Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae)

Rates, Breno; Silva, Luciano; Ireno, Ivanildce C.; Leite, Felipe Silveira; Borges, Márcia Helena; Bloch, Carlos; Lima, Maria Elena de; Pimenta, Adriano M.C.

doi:10.1016/j.toxicon.2010.09.010

Cited by 16 publications

(10 citation statements)

References 82 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The unique kind of peptide in the skin secretion of sub-family Phyllomedusinae is phyllokinin (PK), which displays two amino acid residues Ile-Tyr extended at C -terminals. PK was first reported from the studies of skin of Phyllomedusa rohdei with a post-translational modification of tyrosine O -sulfation and this peptide was subsequently discovered from other species in this sub-family [ 29 , 32 , 33 , 35 , 41 , 42 ]. Similar to PK, some of the BRPs were C -terminal extended with one or two amino acid residues, which are considered to be more potent than conventional BK because the extended region could inhibit the enzymatic metabolism of degradation of the BRPs, which prolong the ligand-receptor interaction [ 43 ].…”

Section: The Distribution Of Brps Among Amphibianmentioning

confidence: 99%

A Review on Bradykinin-Related Peptides Isolated from Amphibian Skin Secretion

Chen

et al. 2015

Toxins

View full text Add to dashboard Cite

Amphibian skin secretion has great potential for drug discovery and contributes hundreds of bioactive peptides including bradykinin-related peptides (BRPs). More than 50 BRPs have been reported in the last two decades arising from the skin secretion of amphibian species. They belong to the families Ascaphidae (1 species), Bombinatoridae (3 species), Hylidae (9 speices) and Ranidae (25 species). This paper presents the diversity of structural characteristics of BRPs with N-terminal, C-terminal extension and amino acid substitution. The further comparison of cDNA-encoded prepropeptides between the different species and families demonstrated that there are various forms of kininogen precursors to release BRPs and they constitute important evidence in amphibian evolution. The pharmacological activities of isolated BRPs exhibited unclear structure–function relationships, and therefore the scope for drug discovery and development is limited. However, their diversity shows new insights into biotechnological applications and, as a result, comprehensive and systematic studies of the physiological and pharmacological activities of BRPs from amphibian skin secretion are needed in the future.

show abstract

Section: The Distribution Of Brps Among Amphibianmentioning

confidence: 99%

A Review on Bradykinin-Related Peptides Isolated from Amphibian Skin Secretion

Chen

et al. 2015

Toxins

View full text Add to dashboard Cite

show abstract

“…Bombesins-while canonical bombesin is lacking in Phyllomedusa skin, its structural homologue, phyllolitorin, has been found in P. sauvagei, P. rohdei and P. burmeisteri skin 13 . Tryptophyllins-to date, more than 90% of the representatives of this type of peptide have been reported from phyllomedusine skin 17 - 19 . Sauvagine-this peptide, with forty amino acid residues, was isolated from the skin of P. sauvagei .…”

Section: Introductionmentioning

confidence: 99%

Identification and Functional Analysis of a Novel Tryptophyllin Peptide from the Skin of the Red-eye Leaf Frog, Agalychnis callidryas

Wang¹,

Zhou²,

Chen³

et al. 2015

Int. J. Biol. Sci.

View full text Add to dashboard Cite

Amphibian skin has proved repeatedly to be a largely untapped source of bioactive peptides and this is especially true of members of the Phyllomedusinae subfamily of frogs native to South and Central America. Tryptophyllins are a group of peptides mainly found in the skin of members of this genus. In this study, a novel tryptophyllin (TPH) type 3 peptide, named AcT-3, has been isolated and structurally-characterised from the skin secretion and lyophilised skin extract of the red-eye leaf frog, Agalychnis callidryas. The peptide was identified in and purified from the skin secretion by reverse-phase HPLC. MALDI-TOF mass spectrometry and MS/MS fragmentation sequencing established its primary structure as: pGlu-Gly-Lys-Pro-Tyr-Trp-Pro-Pro-Pro-Phe-Leu-Pro-Glu, with a non-protonated molecular mass of 1538.19Da. The mature peptide possessed the canonical N-terminal pGlu residue that arises from post-translational modification of a Gln residue. The deduced open-reading frame consisted of 63 amino acid residues encoding a highly-conserved signal peptide of approximately 22 amino acid residues, an intervening acidic spacer peptide domain, a single AcT-3 encoding domain and a C terminal processing site. A synthetic replicate of AcT-3 was found to antagonise the effect of BK on rat tail artery smooth muscle and to contract the intestinal smooth muscle preparations. It was also found that AcT-3 could dose-dependently inhibit the proliferation of human prostate cancer cell lines after 72h incubation.

show abstract

“…Studies focused on venom, which examine the venom composition and mechanisms of action, have increased and, through these, several bioactive molecules have been isolated and/or identified, often of protein character [ 3 ]. We highlight studies on venoms of spiders, snakes, bees, wasps, ants, scorpions, centipedes, and frogs [ 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 ]. These studies have shown that the bioactivity of venom is related mainly to the release of cytokines as well as inflammatory (e.g., nitric oxide) and lipid (e.g., prostaglandins) mediators [ 12 ].…”

Section: Introductionmentioning

confidence: 99%

Analysis of Protein Composition and Bioactivity of Neoponera villosa Venom (Hymenoptera: Formicidae)

Pessoa

Silva

Dias

et al. 2016

IJMS

View full text Add to dashboard Cite

Ants cause a series of accidents involving humans. Such accidents generate different reactions in the body, ranging from a mild irritation at the bite site to anaphylactic shock, and these reactions depend on the mechanism of action of the venom. The study of animal venom is a science known as venomics. Through venomics, the composition of the venom of several ant species has already been characterized and their biological activities described. Thus, the aim of this study was to evaluate the protein composition and biological activities (hemolytic and immunostimulatory) of the venom of Neoponera villosa (N. villosa), an ant widely distributed in South America. The protein composition was evaluated by proteomic techniques, such as two-dimensional electrophoresis. To assess the biological activity, hemolysis assay was carried out and cytokines were quantified after exposure of macrophages to the venom. The venom of N. villosa has a profile composed of 145 proteins, including structural and metabolic components (e.g., tubulin and ATPase), allergenic and immunomodulatory proteins (arginine kinase and heat shock proteins (HSPs)), protective proteins of venom (superoxide dismutase (SOD) and catalase) and tissue degradation proteins (hyaluronidase and phospholipase A2). The venom was able to induce hemolysis in human erythrocytes and also induced release of both pro-inflammatory cytokines, as the anti-inflammatory cytokine release by murine macrophages. These results allow better understanding of the composition and complexity of N. villosa venom in the human body, as well as the possible mechanisms of action after the bite.

show abstract

Peptidomic dissection of the skin secretion of Phasmahyla jandaia (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae)

Cited by 16 publications

References 82 publications

A Review on Bradykinin-Related Peptides Isolated from Amphibian Skin Secretion

A Review on Bradykinin-Related Peptides Isolated from Amphibian Skin Secretion

Identification and Functional Analysis of a Novel Tryptophyllin Peptide from the Skin of the Red-eye Leaf Frog, Agalychnis callidryas

Analysis of Protein Composition and Bioactivity of Neoponera villosa Venom (Hymenoptera: Formicidae)

Contact Info

Product

Resources

About