The role of HspB and CagA in the molecular pathogenesis of helicobacter pylori positive gastric cancer

Luca, Antonella De; Todisco, Anna; Giardullo, Nicola; Pasquale, Luigi; D'Onofrio, V.; Sorrentini, I.; Parodi, M.C.; Iaquinto, Gaetano

doi:10.1016/s1590-8658(01)80300-5

Cited by 1 publication

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“…45 H. pylori GroEL homologue HspB belongs to the HSP60 family 46 and increases the risk of gastric carcinoma by directly inducing the hyperproliferation of gastric cells. 45,47 The bismuth compounds may target the HSPs in at least two ways: (1) the triple amino acids from HspA, His45, Cys51 and C53, make up an oxidation-sensitive zinc binding site and Bi 3+ binds irreversibly to this site (K d E 7 Â 10 À26 M), replacing the bound zinc and inducing changes in the quaternary structure from the native heptamer to a dimer. 48 The heptamer HspA coordinates with the tetradecameric HspB to form a hydrophobic cavity where non-native proteins are encapsulated and refolded rapidly.…”

Section: Enzyme Inhibitionmentioning

confidence: 99%

The actions of bismuth in the treatment of Helicobacter pylori infections: an update

Chen

Zhou

2012

Metallomics

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Helicobacter pylori causes various gastric diseases, such as gastritis, peptic ulcerations and gastric cancer. Bismuth-based triple or quadruple therapies have been commonly recommended for the treatment of H. pylori infections. Up to now, the molecular mechanisms by which bismuth inhibits the growth of H. pylori are far from clear. The present concise review intends to cover the most recent reports and discoveries in the field of the inhibitory mechanism of bismuth against H. pylori as well as the bacterial protective response to drug treatment, which will help us to further understand the molecular mechanisms underlying the actions of metal-based drugs and stimulate further development of effective anti-bacterial drugs.

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