Evidence map›Paper›PMID 22745191›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2012

The HMGA1-IGF-I/IGFBP system: a novel pathway for modulating glucose uptake.

Stefania Iiritano, Eusebio Chiefari, Valeria Ventura, Biagio Arcidiacono, Katiuscia Possidente, Aurora Nocera, Maria T Nevolo, Monica Fedele, Adelaide Greco, Manfredi Greco and 4 more

Abstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
1.1field-weighted citation impact, top 25% 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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 64 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Insulin Resistance and Cancer: In Search for a Causal Link.International journal of molecular sciences · 2021
    Review
  10. Review
  11. Review
  12. HMGA Genes and Proteins in Development and Evolution.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Vitamin DJournal of diabetes research · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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

14 authors at 4 institutions in 1 country.

Stefania IiritanoDipartimento di Scienze della Salute, Università di Catanzaro Magna Græcia, 88100 Catanzaro, Italy.
Eusebio Chiefari
Valeria Ventura
Biagio Arcidiacono
Katiuscia Possidente
Aurora Nocera
Maria T Nevolo
Monica Fedele
Adelaide Greco
Manfredi Greco
Giuseppe Brunetti
Alfredo Fusco
Daniela Foti
Antonio Brunetti
Magna Graecia University · ITInstitute for Experimental Endocrinology and Oncology · ITUniversity of Milan · ITUniversity of Naples Federico II · IT

Funding

Telethon GGP04245
6 · The paper itself

Abstract

We previously showed that loss of the high mobility group A1 (HMGA1) protein expression, induced in mice by disrupting the Hmga1 gene, considerably decreased insulin receptor expression in the major target tissues of insulin action, causing a type 2-like diabetic phenotype, in which, however, glucose intolerance was paradoxically associated with increased peripheral insulin sensitivity. Insulin hypersensitivity despite impairment of insulin action supports the existence of molecular adaptation mechanisms promoting glucose disposal via insulin-independent processes. Herein, we provide support for these compensatory pathways/circuits of glucose uptake in vivo, the activation of which under certain adverse metabolic conditions may protect against hyperglycemia. Using chromatin immunoprecipitation combined with protein-protein interaction studies of nuclear proteins in vivo, and transient transcription assays in living cells, we show that HMGA1 is required for gene activation of the IGF-binding proteins 1 (IGFBP1) and 3 (IGFBP3), two major members of the IGF-binding protein superfamily. Furthermore, by using positron emission tomography with (18)F-labeled 2-fluoro-2-deoxy-d-glucose, in combination with the euglycemic clamp with IGF-I, we demonstrated that IGF-I's bioactivity was increased in Hmga1-knockout mice, in which both skeletal muscle Glut4 protein expression and glucose uptake were enhanced compared with wild-type littermates. We propose that, by affecting the expression of both IGFBP protein species, HMGA1 can serve as a modulator of IGF-I activity, thus representing an important novel mediator of glucose disposal.

Indexed as

AnimalsBlotting, WesternCell Line, TumorChromatin ImmunoprecipitationGlucoseHep G2 CellsHMGA ProteinsHumansImmunoprecipitationInsulin-Like Growth Factor Binding Protein 1Insulin-Like Growth Factor Binding Protein 3Insulin-Like Growth Factor Binding ProteinsInsulin-Like Growth Factor IMiceMice, KnockoutNIH 3T3 CellsGlucoseHMGA ProteinsIGFBP1 protein, humanIGFBP3 protein, humanInsulin-Like Growth Factor Binding Protein 1Insulin-Like Growth Factor Binding Protein 3Insulin-Like Growth Factor Binding ProteinsInsulin-Like Growth Factor I

Identifiers

PMID22745191
PMCPMC5416968
OpenAlexW1963854785

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.