Linked Life Data

20065505

Source:http://linkedlifedata.com/resource/pubmed/id/20065505

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-1-12
pubmed:abstractText
Physiological process of cell death, apoptosis, plays a beneficial role in organism survival, but in some pathologies, like gastric Helicobacter pylori (Hp) infection, this process may turn against the host organism causing tissue damage. Knowledge of the mechanisms controlling apoptosis may have potential significance in treatment of these pathologic states. Therefore, we sought to determine whether apoptosis induced in the gastric epithelial cells exposed to live Hp involves the alteration in heat shock protein 70 (HSP70) expression and activation of caspase-3 in peroxisome proliferator-activated receptors (PPARgamma dependent manner). Experiments were performed with KATO III, gastric epithelial cells, exposed to CagA and Vac A positive live Hp, water Hp extracts or Hp culture supernatant over different time periods. Total cellular RNA and proteins were isolated for PCR, western-blot and EMSA studies. Genomic DNA was isolated to analyze apoptosis status. We propose new model of Hp induced HSP70 dependent, caspase-3 executed apoptosis in human gastric epithelium. KATO III cells exposed to Hp, showed an increase in caspase-3 activity accompanied and preceeded by activation of nuclear translocation of PPARg peaking at 48 h of culture. Moreover, heat shock factor 1 (HSF-1) bound up with phosphorylated STAT-3 was unable to activate HSP70 protein synthesis in KATO III exposed to Hp. Lack of protective effect of HSP70, activation of caspase-3--dependent apoptosis pathway caused by Hp and alteration of the bax/bcl-2 cellular equilibrium led to gastric epithelial cell death. The observed phenomenon might be helpful in understanding of the mechanism of Hp related gastrointestinal tract diseasess, especially gastric cancer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1899-1505
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
119-28
pubmed:meshHeading
pubmed-meshheading:20065505-Apoptosis, pubmed-meshheading:20065505-Caspase 3, pubmed-meshheading:20065505-Cell Line, Tumor, pubmed-meshheading:20065505-DNA Fragmentation, pubmed-meshheading:20065505-Electrophoretic Mobility Shift Assay, pubmed-meshheading:20065505-Enzyme Activation, pubmed-meshheading:20065505-Epithelial Cells, pubmed-meshheading:20065505-Gastric Mucosa, pubmed-meshheading:20065505-Gene Expression Regulation, Neoplastic, pubmed-meshheading:20065505-HSP70 Heat-Shock Proteins, pubmed-meshheading:20065505-Helicobacter pylori, pubmed-meshheading:20065505-Humans, pubmed-meshheading:20065505-PPAR gamma, pubmed-meshheading:20065505-Protein Transport, pubmed-meshheading:20065505-Proto-Oncogene Proteins c-bcl-2, pubmed-meshheading:20065505-RNA, Messenger, pubmed-meshheading:20065505-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:20065505-Time Factors, pubmed-meshheading:20065505-bcl-2-Associated X Protein
pubmed:year
2009
pubmed:articleTitle
Only live Helicobacter pylori is capable of caspase-3 dependent apoptosis induction in gastric mucosa epithelial cells.
pubmed:affiliation
Department of Medical Physiology, Faculty of Health Sciences, Jagiellonian University Medical College, Cracow, Poland. ppierzchalski@poczta.fm
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't