Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/36443
Title: THE ROLE OF HEAT SHOCK PROTEIN 20 (HSP20) IN THE PATHOGENESIS OF HELICOBACTER PYLORI INFECTIONS
Authors: WEE SOON HUAT, ALVIN
Keywords: Helicobacter pylori, Heat Shock Protein 20, Cytotoxin-associated gene A, Angiopoietin-like 4, Tight junctions, Gastroduodenal diseases
Issue Date: 14-Sep-2012
Source: WEE SOON HUAT, ALVIN (2012-09-14). THE ROLE OF HEAT SHOCK PROTEIN 20 (HSP20) IN THE PATHOGENESIS OF HELICOBACTER PYLORI INFECTIONS. ScholarBank@NUS Repository.
Abstract: Disruption of gastric epithelial cell-cell junctions is essential and critical in the development and progression of severe Helicobacter pylori-associated diseases. This study shows the presence of a surface-localized Heat Shock Protein 20 (HSP20) of H. pylori that initiates the upregulation of host angiopoietin-like 4 (ANGPTL4), a secreted adipocytokine. The increased levels of ANGPTL4 effects the perturbation of tight junctions and loss of barrier function, via ZO-1 redistribution, resulting in the subsequent exposure of basolateral integrins. HSP20 also binds to cytotoxin-associated gene A (CagA) oncoprotein intrabacterially and the CagA-HSP20 complex is then co-translocated into host cells, via the Type IV secretion system, exacerbating further disruption of cell-cell tight junctions. This hitherto unreported mechanism that occurs prior to CagA translocation strengthens HSP20 as the initiator while ANGPTL4 and CagA are the effectors of tight junction disruption of gastric epithelial cells. Taken together, HSP20 can be considered as a potential virulence factor that augments H. pylori pathogenesis.
URI: http://scholarbank.nus.edu.sg/handle/10635/36443
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