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The chemical language of protein glycation

Meghan S Martin1, Jeremiah W Jacob-Dolan1, Vo Tri Tin Pham1

  • 1Department of Chemistry, Tufts University, Medford, MA, USA.

Nature Chemical Biology
|June 28, 2024
PubMed

Insights

Glycation, a non-enzymatic modification, is linked to diseases. This review explores its role in cellular signaling and disease, defining it as carbon stress and discussing advanced glycation end-products (AGEs).

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Glycation is a non-enzymatic post-translational modification (PTM) linked to diabetes, cancer, and aging.
  • Its functional role as a PTM and causal involvement in disease and signaling remain under investigation.

Purpose of the Study:

  • To contextualize glycation as a mechanism of carbon stress.
  • To consolidate knowledge on advanced glycation end-product (AGE) structures and mechanisms.
  • To review the current understanding of glycation as a PTM, including AGE formation, removal, and recognition.

Main Methods:

  • Literature review and synthesis of existing research on glycation.
  • Analysis of AGE structures, formation, and biological roles.
  • Discussion of challenges in understanding glycation's biological consequences.

Main Results:

  • Glycation is presented as a form of carbon stress with implications for disease.
  • Current knowledge on AGEs, their formation, and recognition pathways is summarized.
  • Challenges hindering a full understanding of glycation's biological impact are identified.

Conclusions:

  • Understanding glycation requires further insights into its chemistry and the development of new tools.
  • Predicting, modulating, mimicking, or capturing glycation is crucial for deciphering the glycation network.
  • Advancing glycation biology necessitates continued research into its chemical and biological mechanisms.

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