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1.
J Ethnopharmacol ; 106(2): 279-84, 2006 Jun 30.
Article in English | MEDLINE | ID: mdl-16580800

ABSTRACT

The purpose of this study is to assess the protective effects exerted by Schisandra fructus (SF) on hyaluronidase (HAase) and the recombinant human interleukin-1beta (IL-1beta) induced matrix degradation in human articular cartilage and chondrocytes. The effect of SF on the matrix gene expression of immortalized chondrocyte cell line C-28/I2 treated with HAase was investigated using a reverse transcription polymerase chain reaction (RT-PCR). In addition, the effects of SFEA on HAase and IL-1beta induced matrix degradation in human articular cartilage were assessed using a staining method, and the quantity of glycosaminoglycan (GAG) degraded was calculated from the cultured media. In HAase treatment group, the released GAGs content increased significantly to 15.8+/-0.7 microg, compared with control levels (5.0+/-0.2 microg), whereas co-treatment with SFEA (100 microg/ml) reduced the GAG release to 10.8+/-0.7 microg (P<0.05). Also, in the group treated only with IL-1beta (11.9+/-0.3 microg), the amount of released GAG increased significantly compared to the control (7.9+/-0.1 microg) and the SFEA-treated group (7.8+/-0.4 microg). SFEA at 100 microg/ml inhibited PG degradation (9.0+/-0.5 microg, P<0.05). However, no concentration-dependent increases in inhibitory activity were observed. Therefore, since SFEA treatment resulted in no pathological impact on either the chondrocytes or cartilage, we suggest that SF can be safely used as an effective material for the prevention of proteoglycan (PG) degradation.


Subject(s)
Bone Matrix/metabolism , Cartilage, Articular/drug effects , Chondrocytes/drug effects , Schisandra , Aggrecans/metabolism , Cartilage, Articular/enzymology , Cell Line , Chondrocytes/metabolism , Dose-Response Relationship, Drug , Enzyme Inhibitors/pharmacology , Glycosaminoglycans/metabolism , Humans , Hyaluronoglucosaminidase/antagonists & inhibitors , Hyaluronoglucosaminidase/metabolism , Interleukin-1beta/genetics , Interleukin-1beta/pharmacology , Plant Extracts/pharmacology , Proteoglycans/metabolism , RNA, Messenger/metabolism , Recombinant Proteins/pharmacology , Tissue Culture Techniques
2.
Mol Cells ; 13(1): 5-11, 2002 Feb 28.
Article in English | MEDLINE | ID: mdl-11911474

ABSTRACT

Amyloid beta protein (Abeta) increases free radical production and lipid peroxidation in PC12 nerve cells, leading to apoptosis and cell death. The effect of ursolic acid from Origanum majorana L. on Abeta-induced neurotoxicity was investigated using PC12 cells. Pretreatment with isolated ursolic acid and vitamin E prevented the PC12 cell from reactive oxygen species (ROS) toxicity that is mediated by Abeta. The ursolic acid resulted in decreased Abeta toxicity assessed by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT), lactate dehydrogenase (LDH), and trypan blue assay. Thus, treatment with these antioxidants inhibited the Abeta-induced neurotoxic effect. Therefore, these results indicate that micromolar Abeta-induced oxidative cell death is reduced by ursolic acid from Origanum majorana L.


Subject(s)
Amyloid beta-Peptides/antagonists & inhibitors , Amyloid beta-Peptides/toxicity , Triterpenes/pharmacology , Alzheimer Disease/etiology , Alzheimer Disease/metabolism , Animals , Antioxidants/pharmacology , Cell Death/drug effects , Humans , Lamiaceae/chemistry , Lipid Peroxidation/drug effects , PC12 Cells , Rats , Reactive Oxygen Species/metabolism , Triterpenes/isolation & purification , Vitamin E/pharmacology , Ursolic Acid
3.
Int J Antimicrob Agents ; 21(4): 340-6, 2003 Apr.
Article in English | MEDLINE | ID: mdl-12672580

ABSTRACT

The antimicrobial activity against Clostridium difficile of 109 lactic acid bacteria (LAB) isolated from 32 healthy Korean infants was measured. The ability to show similar activity against Escherichia coli O157:H7 and Staphylococcus aureus was also looked for. Twelve of the 109 LAB showed activity against C. difficile and 19 strains were active against E. coli O157:H7, but none against S. aureus. Four strains had antimicrobial activity against both C. difficile and E. coli O157:H7. Of the 12 strains that had activity against C. difficile, four strains were excluded as Streptococcus species, while the other eight were identified using polymerase chain reaction (PCR) assays using group-specific primers designed from the nucleotide sequences of the 16S rDNA and internal transcribed spacer (ITS) regions of the Bifidobacterium and Lactobacillus species. Based on the sequencing results, the eight strains screened were identified as Bifidobacterium infantis and Lactobacillus salivarius.


Subject(s)
Bifidobacterium/isolation & purification , Clostridium , Feces/microbiology , Lactobacillus/isolation & purification , Amino Acid Sequence , Anti-Bacterial Agents/pharmacology , Bifidobacterium/classification , Bifidobacterium/drug effects , Bifidobacterium/genetics , Clostridium/growth & development , Escherichia coli/physiology , Humans , Infant , Lactobacillus/classification , Lactobacillus/drug effects , Lactobacillus/genetics , Male , Molecular Sequence Data , Polymerase Chain Reaction/methods , RNA, Ribosomal, 16S/genetics , Sequence Analysis, DNA , Staphylococcus aureus/physiology
4.
Planta Med ; 73(14): 1478-81, 2007 Nov.
Article in English | MEDLINE | ID: mdl-17948169

ABSTRACT

NADH-fumarate reductase (NFRD) is a key enzyme in many anaerobic helminths. Decursin and decursinol angelate have been isolated from the roots of ANGELICA GIGAS Nakai (Apiaceae) as NFRD inhibitors. They inhibited ASCARIS SUUM NFRD with IC (50) values of 1.1 and 2.7 microM, respectively. Their target is the electron transport enzyme complex I. Since the inhibitory activities of decursin against bovine heart complexes are weak, it is a selective inhibitor of the nematode complex I. In contrast, decursinol angelate moderately inhibits bovine heart complexes II and III. Decursinol inhibits A. SUUM NFRD to a similar extent, but its target is complex II. It also inhibits bovine heart complexes II and III.


Subject(s)
Anthelmintics/pharmacology , Ascaris suum/enzymology , Benzopyrans/pharmacology , Butyrates/pharmacology , Oxidoreductases Acting on CH-CH Group Donors/antagonists & inhibitors , Angelica/chemistry , Animals , Anthelmintics/chemistry , Benzopyrans/chemistry , Butyrates/chemistry , Molecular Structure
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