Evidence map›Paper›PMID 28218815›Full record

ArticleChembiochem : a European journal of chemical biology2017

Glycoengineering of Esterase Activity through Metabolic Flux-Based Modulation of Sialic Acid.

Mohit P Mathew, Elaine Tan, Jason W Labonte, Shivam Shah, Christopher T Saeui, Lingshu Liu, Rahul Bhattacharya, Patawut Bovonratwet, Jeffrey J Gray, Kevin J Yarema

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

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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

10 authors at 2 institutions in 1 country.

Mohit P MathewDepartment of Biomedical Engineering and, Translational Tissue Engineering Center, The Johns Hopkins University, 5029 Robert H. & Clarice Smith Building, 400 North Broadway, Baltimore, MD, 21231, USA.
Elaine TanDepartment of Biomedical Engineering and, Translational Tissue Engineering Center, The Johns Hopkins University, 5029 Robert H. & Clarice Smith Building, 400 North Broadway, Baltimore, MD, 21231, USA.
Jason W LabonteDepartment of Chemical and Biochemical Engineering, The Johns Hopkins University, 5029 Robert H. & Clarice Smith Building, 400 North Broadway, Baltimore, MD, 21231, USA.
Shivam ShahDepartment of Biomedical Engineering and, Translational Tissue Engineering Center, The Johns Hopkins University, 5029 Robert H. & Clarice Smith Building, 400 North Broadway, Baltimore, MD, 21231, USA.
Christopher T SaeuiDepartment of Biomedical Engineering and, Translational Tissue Engineering Center, The Johns Hopkins University, 5029 Robert H. & Clarice Smith Building, 400 North Broadway, Baltimore, MD, 21231, USA.
Lingshu LiuDepartment of Biomedical Engineering and, Translational Tissue Engineering Center, The Johns Hopkins University, 5029 Robert H. & Clarice Smith Building, 400 North Broadway, Baltimore, MD, 21231, USA.
Rahul BhattacharyaDepartment of Biomedical Engineering and, Translational Tissue Engineering Center, The Johns Hopkins University, 5029 Robert H. & Clarice Smith Building, 400 North Broadway, Baltimore, MD, 21231, USA.
Patawut BovonratwetDepartment of Biomedical Engineering and, Translational Tissue Engineering Center, The Johns Hopkins University, 5029 Robert H. & Clarice Smith Building, 400 North Broadway, Baltimore, MD, 21231, USA.
Jeffrey J GrayDepartment of Chemical and Biochemical Engineering, The Johns Hopkins University, 5029 Robert H. & Clarice Smith Building, 400 North Broadway, Baltimore, MD, 21231, USA.
Kevin J YaremaDepartment of Biomedical Engineering and, Translational Tissue Engineering Center, The Johns Hopkins University, 5029 Robert H. & Clarice Smith Building, 400 North Broadway, Baltimore, MD, 21231, USA.
University of Baltimore · USJohns Hopkins University · US

Funding

Probing the Connections between Monosaccharide Analogs, Sialic Acid Metabolism, aR01CA112314 · NCI · JOHNS HOPKINS UNIVERSITY · PI YAREMA, KEVIN J · 2005 to 2022
$4.5M
Prediction of the Structure of Therapeutic Antibodies with their AntigensR01GM078221 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GRAY, JEFFREY J · 2006 to 2020
$4.0M
Computational Modeling of MUC1 Glycoforms for the Development of Cancer TherapeutF32CA189246 · NCI · JOHNS HOPKINS UNIVERSITY · PI LABONTE, JASON WILLIAM · 2014 to 2016
$169k
NCI NIH HHS F32 CA189246NCI NIH HHS R01 CA112314NIGMS NIH HHS R01 GM078221
6 · The paper itself

Abstract

This report describes the metabolic glycoengineering (MGE) of intracellular esterase activity in human colon cancer (LS174T) and Chinese hamster ovary (CHO) cells. In silico analysis of carboxylesterases CES1 and CES2 suggested that these enzymes are modified with sialylated N-glycans, which are proposed to stabilize the active multimeric forms of these enzymes. This premise was supported by treating cells with butanolylated ManNAc to increase sialylation, which in turn increased esterase activity. By contrast, hexosamine analogues not targeted to sialic acid biosynthesis (e.g., butanoylated GlcNAc or GalNAc) had minimal impact. Measurement of mRNA and protein confirmed that esterase activity was controlled through glycosylation and not through transcription or translation. Azide-modified ManNAc analogues widely used in MGE also enhanced esterase activity and provided a way to enrich targeted glycoengineered proteins (such as CES2), thereby providing unambiguous evidence that the compounds were converted to sialosides and installed into the glycan structures of esterases as intended. Overall, this study provides a pioneering example of the modulation of intracellular enzyme activity through MGE, which expands the value of this technology from its current status as a labeling strategy and modulator of cell surface biological events.

Indexed as

Protein Processing, Post-TranslationalAcetylgalactosamineAcetylglucosamineAnimalsBinding SitesButyric AcidCarboxylesteraseCarboxylic Ester HydrolasesCell Line, TumorCHO CellsCricetulusEpithelial CellsGlycosylationHexosaminesHumansMetabolic EngineeringAcetylgalactosamineAcetylglucosamineButyric AcidCarboxylesteraseCarboxylic Ester HydrolasesCES1 protein, humanCES2 protein, humanHexosaminesN-acetylmannosamineSialic AcidscarboxylesterasehexosaminesManNAcmetabolic glycoengineeringsialic acid

Identifiers

PMID28218815
PMCPMC5757160
OpenAlexW2591423324

What OpenQuestion holds

Textmetadata
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.