Synthetic peptides related to caerulein1. Note 1

Ánastasi, A.; Bernardi, L.; Bertaccini, G.; Bosisio, G.; Castiglione, Roberto; Erspamer, V.; Goffredo, O.; Impicciatore, M

doi:10.1007/bf02144858

Cited by 68 publications

(18 citation statements)

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“…A similar failure of bioassay could be observed also in the distinction from each other or from caerulein of a numtber of synthetic caerulein-like polypeptides (Anastasi, Bernardi, Bertaccini, Bosisio, De Castiglione, Erspamer, Goffredo & Impicciatore, 1968).…”

Section: Discussionmentioning

confidence: 74%

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

Ánastasi

Bertaccini

Cei

et al. 1969

British J Pharmacology

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. 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.

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Section: Discussionmentioning

confidence: 74%

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

Ánastasi

Bertaccini

Cei

et al. 1969

British J Pharmacology

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“…Caerulein, like PG, contains the active, gastrin-like tetrapeptide trp-met-asp-phe-NH2 ; the part of the molecule that is thought to be responsible for stimulation of gastric and pancreatic secretion [7][8][9][10][11].…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, it has been seen that intraperitoneal administration of this drug in rats results in an analogous increase in acid mucopolysaccharides in both salivary acinary cells and glandular ducts [4], In man, salivary secretion has been shown to increase after stimulation of endogenous gastrin by meat extract [5], as well as after administration of secretin and cholecystokinin (CCK) [6], Caerulein is a decapeptide whose molecu lar structure is very similar to that of human gastrin II and CCK, especially in C-terminal amino acids [7,8]. This structural affinity is linked with a similar effect on gastric secre tion, both in experimental animals and in man [9][10][11].…”

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Inhibitory Effect of Caerulein on Salivary Secretion in Man

Loguercio¹,

Costato²,

Blanco³

1991

Digestion

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Previous works have documented that pentagastrin has a stimulatory effect on salivary secretion. In this paper, we have studied the action of caerulein, a peptide that has an active gastrin-like terminal tetrapeptide, on salivary secretion in man. Our data documented that caerulein and pentagastrin have a similar excitatory effect on gastric secretion in man, but different actions on salivary flow. Caerulein, at increasing doses, inhibits salivary flow, but not the secretion of amylase; this effect is statistically significant at 0.5 µg/kg/h which is the same dose that maximally stimulates gastric secretion. The inhibitory effect of caerulein was not reversed by previous injection of papavarin.

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“…Such a decrease in biological action by tyrosine sulfation was reported to occur in leu-enkephalin (11). In contrast with these peptides, CCK requires tyrosine sulfation for its full biological activity, and the anticoagul ant activity of hirudin was potentiated by sulfation of its tyrosine (2)(3)(4)(5)(6). This study provides evidence that the fourth amino acid of All tyrosine could influence the active site of All, possibly by affecting its binding to the receptors.…”

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confidence: 99%

“…Marked alteration of biological ac tivity by sulfation of a tyrosine residue has been reported for CCK and hirudin. CCK requires tyrosine sulfation for its action (2)(3)(4)(5), and tyrosine sulfation of synthetic hirudin peptide increases its anticoagulant activity (6).…”

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confidence: 99%

Pharmacological activity of angiotensin-II modified by tyrosine sulfation.

et al. 1990

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Abstract-An angiotensin-II analogue with a sulfated tyrosine residue was pre pared by arylsulfotransferase treatment of synthetic human angjotensin-II. Its biological activities were studied in isolated smooth muscles, and its effect on blood pressure was determined.The sulfated angiotensin-II (All-S) was about 15-30 fold less potent than angjotensin-II (All) for ileum contraction and gallbladder contraction.The hypertensive potency of AII-S was about 30-fold less than that of Al I.

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Synthetic peptides related to caerulein1. Note 1

Cited by 68 publications

References 1 publication

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

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

Inhibitory Effect of Caerulein on Salivary Secretion in Man

Pharmacological activity of angiotensin-II modified by tyrosine sulfation.

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