• 제목/요약/키워드: GGX

검색결과 3건 처리시간 0.017초

만성폐쇄성폐질환 동물모델에서 GGX의 폐손상 억제 효과 (Inhibitory Effects of GGX on Lung Injury of Chronic Obstructive Lung Disease (COPD) Mice Model)

  • 김태현;양원경;이수원;김승형;유이란;박양춘
    • 대한한의학회지
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    • 제42권3호
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    • pp.56-71
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    • 2021
  • Objectives: This study is aimed to evaluate the protective effects of GGX on lung injury of Chronic Obstructive Lung Disease (COPD) mice model. Materials and Methods: C57BL/6 mice were challenged with lipopolysaccharide (LPS) and cigarette smoke extract (CSE) and then treated with vehicle only (Control group), dexamethasone 3 mg/kg (Dexa group), gam-gil-tang 200 mg/kg (GGT group), GGX 100, 200, and 400 mg/kg (GGX group). After sacrifice, its bronchoalveolar lavage fluid (BALF) or lung tissue was analyzed with cytospin, Enzyme-Linked Immunosorbent Assay (ELISA), real-time polymerase chain reaction (PCR) and hematoxylin & eosin (H&E), and Masson's trichrome staining. Results: In the COPD model, GGX significantly inhibited the increase of neutrophils, TNF-𝛼, IL-17A, CXCL-1, MIP2 in BALF and TNF-𝛼, IL-1𝛽, IL-10 mRNA expression in lung tissue. It also decreased the severity of histological lung injury. Conclusion: This study suggests the usability of GGX for COPD patients by controlling lung tissue injury.

Ovalbumin으로 유발된 천식 동물모델에서 GGX의 효과 (Effects of GGX on an Ovalbumin-induced Asthma Mice Model)

  • 김태현;양원경;이수원;우성천;김승형;박양춘
    • 대한한방내과학회지
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    • 제44권3호
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    • pp.294-312
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    • 2023
  • Objective: The purpose of this study is to evaluate the effects of GGX on an ovalbumin (OVA)-induced asthma mice model. Methods: Balb/c mice were challenged with OVA and then treated with three concentrations of GGX (100, 200, and 400 mg/kg). After sacrifice, the bronchoalveolar lavage fluid (BALF) or lungs of the mice were analyzed by fluorescence-activated cell sorting, ELISA, real-time PCR, H&E, Masson's trichrome, PAS and AB-PAS staining, and immunohistofluorescence staining. Results: GGX significantly inhibited the increase of total cells, immune cells (lymphocyte, neutrophils, macrophage, CD4+, CD8+, CD4+CD69+, CD62L-CD44high+, Gr-1+SiglecF-), and the expression of cytokines (IL-4, IL-5, IL-13, IFN-γ) in BALF. It also significantly inhibited the increase of total cells, immune cells (lymphocyte, neutrophils, eosinophil/macrophage, CD3+, CD19+, CD3+CD193+, CD4+, CD8+, CD4+CD69+, CD62L-CD44high+, and Gr-1+SiglecF-), and the expression of IL-13, TARC, and MCP-1 in lung tissue. GGX decreased the severity of histological lung injury and the expressions of STAT3 and GATA3. Conclusion: This study suggests the probability of using GGX for the treatment of asthma by inhibiting inflammatory immune response.

Characterization of a Novel Alkaline Family VIII Esterase with S-Enantiomer Preference from a Compost Metagenomic Library

  • Lee, Hyun Woo;Jung, Won Kyeong;Kim, Yong Ho;Ryu, Bum Han;Kim, T. Doohun;Kim, Jungho;Kim, Hoon
    • Journal of Microbiology and Biotechnology
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    • 제26권2호
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    • pp.315-325
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    • 2016
  • A novel esterase gene, est7K, was isolated from a compost metagenomic library. The gene encoded a protein of 411 amino acids and the molecular mass of the Est7K was estimated to be 44,969 Da with no signal peptide. Est7K showed the highest identity of 57% to EstA3, which is an esterase from a drinking water metagenome, when compared with the enzymes with reported properties. Est7K had three motifs, SMTK, YSV, and WGG, which correspond to the typical motifs of family VIII esterases, SxxK, Yxx, and WGG, respectively. Est7K did not have the GxSxG motif in most lipolytic enzymes. Three additional motifs, LxxxPGxxW, PLGMxDTxF, and GGxG, were found to be conserved in family VIII enzymes. The results of the phylogenetic analysis and the alignment study suggest that family VIII enzymes could be classified into two subfamilies, VIII.1 and VIII.2. The purified Est7K was optimally active at 40ºC and pH 10.0. It was activated to exhibit a 2.1-fold higher activity by the presence of 30% methanol. It preferred short-length p-nitrophenyl esters, particularly p-nitrophenyl butyrate, and efficiently hydrolyzed glyceryl tributyrate. It did not hydrolyze β-lactamase substrates, tertiary alcohol esters, glyceryl trioleate, fish oil, and olive oil. Est7K preferred an S-enantiomer, such as (S)-methyl-3-hydroxy-2-methylpropionate, as the substrate. The tolerance to methanol and the substrate specificity may provide potential advantage in the use of the enzyme in pharmaceutical and other biotechnological processes.