Activatable Peptides for Rapid and Simple Visualization of Protease Activity Secreted in Living Cells

Activity-based monitoring of cell-secreted proteases has gained significant interest due to the implication of these substances in diverse cellular functions. Here, we demonstrated a cell-based method of monitoring protease activity using fluorescent cell-permeable peptides. The activatable peptide...

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Bibliographic Details
Published in:International journal of molecular sciences 2022-01, Vol.23 (3), p.1605
Main Authors: Kim, Gae-Baik, Lee, Jeong Min, Nguyen, Duc Long, Lee, Joonseok, Kim, Young-Pil
Format: Article
Language:English
Subjects:
Amino acids
Cancer
Cell activation
Cell growth
Cell Line, Tumor
Enzymes
Fluorescence
Gelatinase A
Gene expression
HT29 Cells
Humans
Matrix metalloproteinase
Matrix Metalloproteinase 2 - analysis
Matrix metalloproteinases
Metalloproteinase
Monitoring
Neoplasms - enzymology
Optical Imaging
Peptides
Peptides - chemistry
Peptides - metabolism
Protease
Proteinase
Proteolysis
Visualization
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Summary:Activity-based monitoring of cell-secreted proteases has gained significant interest due to the implication of these substances in diverse cellular functions. Here, we demonstrated a cell-based method of monitoring protease activity using fluorescent cell-permeable peptides. The activatable peptide consists of anionic (EEEE), cleavable, and cationic sequences (RRRR) that enable intracellular delivery by matrix metalloproteinase-2 (MMP2), which is secreted by living cancer cells. Compared to HT-29 cells (MMP2-negative), HT-1080 cells (MMP2-positive) showed a strong fluorescence response to the short fluorescent peptide via cell-secreted protease activation. Our approach is expected to find applications for the rapid visualization of protease activity in living cells.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms23031605