Interfacial Enzymology:  The Secreted Phospholipase A<sub>2</sub>-Paradigm

Berg, Otto G.; Gelb, Michael H.; Tsai, Ming‐Daw; Jain, Mahendra Kumar

doi:10.1021/cr990139w

Cited by 368 publications

(370 citation statements)

References 322 publications

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“…8A) indicating that, under these conditions, increased binding did not significantly affect PLA 2 activity. In model membranes such as PL vesicles, the generation in situ of PL breakdown products can increase the avidity of PLA 2 -membrane interactions (37). Therefore, the increased binding of PLA 2 to the mutant strain we observed when calcium was present, might simply reflect differences induced, directly or indirectly, by greater membrane damage within the envelope of the dltA Ϫ bacteria.…”

Section: Discussionmentioning

confidence: 84%

Role of Charge Properties of Bacterial Envelope in Bactericidal Action of Human Group IIA Phospholipase A2against Staphylococcus aureus

Koprivnjak

Peschel

Gelb

et al. 2002

Journal of Biological Chemistry

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120

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S. aureus, we examined the effects of mutations that prevent specific modifications of cell wall (dltA) and cell membrane (mprF) polyanions. In comparison to the parent strain, isogenic dltA ؊ bacteria are ϳ30 -100؋ more sensitive to PLA 2 , whereas mprF ؊ bacteria are <3-fold more sensitive. Differences in PLA 2 sensitivity of intact bacteria reflect differences in cell wall, not cell membrane, properties since protoplasts from all three strains are equally sensitive to PLA 2 . A diminished positive charge in PLA 2 reduces PLA 2 binding and antibacterial activity. In contrast, diminished cell wall negative charge by substitution of (lipo)teichoic acids with D-alanine reduces antibacterial activity of bound PLA 2 , but not initial PLA 2 binding. Therefore, the potent antistaphylococcal activity of Group IIA PLA 2 depends on cationic properties of the enzyme that promote binding to the cell wall, and polyanionic properties of cell wall (lipo)teichoic acids that promote attack of membrane phospholipids by bound PLA 2 .

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Section: Discussionmentioning

confidence: 84%

Role of Charge Properties of Bacterial Envelope in Bactericidal Action of Human Group IIA Phospholipase A2against Staphylococcus aureus

Koprivnjak

Peschel

Gelb

et al. 2002

Journal of Biological Chemistry

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120

145

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“…In the present study no hydrolysis of surfactant PC was observed in sPLA 2 -IIA-treated mice. This is not surprising, since sPLA 2 -IIA, which bears basic residues resulting in positive charges of its interfacial binding surface, cannot bind well to PC vesicles, as described for PG (33,41,42).…”

Section: Discussionmentioning

confidence: 90%

“…Subtle differences in their sequences markedly affect their substrate interfacial binding and rate of hydrolysis (32,33). Here we analyzed the efficiencies of various sPLA 2 s, including recently cloned sPLA 2 s, to hydrolyze surfactant.…”

Section: Discussionmentioning

confidence: 99%

Inhibitory Effects of Surfactant Protein A on Surfactant Phospholipid Hydrolysis by Secreted Phospholipases A2

Chabot

Koumanov

Lambeau

et al. 2003

The Journal of Immunology

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Hydrolysis of surfactant phospholipids by secreted phospholipases A2 (sPLA2) contributes to surfactant dysfunction in acute respiratory distress syndrome. The present study demonstrates that sPLA2-IIA, sPLA2-V, and sPLA2-X efficiently hydrolyze surfactant phospholipids in vitro. In contrast, sPLA2-IIC, -IID, -IIE, and -IIF have no effect. Since purified surfactant protein A (SP-A) has been shown to inhibit sPLA2-IIA activity, we investigated the in vitro effect of SP-A on the other active sPLA2 and the consequences of sPLA2-IIA inhibition by SP-A on surfactant phospholipid hydrolysis. SP-A inhibits sPLA2-X activity, but fails to interfere with that of sPLA2-V. Moreover, in vitro inhibition of sPLA2-IIA-induces surfactant phospholipid hydrolysis correlates with the concentration of SP-A in surfactant. Intratracheal administration of sPLA2-IIA to mice causes hydrolysis of surfactant phosphatidylglycerol. Interestingly, such hydrolysis is significantly higher for SP-A gene-targeted mice, showing the in vivo inhibitory effect of SP-A on sPLA2-IIA activity. Administration of sPLA2-IIA also induces respiratory distress, which is more pronounced in SP-A gene-targeted mice than in wild-type mice. We conclude that SP-A inhibits sPLA2 activity, which may play a protective role by maintaining surfactant integrity during lung injury.

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“…The kinetics of molecular processes at lipide water interfaces require special treatment (Berg et al, 2001). For a protein at least two separate binding steps e and binding domains e are needed for proper interaction with aggregated lipids, one interfacial binding step and another step involving a single lipid molecule.…”

Section: Discussionmentioning

confidence: 99%

Glycolipid transfer protein: Clear structure and activity, but enigmatic function

Neumann

Opacic

Wechselberger

et al. 2008

Advances in Enzyme Regulation

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Interfacial Enzymology: The Secreted Phospholipase A₂-Paradigm

Cited by 368 publications

References 322 publications

Role of Charge Properties of Bacterial Envelope in Bactericidal Action of Human Group IIA Phospholipase A2against Staphylococcus aureus

Role of Charge Properties of Bacterial Envelope in Bactericidal Action of Human Group IIA Phospholipase A2against Staphylococcus aureus

Inhibitory Effects of Surfactant Protein A on Surfactant Phospholipid Hydrolysis by Secreted Phospholipases A2

Glycolipid transfer protein: Clear structure and activity, but enigmatic function

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Interfacial Enzymology: The Secreted Phospholipase A2-Paradigm

Cited by 368 publications

References 322 publications

Role of Charge Properties of Bacterial Envelope in Bactericidal Action of Human Group IIA Phospholipase A2against Staphylococcus aureus

Role of Charge Properties of Bacterial Envelope in Bactericidal Action of Human Group IIA Phospholipase A2against Staphylococcus aureus

Inhibitory Effects of Surfactant Protein A on Surfactant Phospholipid Hydrolysis by Secreted Phospholipases A2

Glycolipid transfer protein: Clear structure and activity, but enigmatic function

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Interfacial Enzymology: The Secreted Phospholipase A₂-Paradigm