• Title/Summary/Keyword: proteinase inhibitor

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Discovery of New Proteinase Inhibitor for the Treatment of Osteoporosis

  • 손문호
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 2001.04a
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    • pp.89-99
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    • 2001
  • ■ Cathepsin K is a attractive target for selectively and efficiently modulating the osteoclastic bone resorption. ■ OST-1857 is a lead compound which is specifically targeted to cathepsin K and showed efficacy in TPTX rats. ■ OST-compounds are in process of the preclinical study, joined by Yuhan research center.

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Nucleotide Sequence of a Proteinase Inhibitor I Gene in Potato (감자에 존재하는 단백질분해효소 억제제 I 유전자의 염기서열)

  • 이종섭
    • Journal of Plant Biology
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    • v.32 no.2
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    • pp.67-78
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    • 1989
  • Hybridization of DNA isolated from leaves of Russet Burbank potato with tomato cDNA as a probe revealed the presence of about ten inhibitor 1 genes in the genome. Screening of a genomic library of Russet Burbank potato resulted in isolation of seven different genomic clones carrying inhibitor I genes. One of the genomic clones, clone 2, contained two EcoRI fragments of 3.4 and 1.8 kb in size, respectively, which were hybridized with the probe. The nucleotide sequence of parts of the hybridizing EcoRI fragments revealed that they contain a complete gene which codes for an open reading frame of 107 amino acids. It is interrupted by two intervening sequences of 502 and 493 bp, situated at the positions of codons 17 and 43, respectively, of the open reading frame. Putative regulatory sequences, TATAAA and CCACT, were found at the 5' flanking region. In addition, a copy of a 100 bp repeat found at a tomato inhibitor I gene was identified.

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Inhibition of Various Proteases by MAPI and Inactivation fo MAPI by Trypsin

  • Lee, Hyun-Sook;Kho, Yung-Hee;Lee, Kye-Joon
    • 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.

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Phenotypic Alterations in Transgenic Tobacco Plants that Overproduce Cytokinins (Cytokinins overproduction에 따른 담배형질전환체의 변화)

  • Chung, Yong-Yoon
    • The Journal of Natural Sciences
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    • v.10 no.1
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    • pp.33-37
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    • 1998
  • Cytokinin is one of major growth regulators in plants. In this study, the gene isopentenyl transferase (jpt) which encodes a key enzyme involved in the biosynthesis of the growth regulator cytokinin isolated from Agrobacterium tumefaciens was introduced ito tobacco plant via Agrobacterium-mediated transformation. The jpt gene was modulated using the proteinase inhibitor II (PI-IIK) promotor. In general, this promoterlipt gene fusion resulted in overproduction of cytokinins throughout the transgenic plants. The overproduction of cytokinin caused dramatic changes in morphology of the plant, including stem thickness and reduced root development. The studies reported in this paper were initiated to examine the consequences of overproduction of cytokinin in plant.

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Degradation of human immunoglobulins and cytotoxicity on HeLa cells by live Trichomonas vaginalis (질편모충 단백질분해효소의 세포독성 및 인체면역글로불린 분해능)

  • 민득영;류재숙
    • Parasites, Hosts and Diseases
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    • v.35 no.1
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    • pp.39-46
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    • 1997
  • The present study was undertaken to determine whether live T. uaginnlis degrades human secretory IgA, serum If and IgG molecules. Human immunoglobulins were exposed to live trophozoites, parasite Iysate, and excretory-secretory product (ESP) of T ucginnlis. To determine the fragmentation of immunoglobulins, the reaction sample was subjected to SDS-PAGE and EITB, and peroxidase conjugated antihuman IgA and IgG were used as probes. Live trophozoites degraded secretory IgA, serum IgA and IgG, and degradation were pressed forward by the prolongation of the incubation time and by increasing the number of trichomonads respectively. Also the Iysates and ESP of trichomonads degraded IgA and IgG. The cysteine and serine proteinase inhibitors such as I-64, antipain, iodoacetic acid, iodoacetamide, TLCK reduced the ability of cleaving immunoglobulins. The proteinase activity and cytotoxicity of T. uaginnlis to HeLa cells were decreased when live T. vusinalis was treated with metallo-proteinase inhibitor as well as cysteine and serine proteinase inhibitors. These results suggest that proteinase secreted from live T ucginclis may play a part role in host pathogenesis by T. uosinnlis, and the cleaving ability of host immunoglobulins by the proteinase may contribute as a one of immune evasion mechanism for parasite survival in the host.

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Purification and characterization of a trypsin inhibitor from egg of skipjack tuna, Katsuwonus pelamis

  • Kim, Se-Kwon;Park, Joung-Ho;Je, Jae-Young
    • Proceedings of the Korean Society of Fisheries Technology Conference
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    • 2001.05a
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    • pp.148-149
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    • 2001
  • Protein inhibitors are proteins or peptides capable of inhibiting catalytic activities of proteolytic enzymes. They are grouped primarily as either serine, cysteine, aspartic or metallto-proteinase inhibitors. Pretense inhibitors have been hewn since the end of the last century in nematodes and human blood serum, and their ubiquitous distribution in microorganisms, animals and plants has been widely documented. (omitted)

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Gene Expression upon Development of In Vitro Potato Microtuber (감자 기내 소괴경 발달에 따른 유전자 발현)

  • 홍주봉
    • Proceedings of the Botanical Society of Korea Conference
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    • 1987.07a
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    • pp.309-321
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    • 1987
  • Differential gene expressions of patatin, proteinase inhibitor II, PAPI, rbcS and actin in potato microtuber have been examined. Microtubers from the several different stages of development were collected and their protein and mRNA patterns were examined. SDS-PAGE of microtuber proteins revealed that developmental changes in protein should be analogous to that of potatoes grown in the field. The level of patatin mRNA was the highest at the 30th day of development. Proteinse inhibitor IImRNA level was at the highest at the 15th day and decreased thereafter. The levels of PAPI mRNA, rbcS mRNA and actin mRNA were low throughout the time course examined.

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Characterization of F2 Progenies of Wound Minus Arabidopsis Mutant Crossed with Wild Type Plant

  • Park, Sanggyu
    • Journal of Applied Biological Chemistry
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    • v.43 no.1
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    • pp.12-17
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    • 2000
  • To understand the signal transduction pathway that leads to the activation of the wound-inducible proteinase inhibitor II (pin2) promoter. $F_2$ progenies of wound (-) mutant crossed with wild-type Arabidopsis plants were biochemically and genetically characterized. Wound (-) mutant was derived from transgenic Arabidopsis plants containing bacterial cytosine deaminase gene under the control of pin2 promoter. The cytosine deaminase assays indicated that wound (-) mutant is a dominant inhibitor of wound-inducibility as only 3 of the $20F_2$ progenies showed cytosine deaminase (CDase) activity, To construct a structural map of the wound (-) mutant chromosomal regions, cleaved, amplified polymorphic sequences (CAPS) markers that cover all Chromosomes were used. Chromosomal regions covered by three different CAPS markers could be candidates for further fine mapping of the location of the wound (-) mutation. g4026, RGA1 and ASA1 located at 84.9 on recombinant inbred (RI) map of chromosome I, at 1.75 on RI map of chromosome II, and 18.35 on RI map of chromosome V, respectively.

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