Odorrana Research Articles

Skin bradykinin-related peptides (BRPs) and their biosynthetic precursors (kininogens): Comparisons between various taxa of Chinese and North American ranid frogs

Bradykinins and related peptides (BRPs) occur in the defensive skin secretions of many amphibians. Here we report the structures of BRPs and their corresponding biosynthetic precursor cDNAs from the Chinese brown frog, Rana chensinensis, and the North American leopard frog, Lithobates pipiens. R. chensinensis skin contained four transcripts each encoding a different kininogen whose organizations and spectrum of encoded BRPs were similar to those reported for the pickerel frog, Lithobates palustris. In contrast, from L. pipiens, a single skin kininogen was cloned whose structural organization and spectrum of mature BRPs were similar to those reported for the Chinese piebald odorous frog, Huia schmackeri. These data also implied that the endogenous precursor processing proteases in each species pair have identical site-directed specificities, which in part may be dictated by the primary structures of encoded BRPs. Thus the spectra of skin BRPs and the organization of their biosynthetic precursors are not consistent with recent taxonomy. The natural selective pressures that mould the primary structures of amphibian skin secretion peptides are thought to be related to the spectrum of predators encountered within their habitats. Thus similarities and differences in skin bradykinins may be reflective of predator spectra rather than indicative of species relatedness.

Rapid identification of precursor cDNAs encoding five structural classes of antimicrobial peptides from pickerel frog ( Rana palustris) skin secretion by single step “shotgun” cloning

The skin secretion of the North American pickerel frog ( Rana palustris) has long been known to have pronounced noxious/toxic properties and to be highly effective in defence against predators and against other sympatric amphibians. As it consists largely of a complex mixture of peptides, it has been subjected to systematic peptidomic study but there has been little focus on molecular cloning of peptide-encoding cDNAs and by deduction, the biosynthetic precursors that they encode. Here, we demonstrate that the cDNAs encoding the five major structural families of antimicrobial peptides can be elucidated by a single step “shotgun” cloning approach using a cDNA library constructed from the source material of the peptidomic studies—the defensive skin secretion itself. Using a degenerate primer pool designed to a highly conserved nucleic acid sequence 5′ to the initiation codon of known antimicrobial peptide precursor transcripts, we amplified cDNA sequences representing five major classes of antimicrobial peptides, such as esculentins, brevinins, ranatuerins, palustrins and temporins. Bioinformatic comparisons of precursor open-reading frames and nucleic acid sequences revealed high degrees of structural similarities between analogous peptides of R. palustris and the Chinese bamboo odorous frog, Rana versabilis. This approach thus constitutes a robust technique that can be used either alone or ideally, in parallel with peptidomic analysis of skin secretion, to rapidly extract primary structural information on amphibian skin secretion peptides and their biosynthetic precursors.

An antimicrobial peptide with antimicrobial activity against Helicobacter pylori

An antimicrobial peptide named odorranain-HP was identified from skin secretions of the diskless odorous frog, Odorrana grahami. It is composed of 23 amino acids with an amino acid sequence of GLLRASSVWGRKYYVDLAGCAKA. By BLAST search, odorranain-HP had similarity to antimicrobial peptide odorranain-W1 but it has a different GLLR N-terminus. The cDNA encoding odorranain-HP was cloned from the cDNA library of the skin of O. grahami. This peptide showed antimicrobial activities against tested microorganisms. Interestingly, odorranain-HP could exert antimicrobial capability against Helicobacter pylori, along with its antimicrobial activities similar to odorranain-W1. This is the first report of naturally occurring peptide with anti- H. pylori activity from amphibian skins.

Lividins: Novel antimicrobial peptide homologs from the skin secretion of the Chinese Large Odorous frog, Rana ( Odorrana) livida: Identification by “shotgun” cDNA cloning and sequence analysis

Odorous frogs of the sub-genus Odorrana are of oriental distribution, and are so called due to the foul smell of their defensive skin secretions released from specialized skin glands following stress or predator attack. Here we report the application of a “shotgun” skin secretion cDNA library cloning technique which can rapidly expedite identification of secretion bioactive peptides. From a library constructed from the skin secretion of the Large Chinese Odorous frog, Rana ( Odorrana) livida, we have identified four novel peptides whose primary structures were deduced initially from cloned precursors. Subsequently, mature peptides were located in and structurally characterized from reverse phase HPLC fractions of skin secretion. Named lividins 1–4, these were found to be structural homologs of known antimicrobial peptide families from Rana frogs. Rapid identification of novel peptides can thus be rapidly achieved using this non-invasive, non-destructive technology and the extensive similarities revealed between antimicrobial peptide precursor organization and nucleic acid sequences would lend support to the hypothesis that they have a common ancestral origin.

The Chinese bamboo leaf odorous frog ( Rana ( Odorrana) versabilis) and North American Rana frogs share the same families of skin antimicrobial peptides

The Chinese bamboo leaf odorous frog ( Rana ( Odorrana) versabilis) and the North American pickerel frog ( Rana palustris) occupy different ecological niches on two different continents with no overlap in geographical distribution. R. palustris skin secretions contain a formidable array of antimicrobial peptides including homologs of brevinin-1, esculentin-1, esculentin-2, ranatuerin-2, a temporin and a family of peptides considered of unique structural attributes when isolated, palustrins 1–3. Here we describe the structures of mature peptides and precursors of eight putative antimicrobial peptides from the skin secretion of the Chinese bamboo leaf odorous frog ( Rana ( Odorrana) versabilis). Each peptide represents a structural homolog of respective peptide families isolated from R. palustris, including two peptides identical in primary structure to palustrin 1c and palustrin 3b. Additionally, two peptides were found to be structural homologs of ranatuerin 2B and ranatuerin 2P from the closely-related North American species, Rana berlandieri (the Rio Grande leopard frog) and Rana pipiens (the Northern leopard frog), respectively. Both palustrins and ranatuerins have hitherto been considered unique to North American ranid frogs. The use of primary structures of amphibian skin antimicrobial peptides is thus questionable as a taxonomic device or alternatively, the micro-evolution and/or ancestry of ranid frogs is more highly complex than previously thought.

Auditory response characteristics of the piebald odorous frog and their implications

The piebald odorous frog (Odorrana schmackeri), the large odorous frog (Odorrana livida) and the concave-eared torrent frog (Amolops tormotus) are sympatric species living near the same torrent streams in the vicinity of Mt. Huangshan, China. A recent study demonstrated that A. tormotus can use sound signals involving ultrasonic components for communication in a noisy environment, and another sympatric species, O. livida, can also perceive ultrasonic sound. Here we report data on the hearing range of O. schmackeri by studying auditory evoked potentials and single-unit data from the torus semicircularis. This frog exhibits its two most sensitive peaks at 2 kHz and 3.5-4.0 kHz with thresholds <42 dB SPL, with an upper frequency limit of hearing at 8.5 kHz with threshold of 87 dB SPL. The upper limit is much lower than those of O. livida and A. tormotus, at 22 and 34 kHz, respectively. It suggests that sympatric species may respond differently to similar environmental selection pressures sculpting auditory communication systems.

Antiaging Medicine: Antioxidants and Aging

Antioxidants & Redox SignalingVol. 8, No. 3-4 Forum EditorialAntiaging Medicine: Antioxidants and AgingVittorio Calabrese and Mahin D. MainesVittorio CalabreseSearch for more papers by this author and Mahin D. MainesSearch for more papers by this authorPublished Online:5 May 2006https://doi.org/10.1089/ars.2006.8.362AboutSectionsPDF/EPUB ToolsPermissionsDownload CitationsTrack CitationsAdd to favorites Back To Publication ShareShare onFacebookTwitterLinked InRedditEmail FiguresReferencesRelatedDetailsCited byFood for Brain Health4 October 2021The antioxidant and antibacterial study of Canarium indicum L. latex extractIOP Conference Series: Materials Science and Engineering, Vol. 1011, No. 1The Potential of Developing Additives from Marine Bioresources for the Food Industry28 August 2020Identification and characterization of a novel gene-encoded antioxidant peptide obtained from amphibian skin secretions23 November 2018 | Natural Product Research, Vol. 34, No. 6Potential skin protective effects after UVB irradiation afforded by an antioxidant peptide from Odorrana andersoniiBiomedicine & Pharmacotherapy, Vol. 120Ultrasound-Assisted Aqueous Extraction of Phenolic, Flavonoid Compounds and Antioxidant Activity of Mucuna macrocarpa Beans: Response Surface Methodology Optimization27 December 2018 | Journal of the American College of Nutrition, Vol. 38, No. 4Identification and Characterization of a Novel Gene-encoded Antioxidant Peptide from Odorous Frog SkinProtein & Peptide Letters, Vol. 26, No. 3Optimization of heat treatment and curcumin level for the preparation of anti-oxidant rich ghee from fermented buffalo cream by Central Composite Rotatable Design15 March 2018 | Journal of Food Science and Technology, Vol. 55, No. 5Impact of extraction techniques on antioxidant capacities and phytochemical composition of polyphenol-rich extractsFood Chemistry, Vol. 237Osteoporosis and alzheimer pathology: Role of cellular stress response and hormetic redox signaling in aging and bone remodeling10 June 2014 | Frontiers in Pharmacology, Vol. 5Cellular Stress Response, Hormesis, and Vitagens in Aging and LongevityStress responses, vitagenes and hormesis as critical determinants in aging and longevity: Mitochondria as a “chi”25 April 2013 | Immunity & Ageing, Vol. 10, No. 1Há evidências científicas na medicina antienvelhecimento?Anais Brasileiros de Dermatologia, Vol. 85, No. 1Vitagenes, cellular stress response, and acetylcarnitine: Relevance to hormesisBioFactors, Vol. 35, No. 2Nuclear translocation of haeme oxygenase-1 is associated to prostate cancer20 November 2007 | British Journal of Cancer, Vol. 97, No. 12Redox Regulation of Cellular Stress Response in Aging and Neurodegenerative Disorders: Role of Vitagenes27 December 2006 | Neurochemical Research, Vol. 32, No. 4-5Heme oxygenase and cyclooxygenase in the central nervous system: A functional interplay1 January 2006 | Journal of Neuroscience Research, Vol. 84, No. 7 Volume 8Issue 3-4Mar 2006 InformationCopyright 2006, Mary Ann Liebert, Inc.To cite this article:Vittorio Calabrese and Mahin D. Maines.Antiaging Medicine: Antioxidants and Aging.Antioxidants & Redox Signaling.Mar 2006.362-364.http://doi.org/10.1089/ars.2006.8.362Published in Volume: 8 Issue 3-4: May 5, 2006PDF download

A New Cascade Frog (Amphibia: Ranidae) from Central Vietnam

A new frog species of the family Ranidae (cascade frog from Odorrana -group) is described from central Vietnam. Rana gigatympana sp. nov. is distinguished by very small body size and very large tympanum.

Bradykinins and their cDNA from piebald odorous frog, Odorrana schmackeri, skin

Bradykinin, (des-Arg 9)-bradykinin and bradykinyl-VAPAS, were identified in the skin secretion of the piebald odorous frog, Odorrana schmackeri. Using 3′- and 5′-RACE reactions, bradykinin precursor cDNA was cloned and found to contain an open-reading frame of 311 amino acid residues. The preprobradykinin was found to consist of a putative signal peptide of approximately 20 amino acid residues, followed by seven tandem repeat coding domains of 43–44 amino acids. Bradykinin and its C-terminal extended molecular form were encoded on this single precursor and could be generated by differential post-translational processing.