• Journal of Physiology & Pathology in Korean Medicine
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• v.17 no.3
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• pp.633-642
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• 2003

A pain is the symptom which defends against noxious stimulus about a human body, it is known that if the periphery of perceptive nerve were stimulated by a physical or chemical factors, the stimulation is induced by transmission to pain center in the cerebral cortex according to pain conduction tract. The treatment of pain is to decrease a stimulus that causes a pain or block off a nerve transmitting a stimulus or puts on a way to calm down pain center, but It is for adjustment of a pain to be the most representative in acupuncture among various ways to cure a pain in Oriental medicine. However, the analgesic effect of an individual response to acupuncture stimulation shows marked individual variations, so these days genetic a few approach is attempted. On this the author determined that the responding group was appointed those whose tail flick latency (TFL) responding time delayed the minimum of 30 % comparing with basal reaction time. For those whose TFL time had shorter than 30 % was grouped as a non-responding group. And then the hypothalamus of each group was dissected and RNA was further purified. After synthesizing cDNA using oligo dT primer, products were finally applied to the PCR. The results were as follows; The ratio of responding group to non-responding group was 6:4. Ach T (acetylcholinesterase T subunit), BF-I (Brain factor-I), DBH (Dopamine β-hydroxylase) and PNM (Phosphotidylethanolamine N-Methyltransferase) were revealed significantly in the responding group. Cathepsin B and Tau were revealed significantly in the non-responding group. The PCR results show that Ach T, BF-I, DBH and PNM are expressed abundantly in the responding group, where as cathepsin B and tau are abundant in the non-responding group. These results suggest that the analgesic effect on acupuncture stimulation is related to regulation of neurotransmitter as well as neurodegeration of cerebrum.

• Journal of the korean academy of Pediatric Dentistry
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• v.36 no.4
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• pp.619-624
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• 2009

Pyknodysostosis(PKND) is a rare sclerosing bone disorder that has an autosomal recessive trait, also known as Toulouse-Lautrec syndrome. Deficiency of the cathepsin enzyme K in the osteoclasts of PKND patients results in continuous endosteal bone deposits without osteoclastic resorption or remodeling. This causes a generalized increase in sclerosis and fragility of bones. Osteomyelitis in the mandible and recurrent fracture of the long bones are characteristic complicatons of PKND. The patients present typical features of PKND, such as short stature under 150 cm, open cranial suture and fontanelle, club-shaped phalanges, and underdevelopment of midface. This is a case of a 7-year-old girl with PKND, who visited our clinic with the chief complaint of anterior Open-bite and generalized crowding. The patient had been diagnosed as PKND by an orthopedist and manifested characteristic clinical and radiographic features, such as open cranial suture and fontanelle, obtuse madibular gonial angle, frontal and occipital bossing, grooved palate, club-shaped phalanges, and short stature. Orthodontic treatment was not considered because patients with PKND show abnormal bone resorption and remodeling. Instead, removal of deciduous teeth near exfoliation and TFA were performed, and periodic check-up is planned to maintain good oral hygiene.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2005.11a
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• pp.30-30
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• 2005

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2005.11a
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• pp.31-31
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• 2005

• Parasites, Hosts and Diseases
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• v.57 no.6
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• pp.671-680
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• 2019

Cathepsin D (CatD, EC 3.4.23.5) is a member belonging to the subfamily of aspartic endopeptidases, which are classified into the MEROPS clan AA, family A1. Helminth parasites express a large set of different peptidases that play pivotal roles in parasite biology and pathophysiology. However, CatD is less well known than the other classes of peptidases in terms of biochemical properties and biological functions. In this study, we identified 2 novel CatDs (CsCatD1 and CsCatD2) of Clonorchis sinensis and partially characterized their properties. Both CsCatDs represent typical enzymes sharing amino acid residues and motifs that are tightly conserved in the CatD superfamily of proteins. Both CsCatDs showed similar patterns of expression in different developmental stages of C. sinensis, but CsCatD2 was also expressed in metacercariae. CsCatD2 was mainly expressed in the intestines and eggs of C. sinensis. Sera obtained from rats experimentally infected with C. sinensis reacted with recombinant CsCatD2 beginning 2 weeks after infection and the antibody titers were gradually increased by maturation of the parasite. Structural analysis of CsCatD2 revealed a bilobed enzyme structure consisting of 2 antiparallel β-sheet domains packed against each other forming a homodimeric structure. These results suggested a plausible biological role of CsCatD2 in the nutrition and reproduction of parasite and its potential utility as a serodiagnostic antigen in clonorchiasis.

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2003.10a
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• pp.105-105
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• 2003

• Korean Journal of Medicinal Crop Science
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• v.7 no.3
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• pp.185-192
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• 1999

Four different parts of Hovenia dulcis $T_{HUNB}$; fruit, bark, vessel area, fruit coat were extracted with water and ethanol. The ethanol extracts of bark, fruit coat and fruit were fractionized into diethyl ether, chloroform and aqueous partitions. Ethanol extract of fruit coat increased the activity of cathepsin B up to 55 %, which can enhance the alcohol dehydration in the liver. The ethanol extracts was more effective than water extracts against the growth of Hep3B, MCF7. The ethanol extracts of bark (0.5mg/ml) inhibited 90% the growth of MCF7. Each extracts and fractions (0.5mg/ml) did not show considerable cytotoxicity on HEL299. In overall, most of the fractions had similar effects to ethanol extracts; however, diethyl ether and chloroform fractions had higher bioactivity than ethanol extracts, but aqueous fraction.

• Korean Journal of Medicinal Crop Science
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• v.7 no.4
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• pp.263-268
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• 1999

It was found that the level of alcohol concentration in both mouse and human sera can be significantly decreased up to 42% by oral administration of the mixtures of the extracts of Hovenia dulcis THUNB and Alnus japonica Steud. A single treatment of extract from Hovenia dulcis reduced the serum alcohol concentration to 32%, compared to 13% in treating the extract of Alnus japonica. Similar patterns were observed in enhancing alcohol dehydrogenase (ADH) and glutathion-S-transferase (GST) activity in the liver. The inhibition of cathepsin activity was also greatly reduced by administrating the mixture of both extracts : however, the extract of Alnus japonica did not affect the acitivity of cathepsin. It was concluded that the mixture of both extracts had synergic effect on reducing serum alcohol concentration and improving the detoxification process due to alcohol administration in the liver.

• International Journal of Industrial Entomology and Biomaterials
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• v.9 no.2
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• pp.217-223
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• 2004

A cathepsin L-like cysteine protease, v-cath, encoded by the baculovirus has been shown to playa role in host liquefaction. We have identified a v-cath gene in the silkworm virus, Bombyx mori nuclear polyhedrosis virus (BmNPV) K1 strain. The 969 bp v-cath has an open reading frame of 323 amino acids. A putative cleavage site and catalytic sites were conserved in BmNPV-K1 v-cath. The predicted three-dimensional structure of BmNPV-K1 v-cath revealed that the overall fold of BmNPV-K1 v-cath is similar to that of other proteases of the papain family. The deduced amino acid sequence of BmNPV-K1 v-cath showed 98% and 97% protein sequence identity to BmNPV T3 strain and to Autographa californica nuclear polyhedrosis virus, respectively. The BmNPV-K1 v-cath differed at 4 amino acid positions from BmNPV T3. The v-cath gene in BmNPV-K1 genome is located on the EcoRV 6 kb and XhoI 9 kb fragments. Northern hybridization analysis of BmNPV K1 v-cath gene revealed that it is expressed late in infection.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.29 no.3
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• pp.296-308
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• 1996

Proteolytic enzymes responsible for post-mortem degradation of the fish tissues have been studied in regard with screening the proteases distributed in the fish body by reacting with the specific synthesized substrates. Activities of cathepsin L, B, H, G, and D like enzymes were detected in the muscle crude protease from the both kind of fish, dark fleshed fish (anchovy, Engraulis japonica, and gizzard-shad, Clupanodo punctatus) and white fleshed fish (seabass, Lateolabrax japonicus, and sole, Pleuronichthys cornutus), however, those of chymotrypsin, trypsin, pepsin, and peptidase like enzymes were observed 3n the viscera crude pretense from the fish. Proteolytic activities of the muscle crude protease at pH 6.0 were similar to those of the viscera crude protease at pH 8.0, but, those of the viscera crude protease at pH 8.0 were about 2 times higher than those at pH 6.0. The muscle and viscera crude protease from anchovy showed the strongest proteolytic activity among the four fish crude proteases and the proteolytic activity of the viscera crude protease was approximately 100 times higher than that of the muscle crude protease, which suggest that viscera proteases were more contributed on the development of post-mortem changes than muscle proteases. With the degradation patterns on SDS-polyacrylamide gel electrophoresis against yellowtail myofibrillar proteins, the muscle and viscera crude protease of the four fishes were primary responsible for the degradation of myosin heavy chain, and myosin light chain and actin, respectively.