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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

TitleHistidine-rich protein Hpn from Helicobacter pylori forms amyloid-like fibrils in vitro and inhibits the proliferation of gastric epithelial AGS cells
Authors
KeywordsAmyloid
Gastric epithelial cell
Helicobacter pylori
Hpn
Mitochondria
Issue Date2011
PublisherElsevier 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 Identifierhttp://hdl.handle.net/10722/137221
ISSN
2013 Impact Factor: 5.297
2013 SCImago Journal Rankings: 2.999
ISI Accession Number ID
References

 

Author Affiliations
  1. The University of Hong Kong
  2. Sun Yat-Sen University
  3. Jinan University
DC FieldValueLanguage
dc.contributor.authorGe, Ren_HK
dc.contributor.authorSun, Xen_HK
dc.contributor.authorWang, Den_HK
dc.contributor.authorZhou, Qen_HK
dc.contributor.authorSun, Hen_HK
dc.date.accessioned2011-08-26T14:19:15Z-
dc.date.available2011-08-26T14:19:15Z-
dc.date.issued2011en_HK
dc.identifier.citationBiochimica Et Biophysica Acta - Molecular Cell Research, 2011, v. 1813 n. 8, p. 1422-1427en_HK
dc.identifier.issn0167-4889en_HK
dc.identifier.urihttp://hdl.handle.net/10722/137221-
dc.description.abstractHelicobacter 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.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbamcren_HK
dc.relation.ispartofBiochimica et Biophysica Acta - Molecular Cell Researchen_HK
dc.subjectAmyloiden_HK
dc.subjectGastric epithelial cellen_HK
dc.subjectHelicobacter pylorien_HK
dc.subjectHpnen_HK
dc.subjectMitochondriaen_HK
dc.subject.meshBacterial Proteins - chemistry - physiology - ultrastructure-
dc.subject.meshEpithelial Cells - microbiology - pathology-
dc.subject.meshGastric Mucosa - microbiology - pathology-
dc.subject.meshHelicobacter pylori - pathogenicity - physiology-
dc.subject.meshProteins - chemistry - physiology - ultrastructure-
dc.titleHistidine-rich protein Hpn from Helicobacter pylori forms amyloid-like fibrils in vitro and inhibits the proliferation of gastric epithelial AGS cellsen_HK
dc.typeArticleen_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.bbamcr.2011.04.005en_HK
dc.identifier.pmid21539864en_HK
dc.identifier.scopuseid_2-s2.0-79959365764en_HK
dc.identifier.hkuros189548en_US
dc.identifier.hkuros211146-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79959365764&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume1813en_HK
dc.identifier.issue8en_HK
dc.identifier.spage1422en_HK
dc.identifier.epage1427en_HK
dc.identifier.isiWOS:000292945200004-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridGe, R=7005525090en_HK
dc.identifier.scopusauthoridSun, X=35799316500en_HK
dc.identifier.scopusauthoridWang, D=54411630800en_HK
dc.identifier.scopusauthoridZhou, Q=42462760400en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.citeulike9227500-

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