Structure of the 22-residue somatostatin from catfish. An O-glycosylated peptide having multiple forms.

Andrews, P.; Pubols, M. H.; Hermodson, Mark A.; Sheares, B T; Dixon, Jack E.

doi:10.1016/s0021-9258(18)90688-5

Cited by 53 publications

(2 citation statements)

References 33 publications

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“…Another interesting discovery was glycosylation on somatostatin. Even though it was previously reported that somatostatin-22 from catfish could be glycosylated, mammalian somatostatin-14 or -28 has never been reported to have such modification. Somatostatin is a potent inhibitor of insulin secretion, and therefore, any modification may indicate an altered regulatory effect. , In addition to glycosylation on mature and intact peptide hormones, multiple truncated sequences from large peptide hormones, including glicentin and chromogranin-A, with flanking dibasic residues were identified (Table S1).…”

Section: Resultsmentioning

confidence: 94%

Targeted Mass Spectrometry Approach Enabled Discovery of O-Glycosylated Insulin and Related Signaling Peptides in Mouse and Human Pancreatic Islets

Canales

Glover

et al. 2017

Anal. Chem.

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O-Linked glycosylation often involves the covalent attachment of sugar moieties to the hydroxyl group of serine or threonine on proteins/peptides. Despite growing interest in glycoproteins, little attention has been directed to glycosylated signaling peptides, largely due to lack of enabling analytical tools. Here we explore the occurrence of naturally O-linked glycosylation on the signaling peptides extracted from mouse and human pancreatic islets using mass spectrometry (MS). A novel targeted MS-based method is developed to increase the likelihood of capturing these modified signaling peptides and to provide improved sequence coverage and accurate glycosite localization, enabling the first large-scale discovery of O-glycosylation on signaling peptides. Several glycosylated signaling peptides with multiple glycoforms are identified, including the first report of glycosylated insulin-B chain and insulin-C peptide and BigLEN. This discovery may reveal potential novel functions as glycosylation could influence their conformation and biostability. Given the importance of insulin and its related peptide hormones and previous studies of glycosylated insulin analogues, this natural glycosylation may provide important insights into diabetes research and therapeutic treatments.

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