https://doi.org/10.4081/jbr.2024.12567
Abnormal proteolytic activity profile in plasma of blood donors according to anti-SARS-CoV-2 IgG titer
Submitted: April 13, 2024
Accepted: October 22, 2024
Published: November 6, 2024
Accepted: October 22, 2024
Abstract Views: 49
PDF: 28
Publisher's note
All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.
All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.
Authors
This work aims to study whether there is a relationship between titer values of anti-SARS-CoV-2 IgG and changes in proteolytic processes. To confirm this hypothesis, we analyzed the content and activity of Matrix Metalloproteinases (MMPs) as well as the concentration and composition of circulating peptide pools in the plasma of blood donors divided into groups on the basis of anti-SARS-CoV-2 IgG titers. The results of gelatin zymography showed the presence of active MMP-2 in donors’ plasma who recovered from COVID-19. In contrast, collagenases and their complexes were detected in the plasma of donors with no anti-SARS-CoV-2 IgG, while their activity was undetectable in some groups of COVID-19 convalescent individuals. The content of MMPs also differed among the donors with different titers of anti-SARS-CoV-2 IgG. Plasma peptide content was identical among the donors' groups, but there were more peptide fractions in plasma peptide pools of COVID-19 convalescent individuals; furthermore, they all were characterized by the presence of peptides with molecular weights less than 920 Da and greater than 1530 Da. We hypothesized a link between proteolytic alterations and peptide fraction composition. Our data need further validation to confirm the relationship between the titer values of anti-SARS-CoV-2 IgG and the severity of the proteolytic imbalance.
Löffek S, Schilling O, Franzke CW. Series "matrix metalloproteinases in lung health and disease": Biological role of matrix metalloproteinases: a critical balance. Eur Respir J 2011;38:191-208.
DOI: https://doi.org/10.1183/09031936.00146510
Malemud CJ. Matrix metalloproteinases (MMPs) in health and disease: an overview. Front Biosci 2006;11:1696-701.
DOI: https://doi.org/10.2741/1915
Cabral-Pacheco GA, Garza-Veloz I, Castruita-De la Rosa C, et al. The Roles of matrix metalloproteinases and their inhibitors in human diseases. Int J Mol Sci 2020;21:9739.
DOI: https://doi.org/10.3390/ijms21249739
De Galiza YS, Eloy AMX, Pinheiro RR, et al. Study of metalloproteinases in the blood of goats experimentally infected with caprine encephalitis arthritis virus. Semina: Ciencias Agrarias 2020;41:3165-76.
DOI: https://doi.org/10.5433/1679-0359.2020v41n6Supl2p3165
Isaacson KJ, Martin Jensen M, Subrahmanyam NB, Ghandehari H. Matrix-metalloproteinases as targets for controlled delivery in cancer: An analysis of upregulation and expression. J Control Release 2017;259:62-75.
DOI: https://doi.org/10.1016/j.jconrel.2017.01.034
Lee HS, Kim WJ. The role of matrix metalloproteinase in inflammation with a focus on infectious diseases. Int J Mol Sci 2022;23:10546.
DOI: https://doi.org/10.3390/ijms231810546
Bassiouni W, Ali MAM, Schulz R. Multifunctional intracellular matrix metalloproteinases: implications in disease. FEBS J 2021;288:7162-82.
DOI: https://doi.org/10.1111/febs.15701
Salomão R, Assis V, de Sousa Neto IV, et al. Involvement of matrix metalloproteinases in COVID-19: molecular targets, mechanisms, and insights for therapeutic interventions. Biology (Basel) 2023;12:843.
DOI: https://doi.org/10.3390/biology12060843
Gelzo M, Cacciapuoti S, Pinchera B, et al. Matrix metalloproteinases (MMP) 3 and 9 as biomarkers of severity in COVID-19 patients. Sci Rep 2022;12:1212.
DOI: https://doi.org/10.1038/s41598-021-04677-8
Baldanzi G, Purghè B, Ragnoli B, et al. Circulating peptidome is strongly altered in COVID-19 patients. Int J Environ Res Public Health 2023;20:1564.
DOI: https://doi.org/10.3390/ijerph20021564
Ragnoli B, Purghè B, Manfredi M, et al. New insights in circulating peptidome to differentiate mild to severe COVID-19 patients: Preliminary report. Pulmonology 2024;30:82-4.
DOI: https://doi.org/10.1016/j.pulmoe.2023.04.006
Mohammadhosayni M, Sadat Mohammadi F, Ezzatifar F, et al. Matrix metalloproteinases are involved in the development of neurological complications in patients with Coronavirus disease 2019. Int Immunopharmacol 2021;100:108076.
DOI: https://doi.org/10.1016/j.intimp.2021.108076
Ostapchenko L, Savchuk O, Burlova-Vasilieva N. Enzyme electrophoresis method in analysis of active components of haemostasis system. ABB 2011;2:20-6.
DOI: https://doi.org/10.4236/abb.2011.21004
Tuharov Y, Krenytska D, Halenova T, et al. Plasma levels of MMPs and TIMP-1 in patients with osteoarthritis after recovery from COVID-19. Rev Recent Clin Trials 2023;18:123-8.
DOI: https://doi.org/10.2174/1574887118666230131141608
Kozyk M, Strubchevska K, Marynenko T, et al. Effect of peptides from plasma of patients with coronary artery disease on the vascular endothelial cells. Medicina (Kaunas) 2023;59:238.
DOI: https://doi.org/10.3390/medicina59020238
Kudelski J, Tokarzewicz A, Gudowska-Sawczuk M, et al. The significance of matrix metalloproteinase 9 (MMP-9) and metalloproteinase 2 (MMP-2) in urinary bladder cancer. Biomedicines 2023;11:956.
DOI: https://doi.org/10.3390/biomedicines11030956
Inanc S, Keles D, Oktay G. An improved collagen zymography approach for evaluating the collagenases MMP-1, MMP-8, and MMP-13. BioTechniques 2017;63:174-80.
DOI: https://doi.org/10.2144/000114597
Nakamura H, Fujii Y, Ohuchi E, et al. Activation of the precursor of human stromelysin 2 and its interactions with other matrix metalloproteinases. Eur J Biochem 1998;253:67-75.
DOI: https://doi.org/10.1046/j.1432-1327.1998.2530067.x
Gomez DE, Alonso DF, Yoshiji H, Thorgeirsson UP. Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol 1997;74:111-22.
Bond JS. Proteases: History, discovery, and roles in health and disease. J Biol Chem 2019;294:1643-51.
DOI: https://doi.org/10.1074/jbc.TM118.004156
Fernandez-Patron C, Hard E. Matrix metalloproteinases in health and disease in the times of COVID-19. Biomolecules 2022;12:692.
DOI: https://doi.org/10.3390/biom12050692
Zoodsma M, de Nooijer AH, Grondman I, et al. Targeted proteomics identifies circulating biomarkers associated with active COVID-19 and post-COVID-19. Front Immunol 2022;13:1027122.
DOI: https://doi.org/10.3389/fimmu.2022.1027122
Snoek-van Beurden PA, Von den Hoff JW. Zymographic techniques for the analysis of matrix metalloproteinases and their inhibitors. BioTechniques 2005;38:73-83.
DOI: https://doi.org/10.2144/05381RV01
Quesada AR, Mar Barbacid M, Mira E. Evaluation of fluorometric and zymographic methods as activity assays for stromelysins and gelatinases. Clin Exp Metastasis 1997;15:26-32.
DOI: https://doi.org/10.1023/A:1018480222301
Brew K, Nagase H. The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity. Biochim Biophys Acta 2010;1803: 55-71.
DOI: https://doi.org/10.1016/j.bbamcr.2010.01.003
Ismael MK, Rasuol LM, Qaddoori YB. Investigation of the relationship between matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase with SARS CoV-2 infections. J Adv Biotechnol Exp Ther 2023;6:35-43.
DOI: https://doi.org/10.5455/jabet.2023.d104
Katrii T, Raksha N, Halenova T, et al. Influence of peptide pools from the plasma of ischemic stroke patients on hemostasis. Curr Top Pept Protein Res 2020;21:21-9.
Raksha N, Halenova T, Vovk T, et al. Protein-peptide composition in the lungs of rats with hyperhomocysteinemia. Boll Soc Ital Biol Sper 2021;94:67-71.
DOI: https://doi.org/10.4081/jbr.2021.9858
de Araujo CB, Heimann AS, Remer RA, et al. Intracellular peptides in cell biology and pharmacology. Biomolecules 2019;9:150.
DOI: https://doi.org/10.3390/biom9040150
Shiryaev SA, Cieplak P, Aleshin AE, et al. Matrix metalloproteinase proteolysis of the mycobacterial HSP65 protein as a potential source of immunogenic peptides in human tuberculosis. FEBS J 2011;278:3277-86.
DOI: https://doi.org/10.1111/j.1742-4658.2011.08244.x
Apcher S, Millot G, Daskalogianni C, et al. Translation of pre-spliced RNAs in the nuclear compartment generates peptides for the MHC class I pathway. Proc Natl Acad Sci USA 2013;110:17951-6.
DOI: https://doi.org/10.1073/pnas.1309956110
Rojas M, Rodríguez Y, Acosta-Ampudia Y, et al. Autoimmunity is a hallmark of post-COVID syndrome. J Transl Med 2022;20:129.
DOI: https://doi.org/10.1186/s12967-022-03328-4
Piccin A, Mullin B, Brown A, Benson G. The lack of anti-PF4 antibodies in convalescent plasma from COVID-19 infected blood donor. Transfus Med 2023;33:272-3.
DOI: https://doi.org/10.1111/tme.12965
Tomimura S, Ogawa F, Iwata Y et al. Autoantibodies against matrix metalloproteinase-1 in patients with localized scleroderma. J Dermatol Sci 2008;52:47-54.
DOI: https://doi.org/10.1016/j.jdermsci.2008.04.013
Zhou JH, Zhang B, Kernstine KH, Zhong L. Autoantibodies against MMP-7 as a novel diagnostic biomarker in esophageal squamous cell carcinoma. World J Gastroenterol 2011;17:1373-8.
DOI: https://doi.org/10.3748/wjg.v17.i10.1373
Nishijima C, Hayakawa I, Matsushita T, et al. Autoantibody against matrix metalloproteinase-3 in patients with systemic sclerosis. Clin Exp Immunol 2004;138:357-63.
DOI: https://doi.org/10.1111/j.1365-2249.2004.02615.x
Iwaki-Egawa S, Matsuno H, Ogawa Y, Watanabe Y. Production of anti-CCP antibodies and matrix metalloproteinase-3 by human rheumatoid arthritis synovial tissues using SCID mice. Ann Rheum Dis 2005;64:1094-5.
DOI: https://doi.org/10.1136/ard.2004.032847
How to Cite
Halenova, T., Rachkovska , A., Krenytska , D., Kostiuk, O., Karbovskyy, V., Vovk, T., Raksha, N., Savchuk, O., & Ostapchenko, L. (2024). Abnormal proteolytic activity profile in plasma of blood donors according to anti-SARS-CoV-2 IgG titer. Journal of Biological Research - Bollettino Della Società Italiana Di Biologia Sperimentale. https://doi.org/10.4081/jbr.2024.12567
Copyright (c) 2024 the Author(s)
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
PAGEPress has chosen to apply the Creative Commons Attribution NonCommercial 4.0 International License (CC BY-NC 4.0) to all manuscripts to be published.