OCCURRENCE OF CAERULEIN IN EXTRACTS OF THE SKIN OF <i>HYLA CAERULEA</i> AND OTHER AUSTRALIAN HYLIDS

de, G.; Endean, R.; Erspamer, V.; Roseghini, M.

doi:10.1111/j.1476-5381.1968.tb00473.x

Cited by 20 publications

(6 citation statements)

References 7 publications

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“…Caerulein (I) is a decapeptide present in the skin of Hyla caerulea and other Australian hylid frogs [1,2], ofLeptodactylus pentadactylus labyrinthicus and related South American leptodactylid frogs, and of the South African amphibian Xenopus laevis [3]. The amino acid sequences reported below clearly show the striking resemblance in chemical structure existing between the caeruleins, the C-terminal ectapeptide of porcine cholecystokininpancreozymin (II) and the Cterminal hexapeptide of gastrin II 0II).…”

mentioning

confidence: 85%

Experiments on the mechanism of action of caerulein at the level of the guinea-pig ileum and colon

1970

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The action of eaerulein in guinea-pig ileum and colon was studied in vitro and in vivo. The action appears to be mediated mainly through nervous pathways, inasmuch as tetrodotoxin is able to abolish more than 90 ~ of the response. One of the mediators liberated by caerulein seems to he acetylcholine, since caerulein gives rise to increased aeetylcholine release associated with stimulation. Furthermore, it enhances the responses to pelvic nerve stimulation, whilst atropine causes a reduction in the responses. At present no data are available for determining the identity of the other mediator(s); however, serotonin and histamine seem not to he involved.

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confidence: 85%

Experiments on the mechanism of action of caerulein at the level of the guinea-pig ileum and colon

1970

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“…Cerulein was discovered from dried skins of the Australian green tree frog ( Litoria caerulea ). Its amino acid sequence is Pglu‐Gln‐Asp‐Tyr[SO 3 H]‐Thr‐Gly‐Trp‐Met‐Asp‐Phe‐NH 2 (Anastasi et al, ; De Caro et al, ). Cerulein induces pancreatitis through dysregulation of digestive enzyme production and cytoplasmic vacuolization, leading to acinar cell death and pancreatic edema and also activates NF‐κB and NADPH oxidase (Zaninovic et al, ; Kim, ).…”

Section: Introductionmentioning

confidence: 99%

Effects of cerulein on keratin 8 phosphorylation and perinuclear reorganization in pancreatic cancer cells: Involvement of downregulation of protein phosphatase 2A and alpha4

Park

Lee

2015

Environ. Toxicol.

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Toxicants can perturb cellular homeostasis by modifying phosphorylation-based signaling. In the present study, we examined the effects of cerulein, an inducer of acute pancreatitis, on keratin 8 (K8) phosphorylation. We found that cerulein dose-dependently induced K8 phosphorylation and perinuclear reorganization in PANC-1 cells, thus leading to migration and invasion. The extracellular signal-regulated kinases (ERK) inhibitor U0126 suppressed cerulein-induced phosphorylation of serine 431 and reorganization of K8. Cerulein reduced the expressions of protein phosphatase 2A (PP2A) via ubiqutination and alpha4. PP2A's involvement in K8 phosphorylation of PANC-1 cells was also confirmed by the observation that PP2A gene silencing resulted in K8 phosphorylation and migration of PANC-1 cells. Overall, these results suggest that cerulein induced phosphorylation and reorganization through ERK activation by downregulating PP2A and alpha4, leading to increased migration and invasion of PANC-1 cells. © 2015 Wiley Periodicals, Inc. Environ Toxicol 31: 2090-2098, 2016.

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“…The striking resemblance of the structure of Caerulein, a decapeptide isolated from the skin of various Australian hylid frogs (Anastasi, Erspamer & Endean, 1968; De Caro, Endean, Erspamer & Roseghini, 1968) to the C-terminal octapeptide of porcine cholecystokininpancreozymin and to the C-terminal hexapeptide of the gastrin 11, promoted extensive pharmacological investigations on its spectrum of activity (Erspamer, 1970). The mainpharmacological properties of Caerulein can be summarized as follows: stimulation of the musculature of the gallbladder, stimulation of pancreatic secretion, stimulation of choleresis (Bertaccini, Grossman, 1970), stimulation of gastric secretion and release of pancreatic hormones (Bertaccini, De Car0 & Melchiorri, 1970; De Caro, Improta & Melchiorri, 1970).…”

Section: Introductionmentioning

confidence: 99%

Effects of Caerulein on exocrine pancreatic secretion in sheep

Beretta

Ormas

Belloli

et al. 1981

Vet Pharm & Therapeutics

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caerulein administered by slow intravenous infusion at increasing dosage rates (0.1, 1.0, 5.0 and 10.0 ng/kg/min X 30 min) stimulated pancreatic juice production in sheep as well as the protein content, the amylolytic, the lipolytic and proteolytic activities of pancreatic juice samples collected at 30 min intervals. A long lasting (300 min) infusion of a high dose of Caerulein by subcutaneous route elicited stimulatory effects with reduced intensities, slower onsets but more sustained durations than those produced by the same dose level administered intravenously.

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OCCURRENCE OF CAERULEIN IN EXTRACTS OF THE SKIN OF HYLA CAERULEA AND OTHER AUSTRALIAN HYLIDS

Cited by 20 publications

References 7 publications

Experiments on the mechanism of action of caerulein at the level of the guinea-pig ileum and colon

Experiments on the mechanism of action of caerulein at the level of the guinea-pig ileum and colon

Effects of cerulein on keratin 8 phosphorylation and perinuclear reorganization in pancreatic cancer cells: Involvement of downregulation of protein phosphatase 2A and alpha4

Effects of Caerulein on exocrine pancreatic secretion in sheep

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