Intracellular Hydrolysis of Peptides

Josefsson, Lars; Sjöström, Hans; Norén, Ove

doi:10.1002/9780470720318.ch11

Cited by 3 publications

(1 citation statement)

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“…However, it is not known why prolidase occurs in that subcellular location. PEPD is abundantly expressed in enterocytes, where it is probably involved in the hydrolysis of dietary proline-containing dipeptides [ 59 ]. Regarding the tissue specificity of prolidase, the highest level of prolidase mRNA expression is observed in the kidneys, small intestine, and duodenum [ 60 ], while high prolidase activity has been reported in erythrocytes and human skin fibroblasts [ 50 ].…”

Section: Enzyme-dependent Activity Of Prolidasementioning

confidence: 99%

Current Understanding of the Emerging Role of Prolidase in Cellular Metabolism

Misiura

Miltyk

2020

IJMS

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Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline. For decades, prolidase has been thoroughly investigated, and several mechanisms regulating its activity are known, including the activation of the β1-integrin receptor, insulin-like growth factor 1 receptor (IGF-1) receptor, and transforming growth factor (TGF)-β1 receptor. This process may result in increased availability of proline in the mitochondrial proline cycle, thus making proline serve as a substrate for the resynthesis of collagen, an intracellular signaling molecule. However, as a ligand, PEPD can bind directly to the epidermal growth factor receptor (EGFR, epidermal growth factor receptor 2 (HER2)) and regulate cellular metabolism. Recent reports have indicated that PEPD protects p53 from uncontrolled p53 subcellular activation and its translocation between cellular compartments. PEPD also participates in the maturation of the interferon α/β receptor by regulating its expression. In addition to the biological effects, prolidase demonstrates clinical significance reflected in the disease known as prolidase deficiency. It is also known that prolidase activity is affected in collagen metabolism disorders, metabolic, and oncological conditions. In this article, we review the latest knowledge about prolidase and highlight its biological function, and thus provide an in-depth understanding of prolidase as a dipeptidase and protein regulating the function of key biomolecules in cellular metabolism.

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Section: Enzyme-dependent Activity Of Prolidasementioning

confidence: 99%