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- Publisher Website: 10.1016/j.bbamcr.2011.04.005
- Scopus: eid_2-s2.0-79959365764
- PMID: 21539864
- WOS: WOS:000292945200004
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Article: Histidine-rich protein Hpn from Helicobacter pylori forms amyloid-like fibrils in vitro and inhibits the proliferation of gastric epithelial AGS cells
Title | Histidine-rich protein Hpn from Helicobacter pylori forms amyloid-like fibrils in vitro and inhibits the proliferation of gastric epithelial AGS cells |
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Authors | |
Keywords | Amyloid Gastric epithelial cell Helicobacter pylori Hpn Mitochondria |
Issue Date | 2011 |
Publisher | Elsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbamcr |
Citation | Biochimica Et Biophysica Acta - Molecular Cell Research, 2011, v. 1813 n. 8, p. 1422-1427 How to Cite? |
Abstract | Helicobacter pylori causes various gastric diseases, such as gastritis, peptic ulcerations, gastric cancer and mucosa-associated lymphoid tissue lymphoma. Hpn is a histidine-rich protein abundant in this bacterium and forms oligomers in physiologically relevant conditions. In this present study, Hpn oligomers were found to develop amyloid-like fibrils as confirmed by negative stain transition electron microscopy, thioflavin T and Congo red binding assays. The amyloid-like fibrils of Hpn inhibit the proliferation of gastric epithelial AGS cells through cell cycle arrest in the G2/M phase, which may be closely related to the disruption of mitochondrial bioenergetics as reflected by the significant depletion of intracellular ATP levels and the mitochondrial membrane potential. The collective data presented here shed some light on the pathologic mechanisms of H. pylori infections. © 2011 Elsevier B.V. |
Persistent Identifier | http://hdl.handle.net/10722/137221 |
ISSN | 2023 Impact Factor: 4.6 2023 SCImago Journal Rankings: 1.500 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ge, R | en_HK |
dc.contributor.author | Sun, X | en_HK |
dc.contributor.author | Wang, D | en_HK |
dc.contributor.author | Zhou, Q | en_HK |
dc.contributor.author | Sun, H | en_HK |
dc.date.accessioned | 2011-08-26T14:19:15Z | - |
dc.date.available | 2011-08-26T14:19:15Z | - |
dc.date.issued | 2011 | en_HK |
dc.identifier.citation | Biochimica Et Biophysica Acta - Molecular Cell Research, 2011, v. 1813 n. 8, p. 1422-1427 | en_HK |
dc.identifier.issn | 0167-4889 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/137221 | - |
dc.description.abstract | Helicobacter pylori causes various gastric diseases, such as gastritis, peptic ulcerations, gastric cancer and mucosa-associated lymphoid tissue lymphoma. Hpn is a histidine-rich protein abundant in this bacterium and forms oligomers in physiologically relevant conditions. In this present study, Hpn oligomers were found to develop amyloid-like fibrils as confirmed by negative stain transition electron microscopy, thioflavin T and Congo red binding assays. The amyloid-like fibrils of Hpn inhibit the proliferation of gastric epithelial AGS cells through cell cycle arrest in the G2/M phase, which may be closely related to the disruption of mitochondrial bioenergetics as reflected by the significant depletion of intracellular ATP levels and the mitochondrial membrane potential. The collective data presented here shed some light on the pathologic mechanisms of H. pylori infections. © 2011 Elsevier B.V. | en_HK |
dc.language | eng | en_US |
dc.publisher | Elsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbamcr | en_HK |
dc.relation.ispartof | Biochimica et Biophysica Acta - Molecular Cell Research | en_HK |
dc.subject | Amyloid | en_HK |
dc.subject | Gastric epithelial cell | en_HK |
dc.subject | Helicobacter pylori | en_HK |
dc.subject | Hpn | en_HK |
dc.subject | Mitochondria | en_HK |
dc.subject.mesh | Bacterial Proteins - chemistry - physiology - ultrastructure | - |
dc.subject.mesh | Epithelial Cells - microbiology - pathology | - |
dc.subject.mesh | Gastric Mucosa - microbiology - pathology | - |
dc.subject.mesh | Helicobacter pylori - pathogenicity - physiology | - |
dc.subject.mesh | Proteins - chemistry - physiology - ultrastructure | - |
dc.title | Histidine-rich protein Hpn from Helicobacter pylori forms amyloid-like fibrils in vitro and inhibits the proliferation of gastric epithelial AGS cells | en_HK |
dc.type | Article | en_HK |
dc.identifier.email | Sun, H:hsun@hkucc.hku.hk | en_HK |
dc.identifier.authority | Sun, H=rp00777 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.bbamcr.2011.04.005 | en_HK |
dc.identifier.pmid | 21539864 | - |
dc.identifier.scopus | eid_2-s2.0-79959365764 | en_HK |
dc.identifier.hkuros | 189548 | en_US |
dc.identifier.hkuros | 211146 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-79959365764&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 1813 | en_HK |
dc.identifier.issue | 8 | en_HK |
dc.identifier.spage | 1422 | en_HK |
dc.identifier.epage | 1427 | en_HK |
dc.identifier.isi | WOS:000292945200004 | - |
dc.publisher.place | Netherlands | en_HK |
dc.identifier.scopusauthorid | Ge, R=7005525090 | en_HK |
dc.identifier.scopusauthorid | Sun, X=35799316500 | en_HK |
dc.identifier.scopusauthorid | Wang, D=54411630800 | en_HK |
dc.identifier.scopusauthorid | Zhou, Q=42462760400 | en_HK |
dc.identifier.scopusauthorid | Sun, H=7404827446 | en_HK |
dc.identifier.citeulike | 9227500 | - |
dc.identifier.issnl | 0167-4889 | - |