• Biomedical Science Letters
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• v.10 no.4
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• pp.429-434
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• 2004

The effects of intravenous administration of high concentration of taurocholic acid (TCA) on cathepsin B and D, and acid phosphatase activities in rat liver lysosome were studied. These liver lysosomal enzymes were determined from the experimental rats with choledocho-caval shunt (CCS). The activities of liver lysosomal cathepsin B and D, and acid phosphatase were found to be significantly increased in the CCS plus TCA injection group than in control group, such as group of CCS alone group. However, these hepatic enzyme activities did not change in the CCS plus tauroursodeoxycholic acid injection group. The above results suggest that TCA stimulates the biosynthesis of the lysosomal cathepsin B and D, and acid phosphatase in the liver.

• Journal of Acupuncture Research
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• v.22 no.3
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• pp.1-12
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• 2005

It was clarified that ethanol extract herb-acupuncture solution (EE-UD) and hydrotherapy herb-acupuncture solution (WE-UD) in Ulmus davidiana Planch (Ulmaceae), are the excellent inhibitors of cathepsin K and L. WE-UD inhibited cathepsin K when IC50 value was 5.32 ${\square}g$/ml, and suppressed cathepsin L when IC50 value was 6.34 ${\square}g$/ml. However, EE-UD indicated the activity of inhibiting cathepsin K and L in the level of 1.45 ${\square}g$/ml and 2.43 ${\square}g$/ml, thus it showed more significance than WE-UD. It could be observed that EE-VD is an excellent inhibitor to cathepsin K with Ki value of 0.8 ${\square}g$/ml. This activity is increased by 10-fold even in the analytical experiment when having operations like glutathione in pH 7.0. Also, this supports the mixture of GSH thiolate anion, thus it was thought that this increase in effectiveness is probably attributable to the enhanced chemical function in the combinations of herb-acupuncture solution towards a place of activity in enzyme. WE-UD showed the time-dependent inhibiting property, thus it allowed to know the disunion and the compounding speed in constant cathepsin K during the process of experiment. Finally, EE-UD was proved to suppress the absorbent bone ash in the experiment related to osteoclast in rats for test, and to the bone in rodent. It was proved that WE-UD has the effect of inhibiting the protease in cathepsin K and L, and in collagen of bone. These results strongly suggest that it is effective in preventing the progress of bone damage, which was induced due to cathepsin K. Also, it obtained the conclusion that it is effective to the reabsorption activity of bone in the bone marrow cells.

• Development and Reproduction
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• v.17 no.3
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• pp.221-229
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• 2013

Cathepsins are members of the multigene family of lysosomal cysteine proteinases and have regulated function in several life processes. The potential role of cathepsin F cysteine gene was expected as protease in the yolk processing mechanism during early developmental stage, but expression analysis was unknown after fertilization. The alignment analysis showed that amino acid sequence of cathepsin F from olive flounder liver expressed sequence tag (EST) homologous to cathepsin F of other known cathepsin F sequences with 87-98% identity. In this study, we examined the gene expression analysis of cathepsin F in various tissues at variety age flounder. Tissue distribution of the cathepsin F mRNA has been shown to be ubiquitous and constitutive pattern regardless of age in each group, although derived from cDNA library using liver sample. The mRNA level of cathepsin F more increased as developmental proceed during embryogenesis and early developmental stage, especially increased in the blastula, hatching stage and 3 days post hatching (dph). As a result, it may suggest that the proteolysis of yolk proteins (YPs) has been implicated as a mechanism for nutrient supply during early larval stages in olive flounder.

• Food Science of Animal Resources
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• v.40 no.3
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• pp.415-425
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• 2020

It is believed that two main proteolytic systems are involved in the tenderization of meat: the cathepsins and the calpains. Many researchers consider the calpain system to be the major contributor to meat tenderness during post-mortem storage. However, the role and activity of cathepsins during post-mortem storage or low temperature meat processing is unclear, particularly for the tough meat cuts like brisket. Thus, the study was designed to investigate the effects of cold (refrigerated and frozen) storage and sous vide processing on the activities of cathepsin B, H, and L in beef brisket. There were no significant changes in pH and cathepsin H activity throughout the 18 d of storage at both temperatures. However, an increase in cathepsin B activity was observed during the first 4 d at both storage temperatures, but subsequently the activity remained unchanged. Cathepsins B and L were found to be more heat stable at sous vide temperatures (50℃ for 24 h, 55℃ for 5 h and at 60℃ and 70℃ for 1 h) compared to cathepsin H. Cathepsin B+L activity was found to increase after sous vide cooking at 50℃ for 1 h but decreased to about 47% relative to the uncooked control after 24 h of cooking. These results suggest that cathepsins B and L may contribute to the improved meat tenderness usually seen in sous vide cooked brisket meat.

• Food Science and Preservation
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• v.12 no.3
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• pp.275-281
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• 2005

This study was carried out to investigate the cathepsin B inhibition effect by Achyranthes japonica N. root extract in vitro. The methanol/$H_{2}O$(4:1, v/v) extract was fractionated by ethyl acetate(F1), chloroform(F2), chloroform/methanol(3:1, v/v)(F3) and methanol(F4). The yield of F4 in Achyranthes japonica N. root was $8.27\%$. As an index material of Achyranthes japonica N. root, 20-hydroxy ecdysone was detected by TLC, and HPLC and it's content was $0.33\%$. Three isolates(F1, F3, F4) showed the cathepsin B inhibition activity, and F4 showed the highest inhibition activity among them. In the inhibition activity on cathepsin B, leupeptin, 20-hydroxy ecdysone and F4(at the same concentration of 20-hydroxy ecdysone.) were 92, 88 and $97\%$ on BANA($N{\alpha}$-benzoyl-DL-arginine ${\beta}$-naphthylamide) substrate, and 62, 36 and $67\%$ on CLN($N{\alpha}$-CBZ(carbobenzlyoxy)-L-lysine p-nitrophenyl ester HCI) substrate, respectively.

• Asian Pacific Journal of Cancer Prevention
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• v.15 no.21
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• pp.9511-9515
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• 2014

Cholangiocarcinoma (CCA) is a cancer of the bile duct epithelial cells. The highest incidence rate of CCA with a poor prognosis and poor response to chemotherapy is found in Southeast Asian countries, especially in northeastern Thailand and Lao PDR. Cathepsin B is a lysosomal cysteine protease which is regulated by cysteine proteinase inhibitors such as cystatin C. Elevation of cathepsin B levels in biological fluid has been observed in patients with inflammatory diseases and many cancers. We aimed to investigate the serum cathepsin B and cystatin C levels of CCA patients to evaluate the feasibility of using cathepsin B and cystatin C as markers for the diagnosis of CCA. Fifty-six sera from CCA patients, 17 with benign biliary diseases (BBD) and 13 from controls were collected and the cathepsin B and cystatin C levels were determined. In addition, cathepsin B expression was investigated immunohistochemically for 9 matched-pairs of cancerous and adjacent tissues of CCA patients. Serum cathepsin B, but not cystatin C, was significantly higher in CCA and BBD patient groups compared to that in the control group. Consistently, all cancerous tissues strongly expressed cathepsin B while adjacent tissues were negative in 7 out of 9 cases. In contrast, serum cystatin C levels were comparable between CCA and control groups, although serum cystatin C levels in the BBD group was higher than that in the control or CCA groups. When the serum cathepsin B to cystatin C ratio was calculated, that of the CCA group was significantly higher than that of the control group, and, although statistically not significant, the ratio of CCA group showed a trend to be higher than that of the BBD group. Thus, the cathepsin B to cystatin C ratio might be used as an alternative marker for aiding diagnosis of CCA.

• Journal of Oral Medicine and Pain
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• v.33 no.1
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• pp.35-40
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• 2008

This experiment was designed to clarify the effect of high concentrations of extracellular glucose on the periodontal ligament cells. The cells were incubated for 24 and 48 hours with ${\alpha}-MEM$ including 1,000 mg/L(control group) and 4,500 mg/L(experimental group) of glucose. Then, the expressions of ${\alpha}5$ integrin, cathepsin-B and -L were examined using RT-PCR method. The results were as follows: 1. ${\alpha}5$ integrin expression was increased after incubation in high glucose media. 2. Cathepsin-B expression was increased after the 24-H incubation with high glucose media, but was decreased after the 48-H incubation. 3. The expression of cathepsin-L was decreased by the high glucose media. Theses results suggest that extracellular glucose at high concentration may be attributed to delayed wound healing in diabetes patients through increase in ${\alpha}5$ integrin and decrease in cathepsins, which lead to accumulation of extracellular matrices and adhesion molecules.

• Journal of Microbiology and Biotechnology
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• v.7 no.5
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• pp.333-340
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• 1997

An actinomycetes, KT-10 isolated from ginseng field in Kyongpook, Korea was selected based on its ability to produce a lysosomal cathepsin B inhibitor. The inhibitor purified from the culture supernatant of the isolate KT-10 showed strong inhibitory effects against cathepsin B as well as against papain when the activities were measured using synthetic substrate, ${\alpha}$-N-benzyloxycarbonyl-L-Iysine p-nitrophenyl ester (CLN) or ${\alpha}$-N-benzoyl-D,L-arginine 2-naphthylamide (BANA). The isolate KT-10 was identified as a species of Streptomyces based on its morphological characteristics and chemotaxonomic data. The TAXON program of Ward was used to identify Streptomyces sp. KT-10 as a strain of Streptomyces luteogriseus belong to cluster 18 of the genus Streptomyces with a Willcox probability 0.999388. The cathepsin B inhibitor was presumed to a novel material composed of a polyhydroxylamine.

• Microbiology and Biotechnology Letters
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• v.29 no.1
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• pp.25-30
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• 2001

A strain of Actinomycetes producing cathepis B inhibitor was isolated from soil and identified as Streptomyces misakiensis. The product of S. misakiensis inhibited effectively cathepsis B proteinases as well as trypsin and papain. The cathepsin B inhibitor were largely produced with incubation for 4 days. The S. misakiensis was the most growth with incubation for 5 days. The cathepsin B inhibitor was isolated from the extraction of both with ethanol, ethanol and chlorofrom, and following several column chromatography such as sephadex G-15, silica gel 60 and sephadex LH-20 chromatography. The moleculer weight of purfied inhibitor was 138 dalton.

• Microbiology and Biotechnology Letters
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• v.23 no.5
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• pp.565-572
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• 1995

The aim of the present research program was to develop a strain of actinomycetes producing extracellular cathepsin B inhibitor. Soil samples were collected from various sites in Korea and a number of actinomycetes were isolated from the soil samples by applying various physical and chemical pretreatments. An economical and effective method was developed for the screening of strains producing low molecular weight cathepsin B inhibitor, and consequently a strain (SMF28) among over 700 isolates was selected. Chemotaxonomic and numerical identification were carried out for the isolate. Fifty taxonomic unit characters were tested and the data were analyzed numerically using TAXON program. The isolate was identified as a strain of Streptomyces chromofuscus.