Rattlesnake Phospholipase A2 Increases CFTR-Chloride Channel Current and Corrects ∆ F508CFTR Dysfunction: Impact in Cystic Fibrosis

Faure, Grazyna; Bakouh, Naziha; Lourdel, Stéphane; Odolczyk, Norbert; Premchandar, Aiswarya; Servel, Nathalie; Hatton, Aurélie; Ostrowski, Maciej; Xu, Haijin; Saul, F.A.; Moquereau, Christelle; Bitam, Sara; Pranke, Iwona; Planelles, Gabrielle; Teulon, Jacques; Herrmann, Harald; Roldán, Ariel; Zielenkiewicz, Piotr; Dadlez, Michał; Lukacs, Gergely L.; Sermet‐Gaudelus, Isabelle; Ollero, Mario; Corringer, Pierre‐Jean; Edelman, Aleksander

doi:10.1016/j.jmb.2016.05.016

Cited by 22 publications

(30 citation statements)

References 46 publications

(30 reference statements)

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“…To investigate the interaction of Peptide 1 with the wt and ΔF508 NBD1, we used real‐time SPR techniques with the Biacore 2000 system (Biacore AB; GE Healthcare). The wt‐ and ΔF508‐ NBD1 molecules were covalently immobilized via their primary amino groups on a CM5 sensor chip (two independent flow‐cell) as described elsewhere . Blank control measurements were performed using one independent flow‐cell on the same sensor chip.…”

Section: Methodsmentioning

confidence: 99%

“…The wt-and DF508-NBD1 molecules were covalently immobilized via their primary amino groups on a CM5 sensor chip (two independent flowcell) as described elsewhere. 34 Blank control measurements were performed using one independent flow-cell on the same sensor chip. Binding experiments were run in TBS buffer (50 mM Tris-HCl, pH 7.4; 150 mM NaCl; 5 mM MgCl 2 ; 1 mM DTT) containing 0.005% (w/v) surfactant P20.…”

Section: Surface Plasmon Resonancementioning

confidence: 99%

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New insights into interactions between the nucleotide‐binding domain of CFTR and keratin 8

et al. 2017

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The intermediate filament protein keratin 8 (K8) interacts with the nucleotide-binding domain 1 (NBD1) of the cystic fibrosis (CF) transmembrane regulator (CFTR) with phenylalanine 508 deletion (ΔF508), and this interaction hampers the biogenesis of functional ΔF508-CFTR and its insertion into the plasma membrane. Interruption of this interaction may constitute a new therapeutic target for CF patients bearing the ΔF508 mutation. Here, we aimed to determine the binding surface between these two proteins, to facilitate the design of the interaction inhibitors. To identify the NBD1 fragments perturbed by the ΔF508 mutation, we used hydrogen-deuterium exchange coupled with mass spectrometry (HDX-MS) on recombinant wild-type (wt) NBD1 and ΔF508-NBD1 of CFTR. We then performed the same analysis in the presence of a peptide from the K8 head domain, and extended this investigation using bioinformatics procedures and surface plasmon resonance, which revealed regions affected by the peptide binding in both wt-NBD1 and ΔF508-NBD1. Finally, we performed HDX-MS analysis of the NBD1 molecules and full-length K8, revealing hydrogen-bonding network changes accompanying complex formation. In conclusion, we have localized a region in the head segment of K8 that participates in its binding to NBD1. Our data also confirm the stronger binding of K8 to ΔF508-NBD1, which is supported by an additional binding site located in the vicinity of the ΔF508 mutation in NBD1.

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Section: Methodsmentioning

confidence: 99%

Section: Surface Plasmon Resonancementioning

confidence: 99%

New insights into interactions between the nucleotide‐binding domain of CFTR and keratin 8

et al. 2017

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“…Remarkably, it was demonstrated that the CB subunit can be internalized in cerebrocortical synaptosomes, independently of the presence of CA or of its catalytic activity [ 80 ]. Finally, it was recently demonstrated that CTX can interact with nicotinic acetylcholine receptors [ 81 ] and that the CB subunit can interact with, and be an allosteric modulator of, cystic fibrosis transmembrane regulator (CTRF) chloride channel [ 82 ]. It was also demonstrated that CB is able to interact with prokaryotic proton-gated ion channel GLIC, a bacterial homolog of pentameric ligand-gated ion channels [ 83 ].…”

Section: Crotoxin a Heterodimeric Neurotoxin From Crotamentioning

confidence: 99%

Secreted Phospholipases A2 from Animal Venoms in Pain and Analgesia

Zambelli

Picolo

Fernandes

et al. 2017

Toxins

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Animal venoms comprise a complex mixture of components that affect several biological systems. Based on the high selectivity for their molecular targets, these components are also a rich source of potential therapeutic agents. Among the main components of animal venoms are the secreted phospholipases A2 (sPLA2s). These PLA2 belong to distinct PLA2s groups. For example, snake venom sPLA2s from Elapidae and Viperidae families, the most important families when considering envenomation, belong, respectively, to the IA and IIA/IIB groups, whereas bee venom PLA2 belongs to group III of sPLA2s. It is well known that PLA2, due to its hydrolytic activity on phospholipids, takes part in many pathophysiological processes, including inflammation and pain. Therefore, secreted PLA2s obtained from animal venoms have been widely used as tools to (a) modulate inflammation and pain, uncovering molecular targets that are implicated in the control of inflammatory (including painful) and neurodegenerative diseases; (b) shed light on the pathophysiology of inflammation and pain observed in human envenomation by poisonous animals; and, (c) characterize molecular mechanisms involved in inflammatory diseases. The present review summarizes the knowledge on the nociceptive and antinociceptive actions of sPLA2s from animal venoms, particularly snake venoms.

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“…Despite the neurotoxicity, several studies have pointing towards other biological activities of CTX that have potential pharmacological value such as immunomodulatory, anti-nociceptive, anti-inflammatory, anti-tumoral and anti-microbial activities (Sampaio et al, 2010;Favoretto et al, 2011;Ye et al, 2011;Wang et al, 2012;He et al, 2013;Han et al, 2014;Almeida et al, 2015;Brigatte et al, 2016;Faure et al, 2016). Thus, a more complete understanding of the neurotoxic action of CTX is relevant not only to improve the treatment of envenomation, but also to enable the biotechnological use of this toxin or new drugs derived from this protein.…”

Section: Introductionmentioning

confidence: 99%

Neuromuscular paralysis by the basic phospholipase A 2 subunit of crotoxin from Crotalus durissus terrificus snake venom needs its acid chaperone to concurrently inhibit acetylcholine release and produce muscle blockage

Cavalcante

Noronha‐Matos

Timóteo

et al. 2017

Toxicology and Applied Pharmacology

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Rattlesnake Phospholipase A2 Increases CFTR-Chloride Channel Current and Corrects ∆ F508CFTR Dysfunction: Impact in Cystic Fibrosis

Cited by 22 publications

References 46 publications

New insights into interactions between the nucleotide‐binding domain of CFTR and keratin 8

New insights into interactions between the nucleotide‐binding domain of CFTR and keratin 8

Secreted Phospholipases A2 from Animal Venoms in Pain and Analgesia

Neuromuscular paralysis by the basic phospholipase A 2 subunit of crotoxin from Crotalus durissus terrificus snake venom needs its acid chaperone to concurrently inhibit acetylcholine release and produce muscle blockage

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