Evidence map›Paper›PMID 33962049›Full record

ReviewMolecular metabolism2021

Insulin-like growth factors: Ligands, binding proteins, and receptors.

Derek LeRoith, Jeff M P Holly, Briony E Forbes

Abstract readReview
In one paragraph

Review in Molecular metabolism, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
175citing papers in PubMed, 3 pooled it
–field-weighted citation impact
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

175 citing papers in PubMed, 3 syntheses or guidelines pooled it.

  1. Pooled it
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  9. Insulin-like growth factor receptor signaling in physiology and disease.Signal transduction and targeted therapy · 2026
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115 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

3 authors.

Derek LeRoithDivision of Endocrinology, Diabetes and Bone Diseases, Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, NY, USA.
Jeff M P HollyTranslational Health Sciences, Bristol Medical School, Learning & Research Building, Southmead Hospital, Bristol, BS10 5NB, UK. Electronic address: jeff.holly@bristol.ac.uk.
Briony E ForbesDiscipline of Medical Biochemistry, Flinders Health and Medical Research Institute, Flinders University, Bedford Park, 5042, Australia.

Funding

Stable Isotope and Metabolomics CoreP60DK020541 · NIDDK · YESHIVA UNIVERSITY · PI PESSIN, JEFFREY E. · 1986 to 2014
$29.8M
Translational Research CoreP30DK020541 · NIDDK · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI JEFFREY E. PESSIN · 2015 to 2026
$27.7M
NIDDK NIH HHS P30 DK020541
6 · The paper itself

Abstract

backgroundThe insulin-like growth factor family of ligands (IGF-I, IGF-II, and insulin), receptors (IGF-IR, M6P/IGF-IIR, and insulin receptor [IR]), and IGF-binding proteins (IGFBP-1-6) play critical roles in normal human physiology and disease states. SCOPE OF REVIEW: Insulin and insulin receptors are the focus of other chapters in this series and will therefore not be discussed further. Here we review the basic components of the IGF system, their role in normal physiology and in critical pathology's. While this review concentrates on the role of IGFs in human physiology, animal models have been essential in providing understanding of the IGF system, and its regulation, and are briefly described. MAJOR

conclusionsIGF-I has effects via the circulation and locally within tissues to regulate cellular growth, differentiation, and survival, thereby controlling overall body growth. IGF-II levels are highest prenatally when it has important effects on growth. In adults, IGF-II plays important tissue-specific roles, including the maintenance of stem cell populations. Although the IGF-IR is closely related to the IR it has distinct physiological roles both on the cell surface and in the nucleus. The M6P/IGF-IIR, in contrast, is distinct and acts as a scavenger by mediating internalization and degradation of IGF-II. The IGFBPs bind IGF-I and IGF-II in the circulation to prolong their half-lives and modulate tissue access, thereby controlling IGF function. IGFBPs also have IGF ligand-independent cell effects.

Indexed as

AnimalsCell CommunicationHumansInsulin-Like Growth Factor Binding ProteinsLigandsReceptor, InsulinSomatomedinsInsulin-Like Growth Factor Binding ProteinsLigandsReceptor, InsulinSomatomedinsCancerGrowthInsulin-like growth factor binding proteinsInsulin-like growth factor receptorsInsulin-like growth factorsMetabolism

Identifiers

PMID33962049
PMCPMC8513159

What OpenQuestion holds

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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.