Evidence map›Paper›PMID 28726377›Full record

ArticleAnalytical chemistry2017

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

Qing Yu, Alejandra Canales, Matthew S Glover, Rahul Das, Xudong Shi, Yang Liu, Mark P Keller, Alan D Attie, Lingjun Li

Abstract read
In one paragraph

Article in Analytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
6.0field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 51 citations in OpenAlex.

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  5. Peptidomics.Nature reviews. Methods primers · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Qing YuSchool of Pharmacy, University of Wisconsin , Madison, Wisconsin 53705, United States.ORCID 0000-0003-0468-5353
Alejandra CanalesDepartment of Biochemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.
Matthew S GloverSchool of Pharmacy, University of Wisconsin , Madison, Wisconsin 53705, United States.
Rahul DasDepartment of Biochemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.
Xudong ShiDepartment of Surgery, Wisconsin Institute for Medical Research , Madison, Wisconsin 53705, United States.
Yang LiuDepartment of Chemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.
Mark P KellerDepartment of Biochemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.
Alan D AttieDepartment of Biochemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.
Lingjun LiSchool of Pharmacy, University of Wisconsin , Madison, Wisconsin 53705, United States.ORCID 0000-0003-0056-3869
University of Wisconsin–Madison · USWisconsin Institutes for Discovery · US

Funding

Institutional Training in the Genomic SciencesT32HG002760 · NHGRI · UNIVERSITY OF WISCONSIN-MADISON · PI Qiongshi Lu · 2003 to 2026
$17.7M
Training Program in Translational Cardiovascular Science (TPTCS)T32HL007936 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI Lee Lochbaum Eckhardt, Gail A Robertson · 2001 to 2026
$11.6M
Mass Spectrometric Studies of Neuropeptides in FeedingR01DK071801 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI · 2006 to 2026
$6.7M
Acquisition of a High-Field Dual Source FTICR-MS for Pharmaceutical ResearchS10RR029531 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2011 to 2011
$2.1M
The Role of Sorcs1 and Sortilin in Diabetes SusceptibilityR01DK102948 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI ATTIE, ALAN D · 2015 to 2019
$1.7M
Mass Defect-based Chemical Tags for Multiplex Glycan QuantitationR21AG055377 · NIA · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2016 to 2017
$603k
NCRR NIH HHS S10 RR029531NHGRI NIH HHS T32 HG002760NHLBI NIH HHS T32 HL007936NIA NIH HHS R21 AG055377NIDDK NIH HHS R01 DK071801NIDDK NIH HHS R01 DK102948
6 · The paper itself

Abstract

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.

Indexed as

AnimalsGlycosylationHumansInsulinIntracellular Signaling Peptides and ProteinsIslets of LangerhansMass SpectrometryMiceTissue Culture TechniquesInsulinIntracellular Signaling Peptides and Proteins

Identifiers

PMID28726377
PMCPMC6314835
OpenAlexW2738682266

What OpenQuestion holds

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LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.