• The Plant Pathology Journal
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• v.24 no.4
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• pp.367-374
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• 2008

The genomes of plants contain more than 600 genes encoding a diverse set of proteases and the subunits of proteasomes. These proteases and proteasomes consist of plant proteolytic systems, which are involved in various cellular metabolic processes. Plant proteolytic systems have been shown to have diverse roles in defense responses, such as execution of the attack on the invading organisms, participation in signaling cascades, and perception of the invaders. In order to provide a framework for illustrating the importance of proteolytic systems in plant defense, characteristics of non-proteasome proteases and the 26S proteasome are summarized. The involvement of caspase-like proteases, saspases, apoplastic proteases, and the 26S proteasome in pathogen defense suggests that plant proteolytic systems are essential for defense and further clarity on the roles of plant proteases in defense is challenging but fundamentally important to understand plant-microbe interactions.

• Journal of Microbiology
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• v.33 no.4
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• pp.344-349
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• 1995

The alkalophilic bacterium, Xanthomonas sp. JK311, producing extracellular proteases, was isolated from soil. Xanthomonas sp. JK311 produced five extracellular proteases that are all metalloproteases. Four of them were resistant against 1% SDS. Chromosomal DNA of the Xanthomonas sp. JK311 was digested with BamHI and cloned into PUC19. Among E. coli strain HB101 transformants, a clone secreting the proteases was screened through halo formation on skim-milk agar plate and by Southern blot analysis. It had the recombinant plasmid pXEP-1 containing the 7.5 kb-BamHI DNA fragment and produced three extacellular proteases. Their protease properties corresponded to those of Xanthomonas sp. JK311.

• Ocean and Polar Research
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• v.30 no.4
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• pp.467-472
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• 2008

Antarctic krill has a strong proteolytic enzyme system, which comes from a combination of several proteases. This powerful activity can be easily detected by krill's superior post mortem autolysis. Mammalian skin consists of epidermis and dermal connective tissue, and functions as a barrier against threatening environments. A clot in a wound site of the skin should be removed for successful skin regeneration. Epithelial cells secrete proteases to dissolve the clot. In previous studies Antarctic krill proteases were purified and characterized. The proteolytic enzymes from Antarctic krill showed higher activity than mammalian enzymes. It has been suggested that these krill clean up the necrotic skin wound to induce a natural healing ability. The enzymes exhibited additional possibilities for several other biomedical applications, including dental plaque controlling agent and healing agent for corneal alkali burn. Considering that these versatile activities come from a mixture of several enzymes, discovering other proteolytic enzymes could be another feasible way to enhance the activity if they can be used together with krill enzymes. Molecular cloning of the krill proteases should be carried out to study and develop the applications. This review introduces possible roles of the unique Antarctic krill proteases, with basic information and suggestion for the development of an application to skin regeneration.

• Korean Journal of Microbiology
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• v.30 no.6
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• pp.501-506
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• 1992

An alkalophilic Vibrio sp. RH530 showing high proteolytic activity was isolated form soil samples by enrichment culture. The activity staining using gelatin SDS- polyacrylamide gel electrophoresis (PAGE ) revealed that the strain produced an alkaline major protease (Apr B) with a size of 27 kDa, and at least six minor proteases. The apparent sizes of four of the minor proteases were approximately 45, 28, 22 and 19 kDa. Apr B and five of the minor proteases were inhibited by serine protease inhibitors including PMSF and DFP, suggesting that they are serine proteases. One of the minor proteases was inhibited by metalloprotease inhibitors, not by serine protease inhibitors, indicating it to be a metalloprotease. Furthermore, the activities of Apr B and Prt 3 were not inhibited by SDS in the reaction mixture. The production of Apr B and some of the minor proteases was specifically affected by culture temperature (30 to 37.deg.C) and pH (7 to 10). The production of Apr B. Prt 2, Prt 5 and Prt 6 was mainly affected by culture temperature, while Prt 4 by culture pH. Prt 1 and Prt 3 were not affected by neither of these factors.

• Asian Pacific Journal of Cancer Prevention
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• v.16 no.18
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• pp.8047-8052
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• 2016

Proteases are important molecules that are involved in many key physiological processes. Protease signaling pathways are strictly controlled, and disorders in protease activity can result in pathological changes such as cardiovascular and inflammatory diseases, cancer and neurological disorders. Many proteases have been associated with increasing tumor metastasis in various human cancers, suggesting important functional roles in the metastatic process because of their ability to degrade the extracellular matrix barrier. Proteases are also capable of cleaving non-extracellular matrix molecules. Inhibitors of proteases to some extent can reduce invasion and metastasis of cancer cells, and slow down cancer progression. In this review, we focus on the role of a few proteases and their inhibitors in tumors as a basis for cancer prognostication and therapy.

• Parasites, Hosts and Diseases
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• v.40 no.2
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• pp.89-92
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• 2002

The cysteine proteases of Paragonimus westermani metacercariae are involved in metacercarial excystment, host immune modulation, and possibly in tissue penetration. In order to clarify the origin of the enzymes, 28 and 27 kDa cysteine proteases in metacercarial excretory-secretory products were purified through the FPLC system using Mono Q column chromatography. The polyclonal antibodies to the enzymes were produced in BALB/c mice. Immunolocalization studies revealed that both cysteine proteases were distributed at the linings of excretory bladder and excretory concretions of the metacercariae. It was suggested that the excretory epithelium of P. westermani undertake the secretory function of metacercarial cysteine proteases, in addition to its role as a route for eliminating waste products.

• Journal of Microbiology
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• v.42 no.2
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• pp.156-159
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• 2004

In general, the salinity of the ocean is close to 3.5％ and marine vibrios possess the respiratory chain-linked Na$\^$+/ pump. The influence of sodium chloride and the proton conductor carbonylcyanide m-chlo-rophenylhydrazone (CCCP) on the production of extracellular proteases in a marine Vibrio strain was examined. At the concentration of 0.5 M, sodium chloride minimally inhibited the activity of extra-cellular proteases by approximately 16％, whereas at the same concentration, the producton of extra-cellular proteases was severely inhibited. On the other hand, the production of extracellular proteases was completely inhibited by the addition of 2 ${\mu}$M CCCP at pH 8.5, where the respiratory chain-linked Na$\^$+/ pump functions.

• Journal of Microbiology and Biotechnology
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• v.10 no.2
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• pp.181-186
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• 2000

MAPI (microbial alkaline protease inhibitor) was isolated from cultrue broth of Streptomyces chromofuscus SMF28. The Ki values of MAPI for the representative serine proteases such as chymotrypsin and proteinase K were 0.28 and $0.63{\;}\mu\textrm{M}$, respectively, and for the cysteine proteases cathepsin B and papain were 0.66 and $0.28{\;}\mu\textrm{M}$, respectively. These data indicate that MAPI is not a potent selective inhibitor of serine or cysteine proteases. Progress curves for the inhibition of three proteases by MAPI exhibithe characteristic patterns; MAPI exhibited slow-binding inhibition of cathepsin B. It was rapidly associated with chymotrypsin before the addition of substrate and then reactivation of MAPI-inhibited enzyme was investigated in the presence of substrate. On the other hand, MAPI-proteinase K interaction was typical for those classical inhibitors. When MAPI was incubated with trypsin, there was an extensive reduction in the ingibitory activities of MAPI corresponding to 66.5% inactivation of MAPI, indicating that trypsin-like protease may play a role in the decrease of the inhibitory activity during cultivation.

• The Korean Journal of Food And Nutrition
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• v.20 no.4
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• pp.378-383
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• 2007

To study the characteristics and processing of Kochujang which is rapidly fermented by commercial enzymes, three kinds of Kochujang(KP-FA, KP-FN, and KP-BN) using commercial proteases and one Kochujang(KM) using Meju were prepared and their qualities investigated. There were only small differences in pH and acidity between each Kochujang. The moisture contents were high tendency in the three kinds of Kochujangs using the commercial proteases at 20 days of fermentation. Reducing sugars had a tendency to decrease during the fermentation in the Kochujangs using the proteases. During the first half of fermentation, the Kochujangs made with proteases showed higher amino nitrogen contents than the Kochujang(KM) made using Meju. Acidic protease activity was high in KP-FA at 20 days of fermentation and neutral protease activity was high in KP-FN and KP-BN at the beginning of fermentation. The Kochujangs made using the proteases, through 20 days of fermentation, obtained high preference in the sensory evaluation for color, texture, and overall acceptability. However, the hot taste was stronger in these Kochujangs during the fermentation.

• Proceedings of the PSK Conference
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• 2002.10a
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• pp.332.2-333
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• 2002

Three alkaline proteases. designated JB-1. JB-2, and JB-3, are extracellular enzymes produced by Bacillus spp. JB411 which was isolated korean soil. They were separated by DEAE-sepharose CL-6B gel. and further purified using ammonium sulfate precipitation. ultra membrane filtration. and Ultrogel AcA gel filtration. The optimun pH values of proteases IB-1. JB-2. and JB-3. were shown to be 9.5. 9.5 and 7.5. respectively. All three proteases were stable in the pH range of 5-11. (omitted)