Evidence map›Paper›PMID 22457533›Full record

ArticleMolecular & cellular proteomics : MCP2012

Metabolic flux increases glycoprotein sialylation: implications for cell adhesion and cancer metastasis.

Ruben T Almaraz, Yuan Tian, Rahul Bhattarcharya, Elaine Tan, Shih-Hsun Chen, Matthew R Dallas, Li Chen, Zhen Zhang, Hui Zhang, Konstantinos Konstantopoulos and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

69 citing papers in PubMed, 109 citations in OpenAlex.

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  15. Altered glycosylation in pancreatic cancer and beyond.The Journal of experimental medicine · 2022
    Review
  16. The Applications of Metabolic Glycoengineering.Frontiers in cell and developmental biology · 2022
    Review
  17. Site-specificiScience · 2021
    Article
  18. Article
  19. Article
  20. Review

9 more citing papers are in PubMed but not listed here.

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

11 authors at 1 institution in 1 country.

Ruben T AlmarazDepartment of Chemical and Biomolecular Engineering, The Johns Hopkins Medical Institution, Baltimore, MD, USA.
Yuan Tian
Rahul Bhattarcharya
Elaine Tan
Shih-Hsun Chen
Matthew R Dallas
Li Chen
Zhen Zhang
Hui Zhang
Konstantinos Konstantopoulos
Kevin J Yarema
Johns Hopkins University · US

Funding

Shared Resource CoresP01HL107153 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2011 to 2017
$16.8M
Glycoprotein biomarkers for the early detection of aggressive prostate cancerU01CA152813 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2010 to 2021
$6.2M
Probing the Connections between Monosaccharide Analogs, Sialic Acid Metabolism, aR01CA112314 · NCI · JOHNS HOPKINS UNIVERSITY · PI YAREMA, KEVIN J · 2005 to 2022
$4.5M
Molecular Characterization of Cell-Cell Interactions in Cancer MetastasisR01CA101135 · NCI · JOHNS HOPKINS UNIVERSITY · PI KONSTANTOPOULOS, KONSTANTINOS · 2003 to 2011
$2.5M
NCI NIH HHS R01 CA101135NCI NIH HHS R01CA101135NCI NIH HHS R01 CA112314NCI NIH HHS R01CA112314NCI NIH HHS U01 CA152813NCI NIH HHS U01CA152813NHLBI NIH HHS P01 HL107153NHLBI NIH HHS P01HL107153-01
6 · The paper itself

Abstract

This study reports a global glycoproteomic analysis of pancreatic cancer cells that describes how flux through the sialic acid biosynthetic pathway selectively modulates a subset of N-glycosylation sites found within cellular proteins. These results provide evidence that sialoglycoprotein patterns are not determined exclusively by the transcription of biosynthetic enzymes or the availability of N-glycan sequons; instead, bulk metabolic flux through the sialic acid pathway has a remarkable ability to increase the abundance of certain sialoglycoproteins while having a minimal impact on others. Specifically, of 82 glycoproteins identified through a mass spectrometry and bioinformatics approach, ≈ 31% showed no change in sialylation, ≈ 29% exhibited a modest increase, whereas ≈ 40% experienced an increase of greater than twofold. Increased sialylation of specific glycoproteins resulted in changes to the adhesive properties of SW1990 pancreatic cancer cells (e.g. increased CD44-mediated adhesion to selectins under physiological flow and enhanced integrin-mediated cell mobility on collagen and fibronectin). These results indicate that cancer cells can become more aggressively malignant by controlling the sialylation of proteins implicated in metastatic transformation via metabolic flux.

Indexed as

Neoplasm MetastasisCell AdhesionCell Line, TumorCell MovementCollagenFibronectinsFlow CytometryGene ExpressionHumansHyaluronan ReceptorsIntegrin alpha6Models, MolecularNeoplasm ProteinsPancreatic NeoplasmsSelectinsSialic AcidsCollagenFibronectinsHyaluronan ReceptorsIntegrin alpha6Neoplasm ProteinsSelectinsSialic AcidsSialoglycoproteins

Identifiers

PMID22457533
PMCPMC3394959
OpenAlexW2137830517

What OpenQuestion holds

Textmetadata
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.