Evidence map›Paper›PMID 14562042›Full record

ArticleOncogene2003

Ras oncogene directs expression of a differentially sialylated, functionally altered beta1 integrin.

Eric Clinton Seales, Gustavo Adolfo Jurado, Anuj Singhal, Susan Lynn Bellis

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2003. 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
1.3field-weighted citation impact, top 23% 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, 127 citations in OpenAlex.

  1. Article
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  9. Review
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  11. Article
  12. Article
  13. ST6Gal1: Oncogenic signaling pathways and targets.Frontiers in molecular biosciences · 2022
    Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

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

4 authors at 1 institution in 1 country.

Eric Clinton SealesDepartment of Physiology and Biophysics, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Gustavo Adolfo Jurado
Anuj Singhal
Susan Lynn Bellis
University of Alabama at Birmingham · US

Funding

Regulation of beta1 integrin glycosylation by rasR01CA084248 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BELLIS, SUSAN L · 2002 to 2011
$2.4M
VOCATIONAL EVALUATION OF PATIENTS WITH RHEUMATOID ARTHRITISP60AR020614 · NIAMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI HAGOOD, JAMES S · 1986 to 2001
$2.4M
NCI NIH HHS R01CA84248NIAMS NIH HHS 5 P60 AR20614-23
6 · The paper itself

Abstract

Intense investigation has centered on understanding the regulation of integrin cell adhesion receptors. In the present study, we propose that variant N-glycosylation represents an important mechanism for regulation of beta1, but not beta3 or beta5 integrins. We find that expression of oncogenic ras in HD3 colonocytes causes increased alpha2-6 sialylation of beta1 integrins, whereas expression of dominant-negative ras induces decreased alpha2-6 sialylation, relative to cells with wild-type ras. In contrast, neither beta3 nor beta5 integrins are alpha2-6 sialylated, regardless of the state of ras activation. Results from RT-PCR analyses suggest that differential integrin sialylation is due to a ras-dependent alteration in the expression of ST6Gal I, the enzyme that adds alpha2-6-linked sialic acids. Cells that express differentially sialylated beta1 integrins exhibit altered adhesion to collagen I (a beta1 ligand), but not to vitronectin (a beta3 or beta5 ligand). Similarly, the enzymatic removal of cell surface sialic acids from control cells alters binding to collagen, but not to vitronectin. Finally, using a cell-free receptor/ligand-binding assay, we show that purified, desialylated alpha1beta1 integrins have diminished collagen-binding capability, providing strong evidence that sialic acids play a causal role in regulating beta1 integrin function.

Indexed as

Base SequenceCell AdhesionCell LineChromatography, AffinityColonDNA PrimersEnzyme-Linked Immunosorbent AssayGene Expression RegulationGenes, rasGenetic VectorsHumansIntegrin beta1Intestinal MucosaLectinsNeuraminidasePeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseDNA PrimersIntegrin beta1LectinsNeuraminidasePeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseSialic Acids

Identifiers

PMID14562042
OpenAlexW2055229669

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.