Structure and pharmacological actions of phyllocaerulein, a caerulein‐like nonapeptide: its occurrence in extracts of the skin of Phyllomedusa sauvagei and related Phyllomedusa species

Abstract

. The South American amphibian Phyllomedusa sauvagei contains in its skin large amounts of a polypeptide closely resembling caerulein in its pharmacological actions. This polypeptide, called phyllocaerulein, was obtained in a pure form, and upon acid hydrolysis, enzymic digestion and end‐group determination experiments it proved to be a nonapeptide of the following compositionPyr‐Glu‐Tyr(SO3H)‐Thr‐Gly‐Trp‐Met‐Asp‐Phe‐NH2It may be seen that caerulein and phyllocaerulein have in common the C‐terminal heptapeptide and the N‐terminal pyroglutamyl residue. . Phyllocaerulein is indistinguishable from caerulein even in parallel bio‐assay. However, the former polypeptide seems to be somewhat more potent than the latter on all the preparations tested. . In different batches of Phyllomedusa sauvagei skin the phyllocaerulein content ranged between 150 and 600 μg/g of fresh tissue.Phyllocaerulein or similar polypeptides occur also in the skin of several other Phyllomedusa species, among which are Phyll. burmeisteri, Phyll. dachnicolor, Phyll, helenae, Phyll. annae, Phyll. callidryas and Phyll. bicolor. . The qualitative identification and quantitative estimation of caerulein‐like polypeptides in crude skin extracts may be complicated by the concomitant occurrence of other active polypeptides. These, however, are poorly effective on some test preparations which seem to respond selectively to caerulein. . Like that of caerulein, the biological significance of phyllocaerulein is completely obscure.

Analysis of sulfated peptides from the skin secretion of the Pachymedusa dacnicolor frog using IMAC‐Ga enrichment and high‐resolution mass spectrometry

“…After de novo sequencing and searching against protein data banks it was identified as phyllocaerulein (pEEY s TGWMDF‐NH 2 ). Phyllocaerulein is a well‐studied sulfated peptide which was characterized early on by Anastasi et al . It is also found in the skin secretions of P. dacnicolor and other frog species belonging to the Phyllomedusinae genus.…”

Cholecystokinin Expression in Tumors: Biogenetic and Diagnostic Implications

“…It is possible that the common ancestor resembles the cionin peptide isolated from protochordean neurons [7]. The frog skin peptides cerulein and phyllocerulein [15,16] are also members of the family (Figure 1). Only CCK and gastrin gene products, however, represent the family in mammals.…”

PH-sauvagine from the skin secretion of Phyllomedusa hypochondrialis: A novel CRF-like peptide with smooth muscle contraction activity

“…Phyllomedusa hypochondrialis, the so-called orange-legged leaf frog, is a typical South American species, distributed in the east of the Andes from Colombia and the Guianas southward to Argentina, Paraguay, northeastern and southeastern Brazil (Frost, 2004). A wide variety of peptides have been isolated from members of the subfamily Phyllomedusinae and these can be grouped, on a primary structural basis, into seven distinct families: the caeruleins (phyllocaerulein), the tachykinins (phyllomedusin), the bombesins (phyllolitorin, [Leu8]-phyllolitorin, rohdei-litorin), the bradykinins (phyllokinin), the sauvagines, the dermorphins (dermorphin, [Hyp6] -dermorphin) and the tryptophyllins (Anastasi et al, 1966(Anastasi et al, , 1969Anastasi and Erspamer, 1970;Barra et al, 1985;Mignogna et al, 1997;Montecucchi et al, 1980;Montecucchi et al, 1981Montecucchi et al, , 1989Montecucchi, 1985;Yasuhara et al, 1983).…”