causes an increase of the substrate preference towards this activity.
12

Inhibitory proteaz lizosomalnych lupin i liscieni nasion wyki

59%
Roszkowska-Jakimiec W., Kiziewicz B., Lahuta L.
Bromatologia i Chemia Toksykologiczna
|
2005
|
tom 38
|
nr Supl.
333-335
Łupiny i liścienie różnych gatunków i odmian wyki zawierają inhibitory katepsyny A, katepsyny В i katepsyny D.
13
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Muscle cathepsins of marine fish and invertebrates

51%
Kolodziejska I., Sikorski Z. E.
Polish Journal of Food and Nutrition Sciences
|
1995
|
tom 04
|
nr 3
Muscle proteases are located mainly in the lysosomes, in the sarcoplasm, and in the extracellular matrix of the connective tissue surrounding each cell. The lysosomal proteases, cathepsins, have optimum activity in the acidic range, although many of them retain high activity also 1 or 2 pH units away from the optimum value. Among the cathepsins there are endopeptidases and exopeptidases. Most cathepsins hydrolyse several proteins of the myofibrils. The major protease of the lysosomes in fish and squid muscles is cathepsin D, an aspartyl endoproteinase. Although it is present in the muscle fibre itself, its generally rather low activity at low temperature limits its significance in tenderization of refrigerated fish of most species. Cathepsin L, a cysteinyl protease, is involved in autolysis and softening in matured chum salmon. Cathepsin B, a cysteinyl carboxypeptidase, is capable to attack also some myofibrillar proteins. Cathepsin A or carboxypeptidase A, and cathepsin C, a dipeptidyl hydrolase and dipeptidyl transferase, contribute to the hydrolysis of muscle proteins in a concerted action with the other cathepsins.
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