Structure-function relationship in the interaction of mastoparan analogs with neutrophil NADPH oxidase

Tisch-Idelson, Daphna; Fridkin, Mati; Wientjes, Frans B.; Aviram, Irit

doi:10.1016/s0006-2952(01)00561-5

Cited by 14 publications

(12 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Mastoparan is also known to affect the activity of phospholipase D2 (1), Rho (2), nucleotide diphosphate kinase (3), calmodulin (4), glycogen phosphorylase (5), phospholipase A2 (6), p67-phox (7), and the type II phosphatidylinositol 4-kinase (PI4KII) 2 (8,9). PI4KII␣ localizes to membranes of the Golgi-endosomal system (10,11) where it provides the phosphatidylinositol 4-phosphate (PI4P) that is required to recruit the AP-1 clathrin adaptor complex to membranes of the trans-Golgi network (TGN) (11).…”

mentioning

confidence: 99%

“…Two distinct modes of binding have been identified, one in which the peptide binds only to the target protein and another in which the peptide binds concomitantly to a membrane and a target protein. For example, in aqueous solution mastoparan binds directly to p67-phox (7) and to calmodulin. Mastoparan binds to calmodulin in a helical conformation with low nanomolar affinity (18).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Lipid and Peptide Control of Phosphatidylinositol 4-Kinase IIα Activity on Golgi-endosomal Rafts

Waugh

Minogue

Chotai

et al. 2006

Journal of Biological Chemistry

View full text Add to dashboard Cite

The most abundant and widely expressed mammalian phosphoinositide kinase activity is contributed by phosphatidylinositol 4-kinase II␣ (PI4KII␣). In this study we demonstrate that PI4KII␣ is a novel GTP-independent target of the wasp venom tetradecapeptide mastoparan and that different mechanisms of activation occur in different subcellular membranes. Following cell membrane fractionation mastoparan specifically stimulated a high activity Golgi/ endosomal pool of PI4KII␣ independently of exogenous guanine nucleotides. Conversely, GTP␥S stimulated a low activity pool of PI4KII␣ in a separable dense membrane fraction and this response was further enhanced by mastoparan. Overexpression of PI4KII␣ increased the basal phosphatidylinositol 4-kinase activity of each membrane pool, as well as the mastoparan-dependent activities, thereby demonstrating that mastoparan specifically activates this isozyme. Both mastoparan and M7, at concentrations known to invoke secretion, stimulated PI4KII␣ with similar efficacies, resulting in an increase in the apparent V max and decrease in K m for exogenously added PI. Mastoparan also stimulated PI4KII␣ immunoprecipitated from the raft fraction, indicating that PI4KII␣ is a direct target of mastoparan. Finally we reveal a striking dependence of both basal and mastoparan-stimulated PI4KII␣ activity on endogenous cholesterol concentration and therefore conclude that changes in membrane environment can regulate PI4KII␣ activity.The wasp venom peptide mastoparan stimulates signaling by G i and G 0 heterotrimeric G-proteins by enhancing the rate of dissociation of bound GDP, thereby allowing GTP to bind. Increased G i and G 0 signaling then activates a variety of cell-type-dependent events, including secretion and ion transport.However the targets of mastoparan are by no means limited to heterotrimeric G-proteins. Mastoparan is also known to affect the activity of phospholipase D2 (1), Rho (2), nucleotide diphosphate kinase (3), calmodulin (4), glycogen phosphorylase (5), phospholipase A2 (6), p67-phox (7), and the type II phosphatidylinositol 4-kinase (PI4KII) 2 (8, 9). PI4KII␣ localizes to membranes of the Golgi-endosomal system (10, 11) where it provides the phosphatidylinositol 4-phosphate (PI4P) that is required to recruit the AP-1 clathrin adaptor complex to membranes of the trans-Golgi network (TGN) (11). Two membrane fractions containing PI4KII␣ activity have been identified using sucrose density gradient ultracentrifugation (12) and found to possess differing levels of intrinsic kinase activity both in intact membranes and in immunoprecipitates prepared from detergent lysates (13). The higher activity pool is found in membranes that possess the raft-like properties of high buoyancy in sucrose density gradients and resistance to detergent solubilization (12-14). As reported by Barylko et al. (15), rafting of PI4KII␣ is likely to arise from palmitoylation of a cysteine-rich sequence within the kinase domain (residues 174 -178, CCPCC), but whether or not a particular raft lipid enviro...

show abstract

mentioning

confidence: 99%

mentioning

confidence: 99%

Lipid and Peptide Control of Phosphatidylinositol 4-Kinase IIα Activity on Golgi-endosomal Rafts

Waugh

Minogue

Chotai

et al. 2006

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Interaction with G‐proteins has been described in different cell types [29]. In granulocytes, intracellular signaling can be influenced by interaction of pore‐forming peptides with the NADPH oxidase system [30] and degranulation can be observed. These properties have been studied almost exclusively for mastoparan.…”

mentioning

confidence: 99%

Antibacterial and antifungal properties of α‐helical, cationic peptides in the venom of scorpions from southern Africa

Moerman

Bosteels

Noppe

et al. 2002

European Journal of Biochemistry

157

View full text Add to dashboard Cite

Two novel pore-forming peptides have been isolated from the venom of the South-African scorpion Opistophtalmus carinatus. These peptides, designated opistoporin 1 and 2, differ by only one amino acid and belong to a group of a-helical, cationic peptides. For the first time, a comparison of the primary structures of a-helical pore-forming peptides from scorpion venom was undertaken. This analysis revealed that peptides in the range of 40-50 amino acids contain a typical scorpion conserved sequence S(x) 3 KxWxS(x) 5 L. An extensive study of biological activity of synthesized opistoporin 1 and parabutoporin, a poreforming peptide previously isolated from the venom of the South-African scorpion Parabuthus schlechteri, was undertaken to investigate an eventual cell-selective effect of the peptides. Opistoporin 1 and parabutoporin were most active in inhibiting growth of Gram-negative bacteria (1.3-25 lM), while melittin and mastoparan, two well-known cytolytic peptides, were more effective against Gram-positive bacteria in the same concentration range. In addition, the peptides showed synergistic activity with some antibiotics commonly used in therapy. Opistoporin 1 and parabutoporin had hemolytic activity intermediate between the least potent mastoparan and the highly lytic melittin. Furthermore, all peptides inhibited growth of fungi. Experiments with SYTOX green suggested that this effect is related to membrane permeabilization.

show abstract

“…The strong inhibitory effect that PP exerts on fMLP‐ or PMA‐induced

O_{2}^{▪ ‐}

production in PMN [16] has been difficult to explain. To our knowledge, only few other natural peptides are known to inhibit

O_{2}^{▪ ‐}

production in neutrophils: PR‐39 and mastoparan, with IC 50 values of about 5 and 2 μM, respectively [20,21]. PR‐39, a Pro‐Arg rich peptide isolated from porcine PMN, was reported to bind to the SH3‐domains of p47 phox , thereby blocking the association between p47 phox and cytochrome b 558 [20].…”

Section: Discussionmentioning

confidence: 99%

The antimicrobial peptide parabutoporin competes with p47^phox as a PKC‐substrate and inhibits NADPH oxidase in human neutrophils

Remijsen¹,

Fontayne

Verdonck³

et al. 2006

FEBS Letters

View full text Add to dashboard Cite

We investigated parabutoporin (PP), an antimicrobial scorpion peptide, to understand its inhibition on NADPH oxidase in human PMN. We show that PP is a good substrate for all PKC-isotypes, implicated in the activation of NADPH oxidase, and acts as a potent competitive inhibitor of in vitro p47 phox -phosphorylation by PKC-a, -bI, -bII and -d, but not PKC-f. In PMN, PP also inhibits the PMA-stimulated phosphorylation of p47 phox and its subsequent translocation. In contrast, PP affects the PKC-independent activation to a much lesser degree. This indicates that PP inhibits the activation of NADPH oxidase at submicromolar concentrations in a strongly PKC-dependent manner.

show abstract

Structure-function relationship in the interaction of mastoparan analogs with neutrophil NADPH oxidase

Cited by 14 publications

References 42 publications

Lipid and Peptide Control of Phosphatidylinositol 4-Kinase IIα Activity on Golgi-endosomal Rafts

Lipid and Peptide Control of Phosphatidylinositol 4-Kinase IIα Activity on Golgi-endosomal Rafts

Antibacterial and antifungal properties of α‐helical, cationic peptides in the venom of scorpions from southern Africa

The antimicrobial peptide parabutoporin competes with p47^phox as a PKC‐substrate and inhibits NADPH oxidase in human neutrophils

Contact Info

Product

Resources

About

Structure-function relationship in the interaction of mastoparan analogs with neutrophil NADPH oxidase

Cited by 14 publications

References 42 publications

Lipid and Peptide Control of Phosphatidylinositol 4-Kinase IIα Activity on Golgi-endosomal Rafts

Lipid and Peptide Control of Phosphatidylinositol 4-Kinase IIα Activity on Golgi-endosomal Rafts

Antibacterial and antifungal properties of α‐helical, cationic peptides in the venom of scorpions from southern Africa

The antimicrobial peptide parabutoporin competes with p47phox as a PKC‐substrate and inhibits NADPH oxidase in human neutrophils

Contact Info

Product

Resources

About

The antimicrobial peptide parabutoporin competes with p47^phox as a PKC‐substrate and inhibits NADPH oxidase in human neutrophils