Phospholipase A2 and its zymogen from porcine pancreas. VII. Zymogen-catalyzed hydrolysis of monomeric substrates and the presence of a recognition site for lipid-water interfaces in phospholipase A2

Pieterson, W. A.; Vidal, Juan C.; Volwerk, Johannes J.; Haas, G.H. de

doi:10.1021/bi00704a021

Cited by 276 publications

(155 citation statements)

References 23 publications

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“…Alternatively, the orientation of polar group on micelle surface makes possible a polar interaction of the ATPase complex with the lipid interface. Other examples of interfacial activation are found with phospholipase A2 from porcine pancreas [32,42] and Crotalus adamanteus [31] and indicate a phenomenon of general interest in lipid-protein interaction.…”

Section: Reactivation Of Atpase Complexmentioning

confidence: 98%

The role of phospholipid acyl chains in the activation of mitochondrial ATPase complex

Bruni

Dijck

Gier

1975

Biochimica et Biophysica Acta (BBA) - Biomembranes

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SUMMARY1. The role of length and unsaturation of phospholipid acy! chains in the activation of ATPase complex was studied with synthetic phosphatidylcholines and a phospholipid-dependent preparation obtained after cholate-extraction of submitochondrial particles (Kagawa, Y. and Racker, E. (1966) J. Biol. Chem. 241, 2467-2474.2. Micelle-forming, short-chain phosphatidylcholines produced activation only at critical micellar concentration. The reactivated complex was cold-stable but the oligomycin sensitivity was low.3. Bilayer-forming saturated phosphatidylcholines produced activation which was maximal at 9 carbon atoms in each chain but decreased sharply as the chainlength was increased and essentially disappeared at 14 carbon atoms. By contrast the oligomycin-sensitivity increased with the increase in chain length.4. Activation of ATPase complex reappeared when bilayers were formed with long-chain unsaturated phosphatidylcholines. The activity was oligomycin sensitive. Significant inhibition of activity was observed also after incorporation of cholesterol into the bilayers.5. By contrast the activation induced by negatively charged liposomes of diacylphosphatidyiglycerol was independent on acyi-chain composition and occurred at very low amounts of phospholipid.6. The discontinuity in the Arrhenius plot of activity of the ATPase complex reactivated with saturated phospholipids was found at temperatures close to the gelto-liquid crystalline transition of the lipid showing that the activity of ATPase complex was sensitive to the physical state of membrane phospholipids.7. It is concluded that (a) reactivation of ATPase complex by isoelectric phospholipids is an interracial activation, the minimum requirement for the lipid effect being micelle formation. (b) In order to gain the properties of the native complex a stable lamellar phase is needed. Both activity and oligomycin sensitivity are regulated by the chain length and degree of unsaturation of phospholipid acyl chains.

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Section: Reactivation Of Atpase Complexmentioning

confidence: 98%

The role of phospholipid acyl chains in the activation of mitochondrial ATPase complex

Bruni

Dijck

Gier

1975

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…It has been shown in recent years that many zymogens including trypsinogen, chymotrypsinogen, procarboxypeptidase, prophospholipase [1][2][3][4][5][6][7], etc. display toward certain substrates or pseudo-substrates a weak intrinsic activity prior to activation.…”

Section: Introductionmentioning

confidence: 99%

Pre‐existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz)

Vincent

Lazdunski

1976

FEBS Letters

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“…Although both PLA and proPLA hydrolyze monomolecularly dispersed substrates at a fairly slow rate, only the active enzyme shows a rate enhancement of several orders of magnitude when the substrate is present as a micellar aggregate [6]. Various hypotheses have been formulated but up to now no generally accepted explanation of this phenomenon has been given [7].…”

mentioning

confidence: 99%

“…For the pancreatic enzyme experimental work has been guided by the interface recognition site hypothesis, which postulates the presence on the enzyme surface of one or more specific regions, distinct from the active site, important for binding of the protein to the organized lipid substrate [6,8]. So far, however, kinetic and direct binding studies supporting this hypothesis have been performed largely using either phosphatidylcholines as substrates or substrate analogs carrying the phosphocholine polar head group [7].…”

mentioning

confidence: 99%

Evidence that the zymogen of phospholipase A2 binds to a negatively charged lipid-water interface

Volwerk¹,

Jost²,

Griffith³

1984

Chemistry and Physics of Lipids

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Evidence is presented that the zymogen of porcine pancreatic phospholipase A~ (prophospholipase A2) interacts with a lipid-water interface provided that the interface has a net negative surface charge. Fluorescence spectroscopy and non-equilibrium gel filtration indicate that binding of prophospholipase A 2 (proPLA) to mixed detergent micelles is dependent on the presence of an anionic detergent. Prophospholipase binding is accompanied by a change in the environment of the single tryptophan residue qualitatively similar to that observed when the active enzyme, phospholipase A s (PLA), binds to micelles. In addition, the rate of tryptic activation of prophospholipase is significantly reduced in the presence of negatively-charged mixed micelles, whereas no change in rate occurs when neutral micelles are present. These observations suggest that the lack of catalytic activity of the zymogen toward organized substrates carrying a negative surface charge cannot be explained by a failure to bind at the lipidwater interface.

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Phospholipase A2 and its zymogen from porcine pancreas. VII. Zymogen-catalyzed hydrolysis of monomeric substrates and the presence of a recognition site for lipid-water interfaces in phospholipase A2

Cited by 276 publications

References 23 publications

The role of phospholipid acyl chains in the activation of mitochondrial ATPase complex

The role of phospholipid acyl chains in the activation of mitochondrial ATPase complex

Pre‐existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz)

Evidence that the zymogen of phospholipase A2 binds to a negatively charged lipid-water interface

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