Evidence map›Paper›PMID 22643896›Full record

ArticleNature communications2012

O-glycosylation modulates integrin and FGF signalling by influencing the secretion of basement membrane components.

E Tian, Matthew P Hoffman, Kelly G Ten Hagen

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 64 citations in OpenAlex.

  1. GALNT1 emerges as a potential therapeutic target in breast cancer.Journal of cancer research and clinical oncology · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. In vivo models of mucin biosynthesis and function.Advanced drug delivery reviews · 2022
    Review
  11. Role of Glycosylation in Vascular Calcification.International journal of molecular sciences · 2021
    Review
  12. PolypeptideMolecules (Basel, Switzerland) · 2021
    Review
  13. Article
  14. Mucin-TypeFrontiers in neuroanatomy · 2021
    Article
  15. Mucin-Type O-GalNAc Glycosylation in Health and Disease.Advances in experimental medicine and biology · 2021
    Article
  16. Differential splicing of the lectin domain of anThe Journal of biological chemistry · 2020
    Article
  17. Article
  18. Review
  19. Galnt11 regulates kidney function by glycosylating the endocytosis receptor megalin to modulate ligand binding.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Article
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

3 authors at 1 institution in 1 country.

E TianDevelopmental Glycobiology Unit, Laboratory of Cell and Developmental Biology, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892-4370, USA.
Matthew P Hoffman
Kelly G Ten Hagen
National Institutes of Health · US

Funding

Role of O-glycosylation in Animal DevelopmentZIADE000713 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI TEN HAGEN, KELLY G · 2009 to 2025
$30.6M
Growth Factor/Extracellular Matrix Interactions During Branching MorphogenesisZIADE000707 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI HOFFMAN, MATTHEW · 2009 to 2023
$14.0M
Intramural NIH HHS ZIA DE000713
6 · The paper itself

Abstract

Extracellular microenvironments have crucial roles in modulating cell interactions during development. Here we discover that a conserved protein modification (O-glycosylation) influences extracellular matrix composition during mammalian organogenesis, affecting integrin signalling and fibroblast growth factor-mediated cell proliferation. Specifically, mice deficient for an enzyme (Galnt1) that adds sugars to proteins during early stages of organogenesis resulted in intracellular accumulation of major basement membrane proteins and endoplasmic reticulum stress, with resultant effects on fibroblast growth factor signalling, epithelial cell proliferation and organ growth. Exogenous addition of basement membrane components rescued fibroblast growth factor signalling and the growth defects in a β1-integrin-dependent manner. Our work demonstrates for the first time that O-glycosylation influences the composition of the extracellular matrix during mammalian organ development, influencing specific aspects of the endoplasmic reticulum stress response, cell signalling, cell proliferation and organ growth. Our work provides insight into the role of this conserved protein modification in both development and disease.

Indexed as

AnimalsBasement MembraneBlotting, WesternCell ProliferationFibroblast Growth FactorsFluorescent Antibody TechniqueGlycosylationIntegrin beta1IntegrinsMiceModels, BiologicalN-AcetylgalactosaminyltransferasesOrgan Culture TechniquesPolypeptide N-acetylgalactosaminyltransferaseReverse Transcriptase Polymerase Chain ReactionFibroblast Growth FactorsIntegrin beta1IntegrinsN-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferase

Identifiers

PMID22643896
PMCPMC3533247
OpenAlexW1967134470

What OpenQuestion holds

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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.