Cited by 82Advanced Glycation End Products researchSkin Diseases and DiabetesGlycosylation and Glycoproteins Research

Extracellular matrix glycation and receptor for advanced glycation end-products activation: a missing piece in the puzzle of the association between diabetes and cancer

Rojas, Armando, Añazco, Carolina, González, Ileana, Araya, Paulina·2018·Carcinogenesis

Abstract

A growing body of epidemiologic evidence suggests that people with diabetes are at a significantly higher risk of many forms of cancer. However, the molecular mechanisms underlying this association are not fully understood. Cancer cells are surrounded by a complex milieu, also known as tumor microenvironment, which contributes to the development and metastasis of tumors. Of note, one of the major components of this niche is the extracellular matrix (ECM), which becomes highly disorganized during neoplastic progression, thereby stimulating cancer cell transformation, growth and spread. One of the consequences of chronic hyperglycemia, the most frequently observed sign of diabetes and the etiological source of diabetes complications, is the irreversible glycation and oxidation of proteins and lipids leading to the formation of the advanced glycation end-products (AGEs). These compounds may covalently crosslink and biochemically modify structure and functions of many proteins, and AGEs accumulation is particularly high in long-living proteins with low biological turnover, features that are shared by most, if not all, ECM proteins. AGEs-modified proteins are recognized by AGE-binding proteins, and thus glycated ECM components have the potential to trigger Receptor for advanced glycation end-products-dependent mechanisms. The biological consequence of receptor for advanced glycation end-products activation mechanisms seems to be connected, in different ways, to drive some hallmarks of cancer onset and tumor growth. The present review intends to highlight the potential impact of ECM glycation on tumor progression by triggering receptor for advanced glycation end-products-mediated mechanisms.

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Crossref · 10.1093/carcin/bgy012

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Authors
Rojas, A., Añazco, C., González, I., & Araya, P.
Affiliations
  • Biomedical Research Laboratories, Preclinical Sciences Department, Medicine Faculty, Catholic University of Maule, Talca, Chile
  • Catholic University of the Maule (CL)
Venue
Carcinogenesis
Published
2018-01-24
Volume
39
Issue
4
Pages
515-521
ISSN
  • 0143-3334 (ISSN-L)
  • 1460-2180
OpenAlex
W2790744076
Cited by
82
References
92
Citations by year
2026: 7 · 2025: 7 · 2024: 11 · 2023: 12 · 2022: 12 · 2021: 15 · 2020: 5 · 2019: 11 · 2018: 2
FWCI
1.07
Type
journal article
Language
en
Open access
closed
Locations
  • Carcinogenesis (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
  • Health Sciences › Medicine › Dermatology › Skin Diseases and Diabetes
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Keywords
advanced glycation end products, receptor for advanced glycation end products, diabetes and cancer, tumor microenvironment, chronic hyperglycemia, tumor progression, cancer hallmarks
MeSH terms
Receptor for Advanced Glycation End Products, Animals, Diabetes Mellitus, Extracellular Matrix, Glycosylation, Humans, Neoplasms, Glycation End Products, Advanced, Diabetes Complications

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