• 제목/요약/키워드: mori

검색결과 1,645건 처리시간 0.027초

상심자추출물의 Peroxynitrite억제 및 염증 촉진 인자 제어 효과 (Inhibitory Effects of Mori Fructus on the Peroxynitrite and Proinflammatory Proteins)

  • 우성호;정지천;신현철
    • 동의생리병리학회지
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    • 제22권6호
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    • pp.1475-1481
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    • 2008
  • This study was to investigate the inhibitory effects of Mori Fructus on the generation of peroxynitrite ($ONOO^-$), nitric oxide (NO) and superoxide anion radical (${\cdot}O_2{^-}$) in the endothelial cells of rat vessels. The aim of this study was to investigate the $ONOO^-$, NO, ${\cdot}O_2{^-}$ scavenging and anti-inflammatory activitives of Mori Fructus. For this study, the fluorescent probes, namely dihydrorhodamine 123 (DHR 123), 4,5-diaminofluorescein (DAF-2) and 2',7'-dichlorodihydrofluorescein diacetate (DCFDA) were used. Western blotting was performed using anti-NF-${\kappa}B$ (p50, p65), anti-COX-2, anti-iNOS antibodies, respectively. Mori Fructus prevented lipopolysaccharide (LPS)-induced cell death in YPEN cells. Mori Fructus inhibited the generation of $ONOO^-$, NO and ${\cdot}O_2{^-}$ in the LPS-treated cells. Mori Fructus inhibited the expression of COX-2 and iNOS genes by means of decreasing the NF-${\kappa}B$ activation. These results suggest Mori Fructus is effective on inhibiting the generation of $ONOO^-$, NO and ${\cdot}O_2{^-}$, and that therefore it might have a potential role as a treatment for the inflammatory process and inflammation-related diseases.

상백피(桑白皮)의 항알레르기성 효과 (Anti-allergic effect of Cortex Mori)

  • 이헌구;이무삼;양문식;이양근;허훈;손영택;전병득
    • 한국응용약물학회:학술대회논문집
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    • 한국응용약물학회 1994년도 춘계학술대회 and 제3회 신약개발 연구발표회
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    • pp.176-176
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    • 1994
  • Moraceae comprise a large family of sixty genera and neary 1,400 specieses, including important groups such as Artocarpus, Morus, and Ficus. In particular, Morus(mulberry) is a small genus of tree and shrubs found in temperate and subtropical regions of the Northern hemishere and has been widely cultivated in China and Korea, In addition, the root bark of mulberry tree have been used as an antiphlogic, diuretic, and expectorant in white medicine, and the crude drug is known as "Sangbaikpi" in Korea. Recently, some papers have been published reporting the hypotensive effect, antiviral effect, antifungal effect, inhibitory effect of cAMP-phosphodiesterase, and anticancer effect of this extract. Little is known about that Cortex mori could have been an antiallergic effect. The purpose of this study was the development of an antiallergic agent with an antiallergic effect from Cortex mori. For this, several in vivo and in vitro experimental models were used. Results are 1) Cortex mori inhibited the compound 48/80-induced degranu-lation, histamine release and calcium uptake of rat peritoneal mast cells, 2) compound 48/80-induced anaphylactic shock and cutaneous reaction were significantly inhibited by pretreatment of Cortex mori, and 3) Cortex mori inhibited the ovalbumin-induced late astmatic reaction. From the above results it is suggested that Cortex mori has some substances with an antiallergic activity. Our final purpose of this study is to develope the new drug with an antiallergic activity from Cortex mori

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Functional analysis of Bombyx mori Decapentaplegic gene for bone differentiation in a mammalian cell

  • Park, Seung-Won;Goo, Tae-Won;Choi, Gwang-Ho;Kang, Seok-Woo;Kim, Sung-Wan;Kim, Seong-Ryul
    • International Journal of Industrial Entomology and Biomaterials
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    • 제27권1호
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    • pp.159-165
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    • 2013
  • Bone morphogenetic proteins (BMPs) belong to the transforming growth factor (TGF-${\beta}$) superfamily and are involved in osteoblastic differentiation. The largest TGF-${\beta}$ superfamily subgroup shares genetic homology with human BMPs (hBMPs) and silkworm decapentaplegic (dpp). In addition, hBMPs are functionally interchangeable with Drosophila dpp. Bombyx mori dpp may induce bone formation in mammalian cells. To test this hypothesis, we synthesized the 1,285-base pairs cDNA of full-length B. mori dpp using total RNAs obtained from the fat body of 3-day-old of the $5^{th}$ instar larvae and cloned the cDNA into the pCEP4 mammalian expression vector. Next, B. mori dpp was expressed in C3H10T1/2 cells. The target cells transfected with the pCEP4-Bm dpp plasmid showed biological functions similar to those of osteogenic differentiation induction growth factors such as hBMPs. We determined the relative mRNA expression rates of Runt-related transcription factor 2 (RUNX2), osterix, osteocalcin, and alkaline phosphatase (ALP) to validate the osteoblast-specific differentiation effects of B. mori dpp by performing quantitative real-time RT-PCR. Interestingly, mRNA expression levels of the 3 marker genes except RUNX2, in cells expressing B. mori dpp were much higher than those in control cells and C3H10T1/2 cells transfected with pCEP4. These results suggested that B. mori dpp signaling regulates osterix expression during osteogenic differentiation via RUNX2-independent mechanisms.

Molecular Cloning, Bioinformatics Analysis and Expression Profiling of a Gene Encoding Vacuolar-type $H^+-ATP$ Synthetase (V-ATPase) c Subunit from Bombyx mori

  • Lu, Peng;Chen, Keping;Yao, Qin;Yang, Hua-Jun
    • International Journal of Industrial Entomology and Biomaterials
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    • 제15권2호
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    • pp.115-122
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    • 2007
  • As the genome of B.mori is available in GenBank and the EST database of B.mori is expanding, identification of novel genes of B.mori is conceivable by data-mining techniques. We used the in silico cloning method to get the vacuolar-type $H^+-ATP$ synthetase (V-ATPase) c subunit (16 kDa proteolipid subunit) gene of B.mori and analysed with bioinformatics tools. The result was confirmed by RT-PCR and sequencing. The V-ATPase c subunit cDNA contains a 468 bp ORF. The ORF encoded a 155-residue protein that showed extensive homology with V-ATPase c subunits from other 15 species and contained four membrane-spanning helices. Tissue expression pattern analysis revealed that V-ATPase c expressed strongly in Malpighian tubules, not in fat body. This gene has been registered in GenBank under the accession number EU082222.

The innate immune response transcription factor Bombyx mori Relish1 induces high-level antimicrobial peptides in silkworm

  • Kim, Seong-Wan;Kim, Seong-Ryul;Goo, Tae-Won;Choi, Kwang-Ho
    • International Journal of Industrial Entomology and Biomaterials
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    • 제37권2호
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    • pp.49-54
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    • 2018
  • To artificially enhance antimicrobial peptide expression in Bombyx mori, we constructed genetically engineered silkworms overexpressing Rel family transcription factor. The truncated BmRelish1 (BmRelish1t) gene contained a Rel homolog domain (RHD), nuclear localization signal (NLS), acidic and hydrophobic amino acid (AHAA)-rich region, and death domain (DD), but no ankyrin-repeat (ANK) domain. The BmRelish1t gene was controlled by B. mori cytoplasmic actin 3 promoter in the PiggyBac transposon vector. Chromosome analysis of G1 generations of a transgenic silkworm with EGFP expression confirmed stable insertion of BmRelish1t. BmRelish1t gene overexpression in transgenic silkworms resulted in higher mRNA expression levels of B. mori antimicrobial peptides such as lebocin(~20.5-fold), moricin(~8.7-fold), and nuecin(~17.4-fold) than those in normal silkworms.

누에에서의 Mariner 유사 전이인자유전자의 동정 (Identification of Mariner-Like Element(MLE) Gene from Nombyx mori.)

  • 이진성;황재삼;김용성;서동상;권오유
    • 생명과학회지
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    • 제8권3호
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    • pp.285-293
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    • 1998
  • 이미 밝혀져 있는 mariner 전이인자의 전이효소를 암호화하는 부위에 대하여 퇴화성 primer를 사용하여 PCR 방법에 의해 누에(Bombyx mori)에서 ariner 유사 전이닌자의 잠정적인 전이효소 부위를 클로닝 하였다. BmoMAR로 망명된 이 PCR 클론으로부터 추론된 아미노산은 152개로 다섯 개의 종결코돈이 삽입되어 있었으며, Drosophila mauritiana의 active Mos 1에 37%의 아미노산 상동성을 보였다. 또한, 기존의 곤충들에서 밝혀진 mariner-like element에 대한 상동성은 DNA 수주에서는 Apis mellifera에 59% 그리고 아미노산 수준에서는 D. mauritiana 7.9 clone에 37% 상동성을 보였다. 이 결과는 mariner-like element가 B. mori에도 존재하고 있지만. 이들 전이인자의 전이효소를 암호화하는 부위에 종결코돈이 발견되는 것으로 보아서 비활성 전이인자 혹은 일존의 selenoprotein으로 추정된다.

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Molecular Cloning of a cDNA Encoding Putative Calreticulin from the Silkworm, Bombyx mori

  • Kim, Seong-Ryul;Lee, Kwang-Sik;Kim, Iksoo;Kang, Seok-Woo;Nho, Si-Kab;Sohn, Hung-Dae;Jin, Byung-Rae
    • International Journal of Industrial Entomology and Biomaterials
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    • 제6권1호
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    • pp.93-97
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    • 2003
  • We describe here the cloning of a cDNA encoding putative calreticulin (CRT) from the silkworm, Bombyx mori. The CRT cDNA comprised of 1,194 bp encoding 398 amino acid residues. B. mori. CRT has a HDEL sequence at the end of the C-domain. The B. morl, CRT showed 88% protein sequence identity to the G. mellonella CRT, 71 % to A. aegypti CRT, and 63% to H. sapiens CRT, Phylogenetic analysis revealed that the deduced amino acid sequences of the B. mori CRT formed a highly inclusive subgroup with other insect CRTs. Northern blot analysis exhibited an expression of the B. mori CRT gene in the fat body, evidencing the fat body as a major site for CRT synthesis.

Isolation of Two cDNAs Encoding a Putative Peptidohlycan Recognition Protein Gene from the Domestic Silkworm, Bombyx mori

  • Kim, Sang-Hyun;Lee, Heui-Sam;Kim, Jin-Won;Lee, Young-Sin;Kim, Iksoo
    • International Journal of Industrial Entomology and Biomaterials
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    • 제4권1호
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    • pp.31-36
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    • 2002
  • Peptidohlycan recognition protein (PGRP) is one of the pattern recognition proteins in innate immunity of insect. We isolated differentially expressed two cDNAa, BTL-LPI and BTL-LP2, in the fat body of Bombyx mori larvae injected with bacteria by subtractive hybridization method. These two clones showed amino acid sequence divergence of 30.4%. In the comparison with other insect PGRP genes, BTL-LP2 showed 48.8% and 45.2% of sequence homology to the known PGRP genes of Bombyx mori and Tricoplusia ni, respectively, and BTL-LP2 was 31.8% and 30.9% , respectively. Phylogenetic analysis showed relatively close relationship of the BTL-LP2 to the known insect PGRP, unlike BTL-LPI, which was equidistant both to insect and mammals, suggesting a divergent relationships of the two newly cloned B. mori PGRP genes. Northern blot analyses confirmed an induction of the expression of BTL-LP2 by the bacterial infection in the Int body of B. mori, suggesting the involvement of the gene in the insect immunity.

STRONG MORI MODULES OVER AN INTEGRAL DOMAIN

  • Chang, Gyu Whan
    • 대한수학회보
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    • 제50권6호
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    • pp.1905-1914
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    • 2013
  • Let D be an integral domain with quotient field K, M a torsion-free D-module, X an indeterminate, and $N_v=\{f{\in}D[X]|c(f)_v=D\}$. Let $q(M)=M{\otimes}_D\;K$ and $M_{w_D}$={$x{\in}q(M)|xJ{\subseteq}M$ for a nonzero finitely generated ideal J of D with $J_v$ = D}. In this paper, we show that $M_{w_D}=M[X]_{N_v}{\cap}q(M)$ and $(M[X])_{w_{D[X]}}{\cap}q(M)[X]=M_{w_D}[X]=M[X]_{N_v}{\cap}q(M)[X]$. Using these results, we prove that M is a strong Mori D-module if and only if M[X] is a strong Mori D[X]-module if and only if $M[X]_{N_v}$ is a Noetherian $D[X]_{N_v}$-module. This is a generalization of the fact that D is a strong Mori domain if and only if D[X] is a strong Mori domain if and only if $D[X]_{N_v}$ is a Noetherian domain.