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Updated: Jun 26, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Where does prolidase come from and where is it heading? - A review of recent findings
Aleksandra Jaworowska1, Wojciech Miltyk1
1Department of Pharmaceutical and Biopharmaceutical Analysis, Faculty of Pharmacy with the Division of Laboratory Medicine, Medical University of Białystok, Mickiewicza Street 2D, 15-222 Białystok, Poland.
Abstract:
This study provides new insights into prolidase (PEPD) sources, particularly its presence in exosomes, broadening its recognized role in collagen synthesis and tissue repair. Prolidase, a zinc-dependent metalloproteinase, typically functions intracellularly by hydrolyzing proline-containing dipeptides, critical for collagen biosynthesis and connective tissue integrity. However, the discovery of prolidase within exosomes suggests it may participate in intercellular communication, impacting extracellular matrix remodeling, inflammation, and tissue regeneration. Exosome-derived prolidase potentially influences wound healing and immune responses by facilitating the transfer of proline to damaged tissues, thereby promoting local collagen production and repair processes. Furthermore, the presence of prolidase in exosomes highlights its potential role in cancer, possibly facilitating metastasis by promoting extracellular matrix breakdown. This review enhances prolidase as a therapeutic target in regenerative medicine, inflammatory diseases, and cancer metastasis.
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