In the pathogeneses of recurrent tonsillitis (RT) and tonsillar hypertrophy (TH), different immunological mechanisms are involved. Dipeptidyl peptidase IV (DPP IV) and aminopeptidase N (APN) participate in the regulation of the immune response during inflammation. In this study, the localization of DPP IV and the enzymatic activities of DPP IV and APN in 32 patients, 13 with RT and 19 with TH, who underwent tonsillectomy were investigated. The localization of DPP IV in tonsils was studied using histochemical and immunohistochemical methods. The enzymatic activities of DPP IV and APN in tonsillar lymphocytes and the patients' sera were determined kinetically at 37 degrees C using Gly-Pro-p-nitroanilide (for DPP IV) and Ala-p-nitroanilide (for APN) as chromogenic substrates. In samples from both RT and TH patients, DPP IV was found to localize mainly in extrafollicular areas of tonsillar tissue in a pattern corresponding to the T-cell distribution. Significantly higher (P < 0.001) levels of DPP IV and APN activities in sera from patients with TH than in sera from patients with RT were found. A correlation of DPP IV activities in sera and tonsillar lymphocytes from patients with TH was also found (r = 0.518; P < 0.05). Moreover, the results show that DPP IV and APN activities in sera decreased significantly with age. Tonsillar lymphocytes demonstrated a wide range of DPP IV and APN activities, without significant differences between the investigated groups. The results of this study show that the localization of DPP IV does not depend on the type of tonsillitis, whereas the variety in levels of DPP IV and APN activities in sera of patients with TH and RT suggests different patterns of participation of antigen-stimulated tonsils in the immune system.
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http://dx.doi.org/10.1128/CVI.00054-07 | DOI Listing |
Front Mol Biosci
February 2024
Faculty of Pharmaceutical Sciences, Teikyo Heisei University, Tokyo, Japan.
Extracellular vesicles (EVs), which are found in almost all cells and human body fluids, are currently being studied as a source of pathophysiological information. Previously, we demonstrated that at least two types of EVs can be isolated from human whole saliva (WS) using enzymatic activity of dipeptidyl peptidase IV (DPP IV) as a marker for differentiating the EV subsets. In the present study, EV fractions, termed EV-I 20 k-ppt and EV-II 100 k-ppt, were prepared by a combination of size-exclusion chromatography of improved condition and sequential centrifugation.
View Article and Find Full Text PDFInt J Biol Macromol
January 2022
Instituto de Biotecnología, Universidad Nacional Autónoma de México (UNAM), Cuernavaca, Mexico.
Dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.
View Article and Find Full Text PDFInt J Biol Macromol
December 2020
Center for Protein Studies, Faculty of Biology, University of Havana, Havana, Cuba. Electronic address:
Bestatin and bacitracin are inhibitors of metallo aminopeptidases and bacterial proteases. However, their effects on other human peptidases, like dipeptidyl peptidase IV (DPP-IV, EC 3.4.
View Article and Find Full Text PDFIran J Immunol
March 2020
Department of Immunology, School of Medicine, Shahid Behesti University of Medical Sciences, Tehran, Iran.
Background: Emerging evidence suggests that secretome of mesenchymal stem cells has many anti-inflammatory and regenerative properties, which makes it a suitable candidate for the treatment of autoimmune and degenerative diseases. Dipeptidyl Peptidase-IV (DPP-IV)/CD26 and Aminopeptidase N (APN)/CD13 are ubiquitous ecto-enzymes which can digest various substrates including some chemokines and neuropeptides that are involved in inflammatory conditions.
Objective: To evaluate the enzymatic activity of DPP-IV/CD26 and APN/CD13 in MSC conditioned media (MSC-CM).
Am J Physiol Renal Physiol
December 2012
Dept. of Pathology, Hospital Universitario Cruces, Plaza de Cruces s/n, Bizkaia, Spain.
Several studies have proposed that protease expression and activity may have a predictive value in the survival of clear cell renal cell carcinoma (CCRCC). Most efforts on this issue have been focused on the analysis of matrix metalloproteinases (MMP) and very little on the role of other proteases, such as peptidases. The catalytic activity of 9 peptidases (APN, APB, ASP, CAP, DPP-IV, NEP/CD10, PEP, PGI, and PSA) was quantified by fluorometric methods in a series of 79 CCRCC patients, and the results obtained were analyzed for survival (Kaplan-Meier curves, log-rank test, and Cox multivariate analysis).
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