Synthesis of secretin.  II.  Stepwise approach

Bodanszky, Miklos; Ondetti, Miguel A.; Levine, Seymour D.; Williams, Nina J.

doi:10.1021/ja01001a063

Cited by 104 publications

(19 citation statements)

References 2 publications

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“…5,6 The next major obstacle for secretin research was to establish its hormonal status in late 1970s. Using Bodanszky's synthetic secretin, we had successfully raised a high-titer and specific rabbit antisecretin serum to develop a specific high sensitivity radioimmunoassay method for secretin, and we used it to demonstrate that plasma secretin level is elevated in the dog and human upon duodenal administration of diluted acid and, more importantly, after ingestion of a meal.…”

Section: Milestones Of Secretin Researchmentioning

confidence: 99%

Secretin, 100 years later

Chey¹,

Chang²

2003

Journal of Gastroenterology

106

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One hundred years have elapsed since the discovery of secretin by Bayliss and Starling in 1902. In the past century, the research of secretin has gone by many milestones including isolation, purification and structural determination, chemical synthesis, establishment of its hormonal status by radioimmunoassay and immunoneutralization, identification of the specific receptor, cloning of secretin and its receptor, and identification of a secretin-releasing peptide. It has become clear that secretin is a hormone-regulating pancreatic exocrine secretion of fluid and bicarbonate, gastric acid secretion, and gastric motility. The release and actions of secretin is regulated by hormone-hormonal and neurohormonal interactions. The vagus nerve, particularly its afferent pathway, plays an essential role in the physiological actions of secretin. Substantial information about the property of the secretin receptor has been accumulated, but a potent secretin receptor-specific antagonist remains to be formulated. The neural regulatory mechanisms of the release and action of secretin await further elucidation. The physiological role of secretin in intestinal secretions and motility and extragastrointestinal organs remains to be defined. The presence of secretin and its receptor in the central nervous system is well documented, but its function as a neuropeptide has been recognized gradually and requires extensive study in the future.

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Section: Milestones Of Secretin Researchmentioning

confidence: 99%

Secretin, 100 years later

Chey¹,

Chang²

2003

Journal of Gastroenterology

106

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“…,&Aspartyl shifts have been observed during analytical studies on naturally occurring proteins [27,28,31], and the Asp-Gly structure in the peptides secretin [32,33] and PHI [34] have been noted to undergo such an internal rearrangement. Studies on synthetic peptides suggest that a ,&aspartyl shift may occur via formation of a cyclic imide which, on opening, partly gives rise to the &aspartyl peptide [35,36].…”

Section: Discussionmentioning

confidence: 99%

Identification and characterization of variant forms of the gastrin‐releasing peptide (GRP)

et al. 1983

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Porcine intestinal gastrin‐releasing peptide (GRP) has been demonstrated to be structurally identical to the previously characterized gastric GRP. Ion‐exchange and high‐performance liquid chromatography of porcine intestinal extracts have identified two variant GRP forms. Studies on one of these variant forms suggest that a β‐aspartyl shift has occurred in the Asn—His structure of GRP; such a modification in an Asn—His structure occurring in a natural peptide or protein has not been previously reported. This variant GRP, although retaining bioactivity, appears to have reduced potency in elevating canine plasma gastrin levels.

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“…Stepwise elongation from the C-terminal by one amino acid at a time using urethane-protected amino acids such as Z-amino acids and Boc-amino acids, is advantageous in avoiding epimerization during the peptide bond-forming reaction [77,217,218]. Stepwise elongation from the C-terminal by one amino acid at a time using urethane-protected amino acids such as Z-amino acids and Boc-amino acids, is advantageous in avoiding epimerization during the peptide bond-forming reaction [77,217,218].…”

Section: Methods Of Activation In Stepwise Elongationmentioning

confidence: 99%