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Related Concept Videos

Overview of Protein Metabolism01:21

Overview of Protein Metabolism

Proteins are broken down into amino acids during digestion. Unlike fats and carbohydrates, which are stored for later use, proteins are not. Instead, amino acids are either used to produce ATP through oxidation or contribute to the creation of new proteins for the growth and repair of the body. Any surplus amino acids from the diet are converted into glucose or triglycerides rather than excreted.
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
Protein Digestion01:02

Protein Digestion

Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Metastasis02:30

Metastasis

Metastasis is the spread of cancer cells from the original site to distant locations in the body. Cancer cells can spread via blood vessels (hematogenous) as well as lymph vessels in the body.
Epithelial-to-Mesenchymal Transition
The epithelial-to-mesenchymal transition or EMT is a developmental process commonly observed in wound healing, embryogenesis, and cancer metastasis. EMT is induced by transforming growth factor-beta (TGF-β) or receptor tyrosine kinase (RTK) ligands, which further...

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Updated: May 28, 2026

Development of a 68Gallium-Labeled D-Peptide PET Tracer for Imaging Programmed Death-Ligand 1 Expression
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Development of a 68Gallium-Labeled D-Peptide PET Tracer for Imaging Programmed Death-Ligand 1 Expression

Published on: February 3, 2023

Circulating Dipeptides in Cancer: Degradation Fragments or Functional Metabolites?

Kyung-Hee Kim1,2, Byong Chul Yoo3

  • 1Department of Applied Chemistry, School of Science and Technology, Kookmin University, Seoul 02707, Republic of Korea.

International Journal of Molecular Sciences
|May 27, 2026
PubMed
Summary

Circulating dipeptides, often overlooked in cancer metabolomics, may have significant biological roles beyond protein breakdown. This review explores their origins, functions, and potential as cancer biomarkers.

Keywords:
bioactive peptidescancer metabolomicscirculating dipeptidesmetabolic communicationpeptide metabolismproteolysistumor metabolism

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Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools
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Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools

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Development of a 68Gallium-Labeled D-Peptide PET Tracer for Imaging Programmed Death-Ligand 1 Expression
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Development of a 68Gallium-Labeled D-Peptide PET Tracer for Imaging Programmed Death-Ligand 1 Expression

Published on: February 3, 2023

Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools
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Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools

Published on: August 19, 2025

Area of Science:

  • Metabolomics
  • Cancer Biology
  • Biochemistry

Background:

  • Mass spectrometry-based metabolomics detects numerous small molecules in cancer, including dipeptides.
  • Circulating dipeptides are often dismissed as byproducts of protein degradation.
  • Emerging evidence suggests endogenous dipeptides possess biological activities.

Purpose of the Study:

  • To review the origins, transport, and biological implications of circulating dipeptides in cancer.
  • To evaluate the potential of dipeptides as bioactive metabolites in cancer.
  • To propose frameworks for interpreting dipeptides in cancer metabolism.

Main Methods:

  • Literature review of metabolomics studies, proteomics, and molecular biology research.
  • Synthesis of current knowledge on dipeptide generation, transport, and metabolism.
  • Analysis of evidence for biological activities of endogenous dipeptides.

Main Results:

  • Dipeptides originate from diverse sources including proteolysis, autophagy, ECM remodeling, cell death, host catabolism, and microbiome metabolism.
  • Mammalian systems possess peptide transport and intracellular metabolism pathways regulating dipeptide fate.
  • Specific endogenous dipeptides exhibit potential biological activities like antioxidant effects and metabolic modulation.

Conclusions:

  • Circulating dipeptides may serve crucial roles in cancer metabolism, not just as degradation byproducts.
  • Dipeptides could function as indicators of protein turnover, amino acid recycling intermediates, or stress-buffering molecules.
  • Further research into dipeptides may uncover novel cancer biomarkers and therapeutic targets.