Expression of genes encoding antimicrobial and bradykinin-related peptides in skin of the stream brown frog Rana sakuraii

Suzuki, Hirohumi; Iwamuro, Shawichi; Ohnuma, Aya; Coquet, Laurent; Leprince, Jérôme; Jouenne, Thierry; Vaudry, Hubert; Taylor, Christopher K.; Abel, Peter W.; Conlon, J. Michael

doi:10.1016/j.peptides.2006.10.016

Cited by 51 publications

(23 citation statements)

References 28 publications

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“…Temporins are one of the largest groups of antimicrobial peptides within the cationic host defence peptide family. They were originally isolated from skin secretions of the frog Rana temporaria, and are amphipathic a-helical peptides of 8e19 residues with a low net positive charge (0 to þ3) and C-terminal amidation (Mangoni et al, 2007;Suzuki et al, 2007). The reasonably high homology of the temporin-like Dq toxins would suggest potentially similar biological activity, especially given the conservation of the common Pro and Leu residues found in temporin peptide families (Simmaco et al, 1996; residues in green boxes in Fig 6C).…”

Section: Dinoponeratoxinsmentioning

confidence: 99%

Diversity of peptide toxins from stinging ant venoms

Aili

Touchard

Escoubas³

et al. 2014

Toxicon

100

151

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Ants (Hymenoptera: Formicidae) represent a taxonomically diverse group of arthropods comprising nearly 13,000 extant species. Sixteen ant subfamilies have individuals that possess a stinger and use their venom for purposes such as a defence against predators, competitors and microbial pathogens, for predation, as well as for social communication. They exhibit a range of activities including antimicrobial, haemolytic, cytolytic, paralytic, insecticidal and pain-producing pharmacologies. While ant venoms are known to be rich in alkaloids and hydrocarbons, ant venoms rich in peptides are becoming more common, yet remain understudied. Recent advances in mass spectrometry techniques have begun to reveal the true complexity of ant venom peptide composition. In the few venoms explored thus far, most peptide toxins appear to occur as small polycationic linear toxins, with antibacterial properties and insecticidal activity. Unlike other venomous animals, a number of ant venoms also contain a range of homodimeric and heterodimeric peptides with one or two interchain disulfide bonds possessing pore-forming, allergenic and paralytic actions. However, ant venoms seem to have only a small number of monomeric disulfide-linked peptides. The present review details the structure and pharmacology of known ant venom peptide toxins and their potential as a source of novel bioinsecticides and therapeutic agents.

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Section: Dinoponeratoxinsmentioning

confidence: 99%

Diversity of peptide toxins from stinging ant venoms

Aili

Touchard

Escoubas³

et al. 2014

Toxicon

100

151

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show abstract

“…Amphibian skin has proven a remarkably rich storehouse of regulatory peptides including kinins, while the occurrence of BK-related peptides in skin secretions of frogs has been investigated by several groups (1,(10)(11)(12)). Yet, the search for the existence of at least one component of the kallikrein-kinin system in anuran plasma has been unsuccessful, for instance one in the form of a biosynthetic precursor (e.g., pre-pro-BK) (13).…”

Section: Introductionmentioning

confidence: 99%

Identification of bradykinin: related peptides from Phyllomedusa nordestina skin secretion using electrospray ionization tandem mass spectrometry after a single-step liquid chromatography

Conceição¹,

Bruni²,

Sciani³

et al. 2009

J. Venom. Anim. Toxins incl. Trop. Dis

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ABSTRACT:Amphibian skin secretions are a source of potential new drugs with medical and biotechnological applications. Rich in peptides produced by holocrinetype serous glands in the integument, these secretions play different roles, either in the regulation of physiological skin functions or in the defense against predators or microorganisms. The aim of the present work was to identify novel peptides with bradykinin-like structure and/or activity present in the skin of Phyllomedusa nordestina. In order to achieve this goal, the crude skin secretion of this frog was prefractionated by solid phase extraction and separated by reversed-phase chromatography. The fractions were screened for low-molecular-mass peptides and sequenced by mass spectrometry. It was possible to identify three novel bradykininrelated peptides, namely: KPLWRL-NH 2 (Pnor 3), RPLSWLPK (Pnor 5) and VPPKGVSM (Pnor 7) presenting vascular activities as assessed by intravital microscopy. Pnor 3 and Pnor 7 were able to induce vasodilation. On the other hand, Pnor 5 was a potent vasoconstrictor. These effects were reproduced by their synthetic analogues.

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“…Melittin is the basic active component of the venoms of honeybees Apis mellifera and Apis florae 39. Melittin‐related peptides (MRPs) have been reported as components of the secretions of brown frogs: European R.temporaria 21, 40 and Japanese R. tagoi 41 and R. sakuraii 42. MRPs as well as authentic melittin are active towards Gram‐positive and Gram‐negative microorganisms as well as fungi.…”

Section: Resultsmentioning

confidence: 99%

Mass spectrometric study of peptides secreted by the skin glands of the brown frog Rana arvalis from the Moscow region

Samgina¹,

Artemenko²,

Gorshkov³

et al. 2009

Rapid Comm Mass Spectrometry

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A high-performance liquid chromatography nano-electrospray ionization Fourier transform mass spectrometry (HPLC/nanoESI-FTMS) approach involving recording of collision-activated dissociation (CAD) and electron-capture dissociation (ECD) spectra of an intact sample and two its modifications after performic oxidation and reduction followed by carboxamidomethylation helps to establish peptide profiles in the crude secretion of frog species at mid-throughput level, including de novo sequencing. The proposed derivatization procedures allow increasing of the general sequence coverage in the backbone, providing complementary information and, what is more important, reveal the amino acid sequence in the cystine ring ('rana box'). Thus purely mass spectrometric efficient sequencing becomes possible for longer than usual proteolytic peptides. Seventeen peptides belonging to four known families were identified in the secretion of the European brown frog Rana arvalis inhabiting the Moscow region in Russia. Ranatuerins, considered previously a unique feature of the North American species, as well as a new melittin-related peptide, are worth special mention. The developed approach was previously successfully used for the identification of peptides in the skin secretion of the Caucasian green frog Rana ridibunda.

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Expression of genes encoding antimicrobial and bradykinin-related peptides in skin of the stream brown frog Rana sakuraii

Cited by 51 publications

References 28 publications

Diversity of peptide toxins from stinging ant venoms

Diversity of peptide toxins from stinging ant venoms

Identification of bradykinin: related peptides from Phyllomedusa nordestina skin secretion using electrospray ionization tandem mass spectrometry after a single-step liquid chromatography

Mass spectrometric study of peptides secreted by the skin glands of the brown frog Rana arvalis from the Moscow region

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