• 한국수산과학회지
• /
• 제28권5호
• /
• pp.557-568
• /
• 1995

어류의 사후 초기의 변화를 육 및 장기조직중에 분포하는 단백질분해효소의 작용과 관련하여 검토할 목적으로 멸치의 육 및 장기에서 분리한 cathepsin L과 chymotrypsin 및 trypsin의 단백질 기질에 대한 특성과 근원섬유단백질에 대한 분해능을 전기영동적으로 분석하여 다음의 결론을 얻었다. 이들 세 효소의 casein에 대한 친화도는 유사하였고, 근원섬유단백질에 대한 친화도는 casein에 대한 친화도보다 높았다. 멸치와 방어의 근원섬유단백질에 대한 cathepsin L과 chymotrypsin의 활성은 trypsin보다 훨씬 높게 나타났다. $0-25\%$까지의 식염농도에서 세 효소의 단백질분해활성은 식염의 농도에 반비례하였으며, 식염의 공존상태에서 세 효소는 casein 보다 근원섬유단백질에 대하여 높은 활성을 나타내었다. 관원섬유단백질의 효소 분해시에 cathepsin L은 chymotrypsin과 trypsin에 비하여 염농도와 온도에 의한 영향이 적었다. 따라서, 멸치의 사후변화와 젓갈 숙성 중의 자가소화는 trypsin보다는 cathepsin L과 chymotrypsin의 단백질분해활성이 더욱 깊이 관여할 것으로 판단된다.

• BMB Reports
• /
• 제31권6호
• /
• pp.611-614
• /
• 1998

Protein kinase CKII (CKII) is a protein Ser/Thr kinase that is ubiquitously distributed in eukaryotic cells. Although it has been suggested that CKII plays an critical role in cell growth and proliferation, its functional significance and regulation in the cells remain poorly understood. To investigate the exact biological function of CKII, we have identified proteins that interact with the subunits of CKII using the twohybrid system. In this report, we have identified cathepsin L, a lysosomal protease, as a cellular protein capable of interacting with the ${\beta}$ subunit of CKII. Cathepsin L does not interact with the ${\alpha}$ subunit of CKII, supporting the idea that the ${\beta}$ subunit can mediate the interaction of CKII with target proteins. We have found that cathepsin L has several putative CKII phosphorylation sites including Thr-84, Ser-160, Ser-270, Thr-288, and Ser-301. These data suggest that CKII is a possible protein kinase for cathepsin L phosphorylation.

• Journal of Oral Medicine and Pain
• /
• 제33권1호
• /
• pp.35-40
• /
• 2008

고농도 세포외 포도당이 치주인대세포의 integrin 발현과 cathepsin-B 및 -L의 발현에 미치는 영향을 살펴보기 위하여 사람 치주인대로부터 일차배양을 통해 얻은 치주인대세포를 1,000 mg/L 농도의 포도당이 포함된 배양액(대조군)과 4,500mg/L 농도의 포도당이 포함된 배양액(실험군)으로 나누어 24시간과 48시간 배양하였다. 그 후, RT-PCR을 통하여 integrin, cathepsin-B 및 -L의 발현을 평가하여 다음과 같은 결론을 얻었다. 1. 대조군에 비해 실험군에서 ${\alpha}5$ intergrin 발현이 증가하였다. 2. Cathepsin-B는 24시간 배양 실험군에서 발현이 증가하였으나, 48시간 배양후에는 발현이 감소하였다. 3. Cathepsin-L은 24시간과 48시간 배양군 모두에서 대조군에 비해 실험군에서 발현이 감소하였다. 이상의 결과로 보아, 고농도 포도당 조건은 치주인대세포의 integrin 발현을 증가시키며, 이는 세포활성에 영향을 미쳐 치주조직의 재생을 지연시킬 것으로 추측된다. 또한, 이 과정은 cathepsin 발현의 감소로 인해 촉진될 것으로 생각된다.

• 한국축산식품학회지
• /
• 제40권3호
• /
• pp.415-425
• /
• 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.

• Journal of Acupuncture Research
• /
• 제22권3호
• /
• pp.1-12
• /
• 2005

유근피의 ethanol 추출 약침액 (EE-UD)과 수욕 약침액 (WE-UD)은 cathepsin K 와 L의 우수한 억제물로 밝혀졌다. WE-UD는 IC50 수치가 5.32 ${\square}g$/ml일때 cathepsin K를 억제하였고 6.34 ${\square}g$/ml일때 cathepsin L을 억제하였다. 그러나 EE-UD는 cathepsin K와 L을 1.45 ${\square}g$/ml와 2.43 ${\square}g$/ml 수준에서 억제 활동을 보여 WE-UD보다 많은 유의성을 보였다. EE-VD는 0.8 ${\square}g$/ml의 Ki 수치로 cathepsin K에 대하여 우수한 억제물임을 관찰할 수 있었다. 이러한 활동은 분석실험에서도 pH 7.0의 glutathione와 같이 작용하였을때 10배로 늘어났다. 또한 이는 GSH thiolate 음이온의 조합을 지원하므로서 이러한 유효성의 증가는 아마도 효소의 활동 장소로 향한 약침액 배합들의 향상된 화학 작용으로 인한 것으로 사료되었다. WE-UD는 시간 의존적 억제 성을 보임으로서 실험과정 중에 불변의 cathepsin K의 분열과 합성 속도를 알 수 있게 해주었다. 마지막으로 EE-UD는 실험용 쥐의 파골세포와 설치류의 골이 관련된 실험에서 골 재흡수성을 억제함이 입증되었다. WE-UD는 cathepsin K 와 L, 그리고 골의 collagen에서의 단백질 분해를 억제하는 작용이 있음을 증명하였다. 이와 같은 결과들은 cathepsin K로 인하여 유발된 골 손상의 진행을 예방해주는데 효과적인 것임을 강력히 시사하였으며 또한 골수세포들의 골 재흡수 활동에 효과적인 것이라는 결론을 얻었다.

• Food Science and Biotechnology
• /
• 제18권1호
• /
• pp.84-88
• /
• 2009

Cathepsin S is a cysteine protease that affects extracellular matrix remodeling. Recently, several studies have reported that cathepsin S is involved in obesity. Both mouse and human adipose cells produce this enzyme in the early phase of adipocyte differentiation, where it degrades fibronectin. Cathepsin S gene expression is elevated in the adipose tissue of obese mice as compared to that of lean mice. Paecilomyces tenuipes water extracts (PTW) are shown to have an inhibitory effect on cathepsin S activity. In this study, Z-Val-Val-Arg-MCA was used as a cathepsin S-specific substrate in order to examine inhibitory effect of PTW. Supplementing 3T3-L1 cell media with PTW clearly reduced lipid droplet accumulation and cathepsin S-induced adipogenesis. Furthermore, PTW decreased weight gain, subcutaneous adipose tissue growth, the level of serum triglyceride, and total cholesterol in mice fed a high-fat diet. These data suggest that PTW work against adipose cathepsin S and presumably contribute to anti-obese activities.

• 한국미생물·생명공학회지
• /
• 제27권6호
• /
• pp.458-465
• /
• 1999

Streptomyces luteogriseus KT-10 isolated from Korean farm soil produced a strong cathepsin B inhibitor. Optimal conditions for the cathepsin B inhibitor production by s. luteogriseus KT-10 were evaluated. The cathepsin B inhibitor was produced with maximal yield in the cultural condition of pH 7.0 and $25^{\circ}C$ for 4 days. Optimal medium for the cathepsin B inhibitor production was determined to be a medium containing 20g, peptone 3g, yeast extract 1g, K2HPO4 0.5g, MgSO4.7H2O 0.5g, NaNO3 0.5g, NaCl 0.5g per l. The cathepsin B inhibitor produced by S. luteogriseus KT-10 could also inhibit the other proteinases such as trypsin, papain, and cathepsin D.

• Journal of Acupuncture Research
• /
• 제22권2호
• /
• pp.71-81
• /
• 2005

Objective : Dear antler (Cervus korean TEMMINCK var. mantchuricus Swinhoe) used for traditional immunosuppressive and immuno-activating action. The effect of deer antler herbal-acupuncture(DAH) solution, prepared by water extract method, on cathepsin activities in bone tissues (cartilage and synovial) cells from mouse rheumatoid arthritis (RA) model was studied. The cysteine endoprotease cathepsin mediates degradation of the MHC class II invariant chain (Ii) in human and mouse antigen-presenting cells. The studies described here examine the functional significance of cathepsin inhibition on autoantigen presentation and organ-specific autoimmune diseases in a murine model for RA. Methods : An animal model for RA in BALB/c mice thymectomized 3 days after birth (3d-Tx) was constructed All 3d-Tx BALB/c mice developed autoimmune lesions in the bone tissue cells, starting at 3 weeks of age, and the disease mediated by CD4+ T cells was chronic and progressive. Significant inhibitory effects of DAH solution on cathepsin S and L were observed in each organ in a dose-dependent manner. Moreover, we confirmed that cathepsin S and L activity in each organ were clearly inhibited by DAB solution. When we examined the inhibitory effects of DAH solution against autoantigen-specific T cell responses in vitro, in regional lymph node cells, but not in spleens, from model mice, a significant inhibitory effect of DAB solution was observed in a dose-dependent manner. DAH solution do not block T cell proliferation to Con A, indicated that the dose of DAB solution 10 to $20\;{\mu}g/m{\ell}$ was sufficient to inactivate the autoantigen-specific T cell responses in vitro. In vivo therapeutic effects of DAB solution were examined in a murine model for RA, autoantigen-specific (C-II-specific) T cell response were significantly inhibited in LNCs from DAH solution-treated mice. Results : Iinhibition of cathepsin S and L in vivo alters autoantigen presentation and development of organ-specific autoimmunity in RA model. Conclusion : These data identify selective inhibition of cysteine protease cathepsin S and L as a potential therapeutic strategy for autoimmune disease process such RA. Thus, DAH solution will served as a potent anti-inflammatory and anti-arthritic agents for treatment of human RA.

• Journal of Microbiology and Biotechnology
• /
• 제7권5호
• /
• pp.333-340
• /
• 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.

• 수산해양교육연구
• /
• 제28권4호
• /
• pp.903-912
• /
• 2016

Hagfish which belongs to the chordate contact cyclostomata, is important phylogenetic relationship between vertebrate and invertebrate. Cathepsins of the cysteine protease family have traditionally been thought to play a major role in intracellular protein degradation and turnover in lysosomes. In this study, Catepsin L was cloned from Inshore hagfish (Eptatretus burgeri), the cDNA encoding ORF of the Eptatretus burgeri Cathepsin L (EbCtL) is 978 bp. The cDNA encoding proEbCtL was expressed in Escherichia coli strain BL21(DE3) using the pGEX-4T-1 expression vector system. The recombinant proEbCtL protein was overexpressed as a approximately 55 kDa fusion protein. The overproduced soluble GST-fusion protein was then applied to glutathione-Sepharose 4B column chromatography; the sample harboring the fusion protein evidenced a high degree of purity when analyzed via SDS-PAGE and Western blot analysis. Its activity was quantied by cleaving the synthetic peptide Z-FR-AMC, Z-LLE-AMC, and Suc-AAF-AMC, and the optimal pH for the protease activity was 8, 9.5, and 9, respectively.