Purification and characterization of antimicrobial peptides from the skin secretions of the carpenter frog Rana virgatipes (Ranidae, Aquarana)

Conlon, J. Michael; Abraham, Bency; Sonnevend, Ágnes; Jouenne, Thierry; Cosette, Pascal; Leprince, Jérôme; Vaudry, Hubert; Bevier, Catherine R.

doi:10.1016/j.regpep.2005.06.003

Cited by 47 publications

(24 citation statements)

References 31 publications

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“…5.3 and 6.8 g respectively) were collected under permit (GLAC-2005-SCI-0040) in October, 2005 from Fern Creek, Glacier National Park, Montana, USA. Electricallystimulated skin secretions were collected as previously described (Conlon et al, 2005a) and immediately frozen on dry ice for shipment to U.A.E. University.…”

Section: Collection Of Skin Secretionsmentioning

confidence: 99%

Peptidomic analysis of skin secretions supports separate species status for the tailed frogs, Ascaphus truei and Ascaphus montanus

Conlon

Bevier

Coquet

et al. 2007

Comparative Biochemistry and Physiology Part D: Genomics and Pr

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analysis of skin secretions supports separate species status for the tailed frogs, Ascaphus truei and Ascaphus montanus" (2007). USGS AbstractThe tailed frog Ascaphus truei Stejneger, 1899 is the most primitive extant anuran and the sister taxon to the clade of all other living frogs. The species occupies two disjunct ranges in the Northwest region of North America: the Cascade Mountains and coastal area from British Columbia to Northern California, and an inland range in the northern Rocky Mountains and the Blue and Wallowa mountains. A previous study led to the isolation of eight peptides with antimicrobial activity (termed the ascaphins) from skin secretions of A. truei from the coastal range. The present study has used peptidomic analysis to identify the products of orthologous ascaphin genes in electrically-stimulated skin secretions from inland range specimens. Structural characterization of the peptides demonstrated that ascaphins from the inland range contained the following amino acid substitutions compared with orthologs from the coastal range frogs: ascaphin-1 (Ala 12 → Glu), ascaphin-3 (Asp 4 → Glu), ascaphin-4 (Ala 19 → Ser), ascaphin-5 (Lys 12 → Thr), and ascaphin-7 (Gly 8 → Ser and Ser 20 → Asn). Orthologs of ascaphins-2, -6, and -8 were not identified but a paralog of ascaphin-5, identical to ascaphin-5 from coastal range frogs, was found. The data support the claims, derived from analysis of the nucleotide sequences of mitochondrial genes, that the inland populations of the tailed frog should be recognized as a distinct species, the Rocky Mountain tailed frog Ascaphus montanus and that the divergence of the species from A. truei probably occurred in the late Miocene (approximately 10 Mya).

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Section: Collection Of Skin Secretionsmentioning

confidence: 99%

Peptidomic analysis of skin secretions supports separate species status for the tailed frogs, Ascaphus truei and Ascaphus montanus

Conlon

Bevier

Coquet

et al. 2007

Comparative Biochemistry and Physiology Part D: Genomics and Pr

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“…This sequence was thought to play a crucial role for antibacterial activity of those peptides. However, this hypothesis was refuted after discovery of C-terminal truncated Brevinin-1 and Brevinin-2 family peptides from Rana okinavana (Conlon et al 2005b) and R. septentrionalis, respectively (Conlon et al 2005a). Those peptides did not have the characteristic C-terminal cyclic heptapeptide domain, but instead contained a C-terminallyamidated residue (Conlon et al 2005a;Conlon et al 2005b).…”

Section: Innothink Center For Research In Biomedical Innovation and Tmentioning

confidence: 99%

“…1B) (Chan et al 2006;Shai 1999). The primary structure of Brevinin-2 is also poorly conserved with the invariant amino acid residues in the peptide being Lys 7 , Cys 27 , Lys 28 , Cys 33 (Conlon et al 2005a). …”

Section: Innothink Center For Research In Biomedical Innovation and Tmentioning

confidence: 99%

An Overview of Brevinin Superfamily: Structure, Function and Clinical Perspectives

Savelyeva

Ghavami

Davoodpour

et al. 2014

Advances in Experimental Medicine and Biology

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SummaryAntimicrobial peptides are the backbone of first-line defense against various microorganisms in the animal kingdom. Thus, not surprisingly, they are gaining attention in the science and medical fields as a rich repository of new pro-drugs. Below, we focus our attention on the Brevinin family of anuran peptides. While most of them show strong antibacterial activities, some, e.g. Brevinin-2R, appear to be promising anticancer molecules, exhibiting better a therapeutic window than widely-use anticancer drugs like doxorubicin. We briefly introduce the field, followed by highlighting the promising therapeutic properties of Brevinins. Next, we provide information about the cloning and phylogenetic aspects of Brevinin genes. In the final paragraphs of this chapter, we discuss possible large-scale production methods of Brevinins, giving examples of some systems that are already in use. Towards the end, we discuss various means of modification of biologic properties of Brevinins, either by chemical modifications or by amino acid substitution and sequence rearrangements. In this context, also other unique properties of Brevinins are briefly mentioned. Finally, we discuss the future of the Brevinin field,particularly highlighting yet to be answered biologic questions, like for example presumed anti-viral and antitumor activities of Brevinin family members.2

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“…This study describes the effects on insulin secretion from BRIN-BD11 cells of seven synthetic peptides belonging to the temporin family: temporin-1Va, -1Vb, and -1Vc, first isolated from the carpenter frog R. virgatipes [15], temporin-1DRa and-1DRb from the California red-legged frog R. draytonii [18], temporin-1Oe from the mountain brown frog, R. ornativentris [19], and temporin-1TGb from Tago's brown frog R. tagoi [20]. These peptides were selected for study as they differ in cationicity, with a charge at pH 7 of +1 for temporin-10e, +2 for temporin-1Va, -1Vb, and -1Vc, and +3 for temporin-1DRa, -1DRb, and -1TGb (Fig.…”

Section: The Biological Properties Of the Temporins Are Not Confined mentioning

confidence: 99%

Insulin Releasing Properties of the Temporin Family of Antimicrobial Peptides

Abdel-Wahab¹,

Marenah²,

Flatt³

et al. 2007

PPL

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Temporin-1Vb, -1Oe, -1DRb, and -1TGb (10(-8) -10(-6)M) produced significant (p<0.05) and concentration-dependent stimulatory effects on insulin secretion from clonal rat BRIN-BD11 cells without increased release of lactate dehydrogenase. Temporin-1Va and temporin-1Vc (10(-8) - 10(-6)M) also stimulated insulin-release but were cytotoxic at 10(-6)M. Temporin-1DRa was without effect. The temporins at 10(-7) M had no effect on intracellular calcium concentrations suggesting that they stimulate insulin release via a K(ATP) channel- independent pathway.

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Purification and characterization of antimicrobial peptides from the skin secretions of the carpenter frog Rana virgatipes (Ranidae, Aquarana)

Cited by 47 publications

References 31 publications

Peptidomic analysis of skin secretions supports separate species status for the tailed frogs, Ascaphus truei and Ascaphus montanus

Peptidomic analysis of skin secretions supports separate species status for the tailed frogs, Ascaphus truei and Ascaphus montanus

An Overview of Brevinin Superfamily: Structure, Function and Clinical Perspectives

Insulin Releasing Properties of the Temporin Family of Antimicrobial Peptides

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