pH-Activated Phospholipase A 2 : an Important Mucosal Barrier Breaker in Peptic Ulcer Disease

Berstad, Arnold; Berstad, K; Berstad, A

doi:10.1080/00365520212493

Cited by 12 publications

(16 citation statements)

References 53 publications

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“…This can also affect membrane permeability and mucous discharge [55]. Moreover, the pH-activated PLA 2 in H. pylori acted as an initial mucosal barrier breaker in pathogenesis of peptic ulcer [56]. The research indicated that the gastric juice of H. pylori-infected individuals contained significantly higher PLA 2 and PLC concentrations than those of healthy individuals.…”

Section: Bacterial Phospholipase and Pathogenesismentioning

confidence: 97%

Recent Progress on Phospholipases: Different Sources, Assay Methods, Industrial Potential and Pathogenicity

Ramrakhiani

Chand

2011

Appl Biochem Biotechnol

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Significant studies on phospholipases optimization, characterization, physiological role and industrial potential have been conducted worldwide. Some of them have been directed for biotechnological advances such as gene discovery and functional enhancement by protein engineering. Others reported phospholipases as virulence factor and major cause of pathophysiological effects. A general overview on phospholipase is needed for the identification of new reliable and efficient phospholipase, which would be potentially used in number of industrial and medical applications. Phospholipases catalyse the hydrolysis of one or more ester and phosphodiester bonds of glycerophospholipids. They vary in site of action on phospholipid which can be used industrially for modification/production of new phospholipids. Catalytically active phospholipase mainly use phosphatidylcholine as major substrate, but they can also show specificity with other phospholipids. Several accurate phospholipase assay methods are known, but a rapid and reliable method for high-throughput screening is still a challenge for efficient supply of superior phospholipases and their practical applications. Major application of phospholipase is in industries like oil refinery, health food manufacturing, dairy, cosmetics etc. All types of phospholipases can be involved as virulence factor. They can also be used as diagnostic markers for microbial infection. The importance of phospholipase in virulence is proven and inhibitors of the enzyme can be used as candidate for preventing the associated disease.

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Section: Bacterial Phospholipase and Pathogenesismentioning

confidence: 97%

Recent Progress on Phospholipases: Different Sources, Assay Methods, Industrial Potential and Pathogenicity

Ramrakhiani

Chand

2011

Appl Biochem Biotechnol

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“…Moreover, Berstad et al (2002) suggested that the pH-activated phosoholipase A 2 in H. pylori acts as an initial mucosal barrier breaker and is considered to have a pivotal role in the pathogenesis of peptic ulcer. The research also indicated that the gastric juice of H. pyloriinfected individuals contains significantly higher PLA 2 and lyso-PC concentrations than that of healthy individuals (Berstad et al, 2002).…”

Section: Relationship Between Bacterial Phospholipases and Pathogenesismentioning

confidence: 99%

“…Phospholipids and proteins represent the major chemical constituents of the host cell envelope. Therefore phospholipases are likely to be involved in the membrane disruption processes that often occur during host cell invasion (Waite, 1996), such as the pH-activated phospholipase A 2 of Helicobacter pylori (Berstad et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Phospholipase A in Gram-negative bacteria and its role in pathogenesis

2006

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Phospholipase A (PLA) is one of the few enzymes present in the outer membrane of Gram-negative bacteria, and is likely to be involved in the membrane disruption processes that occur during host cell invasion. Both secreted and membrane-bound phospholipase A2 activities have been described in bacteria, fungi and protozoa. Recently there have been increasing reports on the involvement of PLA in bacterial invasion and pathogenesis. This review highlights the latest findings on PLA as a virulence factor in Gram-negative bacteria.

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“…(37) have been widely studied, and inhibition of these enzymes has been analyzed as a new potential pharmacological approach. In this work, we focused on the identification and characterization of H. pylori lipases because this bacterium is an important and widespread pathogen whose lipolytic activity with host lipids seems to favor bacterial colonization and development of ulcers by weakening the barrier properties of gastric mucus and probably also by producing inflammation, cytotoxicity, and cell lysis (5,12,35,44,45,48,51).…”

Section: Discussionmentioning

confidence: 99%

“…Weakening the mucus barrier favors H. pylori colonization of the host cell surface and makes the epithelium more accessible to gastric acid and pepsin. Moreover, lipase and (mainly) phospholipase activities seem to be related to disruption of the apical membrane of epithelial cells, to hemolysis, and to the generation of lysophospholipids and other cytotoxic and proinflammatory lipids detrimental for the mucous gel and epithelium integrity (5,48,51).…”

mentioning

confidence: 99%

Helicobacter pylori EstV: Identification, Cloning, and Characterization of the First Lipase Isolated from an Epsilon-Proteobacterium

Ruiz

Falcocchio

Pastor

et al. 2007

Appl Environ Microbiol

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Bacterial lipases are attracting an enormous amount of attention due to their wide biotechnological applications and due to their roles as virulence factors in some bacteria. Helicobacter pylori is a significant and widespread pathogen which produces a lipase(s) and phospholipases that seem to play a role in mucus degradation and the release of proinflammatory and cytotoxic compounds. However, no H. pylori lipase(s) has been isolated and described previously. Therefore, a search for putative lipase-encoding genes was performed by comparing the amino acid sequences of 53 known lipolytic enzymes with the deduced proteome of H. pylori. As a result, we isolated, cloned, purified, and characterized EstV, a novel lipolytic enzyme encoded by open reading frame HP0739 of H. pylori 26695, and classified it in family V of the bacterial lipases. This enzyme has the properties of a small, cell-bound carboxylesterase (EC 3.1.1.1) that is active mostly with short-chain substrates and does not exhibit interfacial activation. EstV is stable and does not require additional cofactors, and the maximum activity occurs at 50°C and pH 10. This unique enzyme is the first lipase isolated from H. pylori that has been described, and it might contribute to ulcer development, as inhibition by two antiulcer substances (␤-aescin and glycyrrhizic acid) suggests. EstV is also the first lipase from an epsilon-proteobacterium to be described. Furthermore, this enzyme is a new member of family V, probably the least-known family of bacterial lipases, and the first lipase of this family for which kinetic behavior, inhibition by natural substances, and other key biochemical features are reported.

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pH-Activated Phospholipase A 2 : an Important Mucosal Barrier Breaker in Peptic Ulcer Disease

Cited by 12 publications

References 53 publications

Recent Progress on Phospholipases: Different Sources, Assay Methods, Industrial Potential and Pathogenicity

Recent Progress on Phospholipases: Different Sources, Assay Methods, Industrial Potential and Pathogenicity

Phospholipase A in Gram-negative bacteria and its role in pathogenesis

Helicobacter pylori EstV: Identification, Cloning, and Characterization of the First Lipase Isolated from an Epsilon-Proteobacterium

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