ArticleScientific reports2018
The intrinsically disordered E-domains regulate the IGF-1 prohormones stability, subcellular localisation and secretion.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- Fluorescence-Based Multiplex Western Blot to Simultaneously Detect the Insulin-Like Growth Factor-1 (IGF-1) Isoforms.Electrophoresis · 2025Article
- Identification of functional rare coding variants in IGF-1 gene in humans with exceptional longevity.Scientific reports · 2025Article
- Phosphomannomutase 2-congenital disorder of glycosylation: exploring the role of N-glycosylation on the endocrine axes.Frontiers in endocrinology · 2025Review
- Identification of functional rare coding variants in IGF-1 gene in humans with exceptional longevity.bioRxiv : the preprint server for biology · 2024Article
- A home-based lifestyle intervention program reduces the tumorigenic potential of triple-negative breast cancer cells.Scientific reports · 2024Article
- Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.Current research in structural biology · 2024Review
- Alternative Transcripts Diversify Genome Function for Phenome Relevance to Health and Diseases.Genes · 2023Review
- Association between metabolic syndrome, insulin resistance, and IGF-1 in breast cancer survivors of DIANA-5 study.Journal of cancer research and clinical oncology · 2023Article
- The role of mechano growth factor in chondrocytes and cartilage defects: a concise review.Acta biochimica et biophysica Sinica · 2023Review
- Macrophage-derived IGF-1 protects the neonatal intestine against necrotizing enterocolitis by promoting microvascular development.Communications biology · 2022Article
- Defective IGF-1 prohormone N-glycosylation and reduced IGF-1 receptor signaling activation in congenital disorders of glycosylation.Cellular and molecular life sciences : CMLS · 2022Article
- Bioinformatic Analysis of Lytic Polysaccharide Monooxygenases Reveals the Pan-Families Occurrence of Intrinsically Disordered C-Terminal Extensions.Biomolecules · 2021Article
- Molecular cloning, expression, and functional features of IGF1 splice variants in sheep.Endocrine connections · 2021Article
- Insulin-Like Growth Factor-1 (IGF-1) and Its Monitoring in Medical Diagnostic and in Sports.Biomolecules · 2021Review
- Role of Alternatively Spliced Messenger RNA (mRNA) Isoforms of the Insulin-Like Growth Factor 1 (IGF1) in Selected Human Tumors.International journal of molecular sciences · 2020Review
- Review
- Program and Book of the 15th Interuniversity Institute of Myology Meeting - Assisi (Italy), 2018.European journal of translational myology · 2018Article
- Muscle and Bone Health in Postmenopausal Women: Role of Protein and Vitamin D Supplementation Combined with Exercise Training.Nutrients · 2018Review
- Molecular Signatures of the Insulin-like Growth Factor 1-mediated Epithelial-Mesenchymal Transition in Breast, Lung and Gastric Cancers.International journal of molecular sciences · 2018Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insulin-like growth factor-1 (IGF-1) is synthesised as a prohormone (proIGF-1) requiring enzymatic activity to yield the mature IGF-1. Three proIGF-1s are encoded by alternatively spliced IGF-1 mRNAs: proIGF-1Ea, proIGF-1Eb and proIGF-1Ec. These proIGF-1s have a common IGF-1 mature sequence but different E-domains. The structure of the E-domains has not been resolved, and their molecular functions are still unclear. Here, we show that E-domains are Intrinsically Disordered Regions that have distinct regulatory functions on proIGF-1s production. In particular, we identified a highly conserved N-glycosylation site in the Ea-domain, which regulated intracellular proIGF-1Ea level preventing its proteasome-mediated degradation. The inhibition of N-glycosylation by tunicamycin or glucose starvation markedly reduced proIGF-1Ea and mature IGF-1 production. Interestingly, 2-deoxyglucose, a glucose and mannose analogue, increased proIGF-1Ea and mature IGF-1 levels, probably leading to an accumulation of an under-glycosylated proIGF-1Ea that was still stable and efficiently secreted. The proIGF-1Eb and proIGF-1Ec were devoid of N-glycosylation sites, and hence their production was unaffected by N-glycosylation inhibitors. Moreover, we demonstrated that alternative Eb- and Ec-domains controlled the subcellular localisation of proIGF-1s, leading to the nuclear accumulation of both proIGF-1Eb and proIGF-1Ec. Our results demonstrated that E-domains are regulatory elements that control IGF-1 production and secretion.
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Registered trials
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.