Increased prolyl endopeptidase activity in human neoplasia

Prolyl endopeptidase (EC 3.4.21.26) (PEP) is a serine peptidase that converts several biologically active peptides. This enzyme has been linked to several neurological, digestive, cardiovascular and infectous disorders. However, little is known about its involvement in neoplastic processes. This stu...

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Published inRegulatory peptides Vol. 163; no. 1; pp. 102 - 106
Main Authors Larrinaga, Gorka, Perez, Itxaro, Blanco, Lorena, López, José I., Andrés, Leire, Etxezarraga, Carmen, Santaolalla, Francisco, Zabala, Aitor, Varona, Adolfo, Irazusta, Jon
Format Journal Article
LanguageEnglish
Published Kidlington Elsevier B.V 09.08.2010
Elsevier
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Summary:Prolyl endopeptidase (EC 3.4.21.26) (PEP) is a serine peptidase that converts several biologically active peptides. This enzyme has been linked to several neurological, digestive, cardiovascular and infectous disorders. However, little is known about its involvement in neoplastic processes. This study analyzes fluorimetrically cytosolic and membrane-bound PEP activity in a large series ( n = 122) of normal and neoplastic tissues from the kidney, colon, oral cavity, larynx, thyroid gland and testis. Cytosolic PEP activity significantly increased in clear cell renal cell carcinoma, urothelial carcinoma of the renal pelvis and head and neck squamous cell carcinoma. Both cytosolic and membrane-bound PEP activity were also increased in colorectal adenomatous polyps. These data suggest the involvement of PEP in some mechanisms that underlie neoplastic processes.
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ISSN:0167-0115
1873-1686
DOI:10.1016/j.regpep.2010.03.012