Isolation and amino acid sequences of alytesin and bombesin, two analogous active tetradecapeptides from the skin of European discoglossid frogs

Ánastasi, A.; Erspamer, V.; Bucci, Mariarosaria

doi:10.1016/0003-9861(72)90162-2

Cited by 123 publications

(85 citation statements)

References 12 publications

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“…It was shown in a previous paper (Bertaccini, Erspamer & Impicciatore, 1973) that bombesin (Pyr-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-ValGly-His-Leu-Met-NH2), an active tetradecapeptide isolated from methanol extracts of the skin of two European discoglossid frogs Bombina bombina and Bombina variegata variegata (Anastasi, Erspamer & Bucci, 1972), displayed a potent stimulant action on secretion from the denervated fundic pouch of the dog. There was a conspicuous increase in the volume of gastric juice accompanied by an increase in total acid and pepsin outputs and in hydrochloric acid concentration.…”

Section: Methodsmentioning

confidence: 99%

Gastrin Release by Bombesin in the Dog

Bertaccini

Erspamer²,

Melchiorri³

et al. 1974

British J Pharmacology

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163

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The intravenous infusion of bombesin produced in intact dogs and, more strikingly in dogs provided with gastric fistulae a sharp increase in plasma levels of immunoreactive gastrin and at the same time a stimulation of gastric acid secretion. Gastrin response was correlated with the dose of bombesin from approximately 0.1 μg kg−1 h−1 (threshold) to 1 μg kg−1 h−1 (maximum gastrin release). Atropine and metiamide reduced or inhibited gastric acid secretion stimulated by bombesin, but did not affect the rise in gastrin levels. Acidification of the whole stomach or of a perfused antral pouch caused a reduced or delayed response to bombesin. However, the inhibitory effect of acidification could be surmounted by prolonging the duration of bombesin infusion. Antrectomy greatly reduced the rise in gastrin levels and the increase in acid gastric secretion produced by bombesin, but left unaffected the gastric secretagogue effect of pentagastrin. It is concluded that bombesin is a potent releaser of gastrin from the antral mucosa. The possible influence of the renal effects evoked by bombesin in the dog on the gastrin response to the polypeptide is discussed.

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Section: Methodsmentioning

confidence: 99%

Gastrin Release by Bombesin in the Dog

Bertaccini

Erspamer²,

Melchiorri³

et al. 1974

British J Pharmacology

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163

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“…Neuropeptides are small molecules that, in the intestine, modulate several biological processes and modify the activities of cells responsible either for triggering tissue damage or promoting healing [4,5] . The tetradecapeptide bombesin (BBS) was originally isolated from the skin of the amphibian Bombina bombina, and is analogous to mammalian gastrin-releasing peptide [6] . In the gastrointestinal tract, BBS stimulates the secretion of various gut hormones and peptides (for example, gastrin, somatostatin, cholecystokinine, insulin, glucagon, motilin, pancreatic polypeptide and neurotensin), exerts trophic effects on intestinal mucosa and pancreas, and stimulates intestinal motility [7,8] .…”

Section: Introductionmentioning

confidence: 99%

Ameliorative effects of bombesin and neurotensin on trinitrobenzene sulphonic acid-induced colitis, oxidative damage and apoptosis in rats

Akçan¹,

Muhtaroğlu²,

Akgün³

et al. 2008

WJG

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AIM:To investigate the effects of bombesin (BBS) and neurotensin (NTS) on apoptosis and colitis in an ulcerative colitis model. METHODS:In this study, a total of 50 rats were divided equally into 5 groups. In the control group, no colitis induction or drug administration was performed. Colitis was induced in all other groups. Following the induction of colitis, BBS, NTS or both were applied to three groups of rats. The remaining group (colitis group) received no treatment. On the 11th d after induction of colitis and drug treatment, blood samples were collected for TNF-α and IL-6 level studies. Malondialdehyde (MDA), carbonyl, myeloperoxidase (MPO) and caspase-3 activities, as well as histopathological findings, evaluated in colonic tissues. R E S U LT S :A c c o r d i n g t o t h e m a c r o s c o p i c a n d microscopic findings, the study groups treated with BBS, NTS and BBS + NTS showed significantly lower damage and inflammation compared with the colitis group (macroscopic score, 2.1 ± 0.87, 3.7 ± 0.94 and 2.1 ± 0.87 vs 7.3 ± 0.94; microscopic score, 2.0 ± 0.66, 3.3 ± 0.82 and 1.8 ± 0.63 vs 5.2 ± 0.78, P < 0.01). TNF-α and IL-6 levels were increased significantly in all groups compared with the control group. These increases were significantly smaller in the BBS, NTS and BBS + NTS groups compared with the colitis group (TNF-α levels, 169. CONCLUSION:The results of this study suggest BBS and NTS, through their anti-inflammatory actions, support the maintenance of colonic integrity and merit consideration as potential agents for ameliorating colonic inflammation.

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“…These peptides generally belong to families of bioactive peptides, which through evolution have given rise to counterparts in mammals, such as bradykinins (Chen et al 2002), caerulein/cholecystokinin (Anastasi et al 1968), bombesin/gastrin-releasing peptide (Anastasi et al 1972), exendin-4/glucagon like peptide-1 (Chen & Drucker 1997), tachykinins (Falconieri Erspamer et al 1984), calcitonin gene-related peptide (Seon et al 2000), and opioids and neuropeptides (Broccarda et al 1981).…”

Section: Introductionmentioning

confidence: 99%

Brevinin-1 and multiple insulin-releasing peptides in the skin of the frog Rana palustris

Marenah¹,

Flatt²,

Orr³

et al. 2004

Journal of Endocrinology

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Few studies have comprehensively examined amphibian granular gland secretions for novel insulinotropic peptides. This study involved isolation and characterisation of biologically active peptides from the skin secretions of Rana palustris frogs. Crude secretions obtained by mild electrical stimulation from the dorsal skin surface were purified by reversed-phase HPLC on a semipreparative Vydac C18 column, yielding 80 fractions. These fractions were assayed for insulin-releasing activity using glucoseresponsive BRIN-BD11 cells. Acute 20 min incubations were performed in Krebs Ringer bicarbonate buffer supplemented with 5·6 mmol/l glucose in the absence (control) and presence of various fractions. Fractions 29-54 and fractions 68-75 showed significant 2·0-6·5-fold increases in insulin-releasing activity (P,0·001). The fractions showing most prominent insulinotropic activity were further purified to single homogeneous peaks, which, on testing, evoked 1·5-2·8-fold increases in insulin release (P,0·001). The structures of the purified peptides were determined by mass spectrometry and N-terminal amino acid sequencing. Electrospray ionisation ion-trap mass spectrometry analysis revealed molecular masses of 2873·5-8560·4 Da. Sufficient material was isolated to determine the primary amino acid sequence of the 2873·5 Da peptide, revealing a 27 amino acid sequence, ALSILRGLEKLAKMGIALTNCKATKKC, repressing palustrin-1c. The database search for this peptide showed a 48% homology with brevinin-1, an antimicrobial peptide isolated from various Rana species, which itself stimulated insulin release from BRIN-BD11 cells in a concentrationdependent manner. In conclusion, the skin secretions of R. palustris frogs contain a novel class of peptides with insulin-releasing activity that merit further investigation.

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Isolation and amino acid sequences of alytesin and bombesin, two analogous active tetradecapeptides from the skin of European discoglossid frogs

Cited by 123 publications

References 12 publications

Gastrin Release by Bombesin in the Dog

Gastrin Release by Bombesin in the Dog

Ameliorative effects of bombesin and neurotensin on trinitrobenzene sulphonic acid-induced colitis, oxidative damage and apoptosis in rats

Brevinin-1 and multiple insulin-releasing peptides in the skin of the frog Rana palustris

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