Amyloid-type fiber formation in control of enzyme action: interfacial activation of phospholipase A2.

Amyloid-type fiber formation in control of enzyme action: interfacial activation of phospholipase A2. Research Abstract Details 

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Amyloid-type fiber formation in control of enzyme action: interfacial activation of phospholipase A2. Abstract Text:

The lag-burst behavior in the action of phospholipase A(2) (PLA(2)) on 1,2-dipalmitoyl-sn-glycero-3-phosphocholine was investigated at temperatures slightly offset from the main phase transition temperature T(m) of this lipid, thus slowing down the kinetics of the activation process. Distinct stages leading to maximal activity were resolved using a combination of fluorescence parameters, including Förster resonance energy transfer between donor- and acceptor-labeled enzyme, fluorescence anisotropy, and lifetime, as well as thioflavin T fluorescence enhancement. We showed that the interfacial activation of PLA(2), evident after the preceding lag phase, coincides with the formation of oligomers staining with thioflavin T and subsequently with Congo red. Based on previous studies and our findings here, we propose a novel mechanism for the control of PLA(2), involving amyloid protofibrils with highly augmented enzymatic activity. Subsequently, these protofibrils form "mature" fibrils, devoid of activity. Accordingly, the process of amyloid formation is used as an on-off switch to obtain a transient burst in enzymatic catalysis.

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Amyloid-type fiber formation in control of enzyme action: interfacial activation of phospholipase A2. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Biophysical journal

VOLUME: 95

Page Numbers: 215-24

Journal Abbreviation: Biophys. J.

ISSN: 1542-0086

DAY: 13

MONTH: 03

YEAR: 2008

Amyloid-type fiber formation in control of enzyme action: interfacial activation of phospholipase A2. Information

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LANGUAGE: eng

NlmUniqueID: 370626

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Grant and Affiliation Information for Amyloid-type fiber formation in control of enzyme action: interfacial activation of phospholipase A2.

AFFILIATION: Helsinki Biophysics and Biomembrane Group, Medical Biochemistry, Institute of Biomedicine, University of Helsinki, Finland.

Country: United States

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MEDLINETA: Biophys J

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