Evidence map›Paper›PMID 23166326›Full record

ArticleThe Journal of biological chemistry2013

Biochemical characterization of individual human glycosylated pro-insulin-like growth factor (IGF)-II and big-IGF-II isoforms associated with cancer.

Sameer A Greenall, John D Bentley, Lesley A Pearce, Judith A Scoble, Lindsay G Sparrow, Nicola A Bartone, Xiaowen Xiao, Robert C Baxter, Leah J Cosgrove, Timothy E Adams

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Functional evolution of IGF2:IGF2R domain 11 binding generates novel structural interactions and a specific IGF2 antagonist.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Role of insulin-like growth factor-binding proteins in the pathophysiology and tumorigenesis of gastroesophageal cancers.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Review
  16. Review
  17. Article
  18. Article
  19. 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

10 authors at 3 institutions in 1 country.

Sameer A GreenallDivision of Materials Science and Engineering, Commonwealth Scientific and Industrial Research Organisation, Parkville, Victoria 3052, Australia.
John D Bentley
Lesley A Pearce
Judith A Scoble
Lindsay G Sparrow
Nicola A Bartone
Xiaowen Xiao
Robert C Baxter
Leah J Cosgrove
Timothy E Adams
Commonwealth Scientific and Industrial Research Organisation · AUHealth Sciences and Nutrition · AURoyal North Shore Hospital · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insulin-like growth factor II (IGF-II) is a major embryonic growth factor belonging to the insulin-like growth factor family, which includes insulin and IGF-I. Its expression in humans is tightly controlled by maternal imprinting, a genetic restraint that is lost in many cancers, resulting in up-regulation of both mature IGF-II mRNA and protein expression. Additionally, increased expression of several longer isoforms of IGF-II, termed "pro" and "big" IGF-II, has been observed. To date, it is ambiguous as to what role these IGF-II isoforms have in initiating and sustaining tumorigenesis and whether they are bioavailable. We have expressed each individual IGF-II isoform in their proper O-glycosylated format and established that all bind to the IGF-I receptor and both insulin receptors A and B, resulting in their activation and subsequent stimulation of fibroblast proliferation. We also confirmed that all isoforms are able to be sequestered into binary complexes with several IGF-binding proteins (IGFBP-2, IGFBP-3, and IGFBP-5). In contrast to this, ternary complex formation with IGFBP-3 or IGFBP-5 and the auxillary protein, acid labile subunit, was severely diminished. Furthermore, big-IGF-II isoforms bound much more weakly to purified ectodomain of the natural IGF-II scavenging receptor, IGF-IIR. IGF-II isoforms thus possess unique biological properties that may enable them to escape normal sequestration avenues and remain bioavailable in vivo to sustain oncogenic signaling.

Indexed as

AnimalsCell ProliferationFibroblastsGene Expression Regulation, NeoplasticGlycosylationHEK293 CellsHumansInsulin-Like Growth Factor Binding ProteinsInsulin-Like Growth Factor IInsulin-Like Growth Factor IIMass SpectrometryMiceNeoplasmsProtein BindingProtein IsoformsProtein Structure, TertiaryInsulin-Like Growth Factor Binding ProteinsInsulin-Like Growth Factor IInsulin-Like Growth Factor IIProtein IsoformsReceptor Protein-Tyrosine Kinases

Identifiers

PMID23166326
PMCPMC3537057
OpenAlexW2026748545

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.