Intestinal epithelial cell apoptosis due to a hemolytic toxin from Vibrio vulnificus and protection by a 36 kDa glycoprotein from Rhus verniciflua Stokes. (March 2019)
- Record Type:
- Journal Article
- Title:
- Intestinal epithelial cell apoptosis due to a hemolytic toxin from Vibrio vulnificus and protection by a 36 kDa glycoprotein from Rhus verniciflua Stokes. (March 2019)
- Main Title:
- Intestinal epithelial cell apoptosis due to a hemolytic toxin from Vibrio vulnificus and protection by a 36 kDa glycoprotein from Rhus verniciflua Stokes
- Authors:
- Lee, Young-Min
Park, Jong Pil
Lim, Kye-Taek
Lee, Sei-Jung - Abstract:
- Abstract: Rhus verniciflua stokes (RVS) has been used as a functional food to cure inflammatory diseases in Korea. In the present study, we carry out an investigation of the cellular mechanism of a 36 kDa glycoprotein isolated from RVS fruit (RVS glycoprotein) during the apoptosis of human gastrointestinal epithelial HCT116 cells induced by the hemolytic toxin (VvhA) produced by V. vulnificus . Recombinant protein (r) VvhA produced by V. vulnificus stimulated apoptosis by activating the phosphorylation of protein kinase C (PKC) through the production of intracellular reactive oxygen species (ROS). However, RVS glycoprotein significantly inhibited the level of ROS production and PKC activation in rVvhA-stimulated HCT116 cells. Interestingly, we found that RVS glycoprotein has inhibitory effects on the phosphorylation of c-Jun N-terminal kinase (JNK) and nuclear factor-kappa B (NF-κB), which are responsible for the expression of Bax and cleaved caspase-3 in HCT116 cells treated with rVvhA, respectively. On the basis of these results, we suggest that RVS glycoprotein blocks mitochondrial apoptotic cell death induced by rVvhA via the inhibition of ROS-mediated signaling events in HCT116 cells. Highlights: RVS glycoprotein blocks cell death induced by V. vulnificus, VvhA. RVS glycoprotein reduces ROS production to recover cell death induced by rVvhA. RVS glycoprotein suppresses PKC/JNK/NF-κB pathway activated by rVvhA. RVS glycoprotein inhibits expression of Bax andAbstract: Rhus verniciflua stokes (RVS) has been used as a functional food to cure inflammatory diseases in Korea. In the present study, we carry out an investigation of the cellular mechanism of a 36 kDa glycoprotein isolated from RVS fruit (RVS glycoprotein) during the apoptosis of human gastrointestinal epithelial HCT116 cells induced by the hemolytic toxin (VvhA) produced by V. vulnificus . Recombinant protein (r) VvhA produced by V. vulnificus stimulated apoptosis by activating the phosphorylation of protein kinase C (PKC) through the production of intracellular reactive oxygen species (ROS). However, RVS glycoprotein significantly inhibited the level of ROS production and PKC activation in rVvhA-stimulated HCT116 cells. Interestingly, we found that RVS glycoprotein has inhibitory effects on the phosphorylation of c-Jun N-terminal kinase (JNK) and nuclear factor-kappa B (NF-κB), which are responsible for the expression of Bax and cleaved caspase-3 in HCT116 cells treated with rVvhA, respectively. On the basis of these results, we suggest that RVS glycoprotein blocks mitochondrial apoptotic cell death induced by rVvhA via the inhibition of ROS-mediated signaling events in HCT116 cells. Highlights: RVS glycoprotein blocks cell death induced by V. vulnificus, VvhA. RVS glycoprotein reduces ROS production to recover cell death induced by rVvhA. RVS glycoprotein suppresses PKC/JNK/NF-κB pathway activated by rVvhA. RVS glycoprotein inhibits expression of Bax and cleaved-caspase 3 induced by rVvhA. … (more)
- Is Part Of:
- Food and chemical toxicology. Volume 125(2019)
- Journal:
- Food and chemical toxicology
- Issue:
- Volume 125(2019)
- Issue Display:
- Volume 125, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 125
- Issue:
- 2019
- Issue Sort Value:
- 2019-0125-2019-0000
- Page Start:
- 46
- Page End:
- 54
- Publication Date:
- 2019-03
- Subjects:
- Vibrio vulnificus -- VvhA -- Rhus verniciflua Stokes -- Caspase-3 -- Apoptosis -- Gastrointestinal epithelial cells
Bax Bcl-2 associated X protein -- CM-H2DCFDA 2′, 7′ -dichlorofluorescein diacetate -- IPTG isopropyl-β-dthiogalactopyranoside -- JNK c-Jun N-terminal kinase -- MAPKs mitogen-activated protein kinases -- NAC N-acetyl-L-cysteine -- NF-κB nuclear factor-kappa B -- PKC phosphorylation of protein kinase C -- PMSF phenylmethylsulfonyl fluoride -- PVDF polyvinylidene fluoride -- ROS reactive oxygen species -- RVS Rhus verniciflua stokes -- SDS-PAGE sodium dodecyl sulfate polyacrylamide gel electrophoresis -- V. vulnificus Vibrio vulnificus
Toxicology -- Periodicals
Food poisoning -- Periodicals
Food Poisoning -- Periodicals
Toxicology -- Periodicals
Toxicologie -- Périodiques
Intoxications alimentaires -- Périodiques
Food poisoning
Toxicology
Periodicals
Electronic journals
615.9 - Journal URLs:
- http://www.sciencedirect.com/science/journal/02786915 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.fct.2018.12.041 ↗
- Languages:
- English
- ISSNs:
- 0278-6915
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.026900
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 9568.xml