Differential expression of genes encoding preprobrevinin-2, prepropalustrin-2, and preproranatuerin-2 in developing larvae and adult tissues of the mountain brown frog Rana ornativentris

Ohnuma, Aya; Conlon, J. Michael; Iwamuro, Shawichi

doi:10.1016/j.cbpc.2009.09.004

Cited by 16 publications

(13 citation statements)

References 32 publications

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“…Peptides present in frog skin secretion are habitually described as "antimicrobial peptides" because inhibition of bacterial growth was the method used for their detection but this does not preclude the possibility of additional or alternative biological functions in vivo. Several recent studies have implicated frog skin peptides, that were first identified on the basis of their ability to inhibit growth of microorganisms, in the regulation of apoptosis (reviewed in Conlon et al 2009c) and a direct role for dermal cytolytic peptides in controlling the replacement of larval skin cells by adult cells during metamorphosis has been suggested (Ohnuma et al 2010). Other biological activities unrelated to antimicrobial activity include the abilities of members of the temporin family to stimulate chemotaxis of neutrophils, monocytes, and macrophages by a mechanism that involves interaction with the formyl peptide receptor-like 1 (Chen et al 2004), enhance the ability of secretory phospholipase A 2 to hydrolyze anionic liposomes (Zhao and Kinnunen 2003), and relax vascular smooth muscle from rat thoracic aorta .…”

Section: Discussionmentioning

confidence: 99%

The contribution of skin antimicrobial peptides to the system of innate immunity in anurans

2010

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Cationic peptides with the propensity to adopt an amphipathic α-helical conformation in a membrane-mimetic environment are synthesized in the skins of many species of anurans (frogs and toads). These peptides frequently display cytolytic activities against a range of pathogenic bacteria and fungi consistent with the idea that they play a role in the host's system of innate immunity. However, the importance of the peptides in the survival strategy of the animal is not clearly understood. It is a common misconception that antimicrobial peptides are synthesized in the skins of all anurans. In fact, the species distribution is sporadic suggesting that their production may confer some evolutionary advantage to the organism but is not necessary for survival. Although growth inhibitory activity against the chytrid fungus Batrachochytrium dendrobatidis, responsible for anuran population declines worldwide, has been demonstrated in vitro, the ability of frog skin antimicrobial peptides to protect the animal in the wild appears to be limited and there is no clear correlation between their production by a species and its resistance to fatal chytridiomycosis. The low potency of many frog skin antimicrobial peptides is consistent with the hypothesis that cutaneous symbiotic bacteria may provide the major system of defense against pathogenic microorganisms in the environment with antimicrobial peptides assuming a supplementary role in some species.

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Section: Discussionmentioning

confidence: 99%

The contribution of skin antimicrobial peptides to the system of innate immunity in anurans

2010

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“…Metamorphosis is a key event in the development of the amphibian immune system (Rollins-Smith et al, 1997;Ohnuma et al, 2010) (reviewed in Rollins-Smith, 1998). During metamorphosis, R. sylvatica tadpoles must adapt from an aquatic to a mainly terrestrial environment, concomitant with a changing microbial environment.…”

Section: Discussionmentioning

confidence: 99%

Regulation of theRana sylvaticabrevinin-1SY antimicrobial peptide during development and in dorsal and ventral skin in response to freezing, anoxia, and dehydration

Katzenback

Holden

Falardeau

et al. 2014

Journal of Experimental Biology

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Brevinin-1SY is the only described antimicrobial peptide (AMP) of Rana sylvatica. As AMPs are important innate immune molecules that inhibit microbes, this study examined brevinin-1SY regulation during development and in adult frogs in response to environmental stress. The brevinin-1SY nucleotide sequence was identified and used for protein modeling. Brevinin-1SY was predicted to be an amphipathic, hydrophobic, alpha helical peptide that inserts into a lipid bilayer. Brevinin-1SY transcripts were detected in tadpoles and were significantly increased during the later stages of development. Effects of environmental stress (24 h anoxia, 40% dehydration or 24 h frozen) on the mRNA levels of brevinin-1SY in the dorsal and ventral skin were examined. The brevinin-1SY mRNA levels were increased in dorsal and ventral skin of dehydrated frogs, and in ventral skin of anoxic frogs, compared with controls (non-stressed). Brevinin-1SY protein levels in peptide extracts of dorsal skin showed a similar, but not significant, trend to that of brevinin-1SY mRNA levels. Antimicrobial activity of skin extracts from control and stressed animals were assessed for Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Botrytis cinerea, Rhizopus stolonifer and Pythium sulcatum using disk diffusion assays. Peptide extracts of dorsal skin from anoxic, frozen and dehydrated animals showed significantly higher inhibition of E. coli and P. sulcatum than from control animals. In ventral skin peptide extracts, significant growth inhibition was observed in frozen animals for E. coli and P. sulcatum, and in anoxic animals for B. cinerea, compared with controls. Environmental regulation of brevinin-1SY may have important implications for defense against pathogens.

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“…1B). 8,[18][19][20][21][22][23][24] Hence this peptide has been classified into the palustrin-2 family and named palustrin-2CE according to systematic nomenclature. 5) Since there are two prepropeptide cDNAs that have been isolated from adult Rana chensinensis releasing the same palustrin-2CE mature peptide, 25) the cDNA from the tadpole in this study was named as prepropalustrin-2CE3, subsequently.…”

Section: Characteristics Of the Cloned Antimicrobial Peptide Genementioning

confidence: 99%

“…6) After intensive studies, however, several antimicrobial peptides were successively identified in tadpoles of various species, including ranalexin, brevinin-2Oc, palustrin-2Oa, ranatuerin-2Ob, and ranatuerin-2Oe. [6][7][8] Purification of antimicrobial peptides from living animals or chemical synthesis is usually not sufficient, and is costly for research purpose as well as in clinical application. During the past decade, diverse purified recombinant antimicrobial peptides have been produced by various expression systems.…”

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confidence: 99%

Molecular Cloning, Expression, Purification, and Functional Characterization of Palustrin-2CE, an Antimicrobial Peptide ofRana chensinensis

Sun

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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Differential expression of genes encoding preprobrevinin-2, prepropalustrin-2, and preproranatuerin-2 in developing larvae and adult tissues of the mountain brown frog Rana ornativentris

Cited by 16 publications

References 32 publications

The contribution of skin antimicrobial peptides to the system of innate immunity in anurans

The contribution of skin antimicrobial peptides to the system of innate immunity in anurans

Regulation of theRana sylvaticabrevinin-1SY antimicrobial peptide during development and in dorsal and ventral skin in response to freezing, anoxia, and dehydration

Molecular Cloning, Expression, Purification, and Functional Characterization of Palustrin-2CE, an Antimicrobial Peptide ofRana chensinensis

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