DISTRIBUTION OF SERINE PROTEASES IN BLOOD PLASMA AND PANCREAS IN CHRONIC PANCREATITIS AND ONCOPATHOLOGY
T.B. Synelnyk1, O.O. Kravchenko1, O.S. Kostiuk1, O.M. Savchuk1, S.A. Sukhodolia2, L.I. Ostapchenko1
- Taras Shevchenko National University of Kyiv, Educational and Scientific Centre Institute of Biology and Medicine, Ukraine
- National Pirogov Memorial Medical University of Vinnytsya, Ukraine
DOI: https://doi.org/10.15407/fz68.06.031
Abstract
The aim of our study was to evaluate the trypsin-like serine
proteases (TLPs) distribution between systemic circulation
and pancreatic tissue and to investigate the peculiarities of
their involvement in the extracellular matrix components
degradation in patients with pancreatic pathologies with
electrophoretic analysis methods using. Тhe Khmelnitsky
Regional Clinical Hospital patients aged 28-89 were selected
for this study: 20 people with chronic pancreatitis (group
CP); 20 people with pancreatic cancer (group PC); 20
conditionally healthy persons (control). Blood plasma samples
and pancreatic tissue homogenates were obtained from all the
patients, from which the TLPs fractions were subsequently
obtained by the affinity chromatography method. The study
showed that TLPs content in the blood plasma of patients with
pancreatic pathologies is higher, and in tissue homogenates
is lower relative to the values of the corresponding indicators
in the control. Disk-electrophoresis using showed that TLPs
fractions obtained from the blood plasma of patients of all
studied groups contain a lot of high molecular weight (HMW)
proteins, while TLPs from the pancreatic tissue homogenates
of patients with pancreatic pathologies mainly consists of low
molecular weight (LMW) proteins. Enzyme-electrophoresis
results showed that all TLPs fractions include enzymes with
fibrinogenolytic, gelatinolytic and collagenolytic activity.
In plasma, the first were represented by medium molecular
weight (MMW) proteins, and the last two groups included a lot of HMW proteins as well as proteins with very high
molecular weight. In homogenates, fibrinogenolytic activity
was characteristic for LMW proteins only, whereas gelatinases
and collagenases were represented by both MMW and
LMW proteins. Our results indicate the differences in the
TLPs fractions components obtained from blood plasma and
pancreatic tissue of patients with investigated pathologies, as
well as significant distinctions in the processes of extracellular
matrix remodeling under СР and РС.
Keywords:
chronic pancreatitis; pancreatic cancer; trypsin- like serine proteases; electrophoresis.
References
- Kandikattu HK, Venkateshaiah SU, Mishra A. Chronic pancreatitis and the development of pancreatic can- cer. Endocrin Metab Immun Dis Drug Targets. 2020; 20(8):1182-210.
CrossRef
PubMed PubMedCentral
- Spagnolo DM, Greer PJ, Ohlsen CS, Mance S, Ellison M, Breze C, et al. Acute and chronic pancreatitis disease prevalence, classification, and comorbidities: A cohort study of the UK BioBank. Clin Translat Gastroenterol. 2022;13(1):e00455.
CrossRef
PubMed PubMedCentral
Tagirasa R, Yoo E. Role of serine proteases at the tumor- stroma interface. Front Immunol. 2022;13:832418
CrossRef
PubMed PubMedCentral
- Vizovisek M, Ristanovic D, Menghini S, Christiansen MG, Schuerle S. The Tumor proteolytic landscape: A challenging frontier in cancer diagnosis and therapy. Int J Mol Sci. 2021;22(5):2514.
CrossRef
PubMed PubMedCentral
- Rawlings ND, Morton FR, Kok CY, Kong J, Barrett AJ. MEROPS: the peptidase database. Nucleic Acids Res. 2008;36(Database issue):D320-5.
CrossRef
PubMed PubMedCentral
- Patel S. A critical review on serine protease: Key immune manipulator and pathology mediator. Allergol Immunopathol (Madr). 2017;45(6):579-91.
CrossRef
PubMed PubMedCentral
- Magdeldin S, Moser A. Affinity Chromatography. Principles and applications. In: Affinity Chromatography. Magdeldin S (ed.). [Internet]. London: IntechOpen; 2012.
CrossRef
- Ostapchenko L, Savchuk O, Burlova-Vasilieva N. Enzyme electrophoresis method in analysis of active components of haemostasis system. Advan Biosci Biotechnol. 2011;2:20-6.
CrossRef
- Martin CE, List K. Cell surface-anchored serine proteases in cancer progression and metastasis. Cancer Metastas Rev. 2019;38(3):357-87.
CrossRef
PubMed PubMedCentral
- Vitte J. Human mast cell tryptase in biology and medicine. Mol Immunol. 2015;63(1):18-24.
CrossRef
PubMed
- Kumar AA, Buckley BJ, Ranson M. The urokinase plasminogen activation system in pancreatic cancer: prospective diagnostic and therapeutic targets. Biomo- lecules. 2022;12(2):152.
CrossRef
PubMed PubMedCentral
- Baluka D, Urbanek T, Lekstan A, Swietochowska E, Wiaderkiewicz R, Kajor M, et al. The role of the tissue plasminogen activator as a prognostic and differentiation factor in patients with pancreatic cancer and chronic pancreatitis. J Physiol Pharmacol. 2016;67(1): 93-101.
- Candido JB, Maiques O, Boxberg M, Kast V, Peerani E, Tomás-Bort E, et al. Kallikrein-related Peptidase 6 is associated with the tumour microenvironment of pancreatic ductal adenocarcinoma. Cancers (Basel). 2021;13(16):3969.
CrossRef
PubMed PubMedCentral
- Sakugawa C, Haruyama Y, Tanaka H, Fukushima T, Kawaguchi M, Kataoka H. Prognostic significance of hepatocyte growth factor activator inhibitor type 1 (HAI-1) immunoreactivity in pancreatic ductal adenocarcinoma. BMC Res Notes. 2017;10(1):674.
CrossRef
PubMed PubMedCentral
- Fukuoka Y, Schwartz LB. Active monomers of human beta-tryptase have expanded substrate specificities. Int Immunopharmacol. 2007;7(14):1900-8.
CrossRef
PubMed PubMedCentral
- Velasco G, Cal S, Quesada V, Sánchez LM, López-Otín C. Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins. J Biol Chem. 2002;277(40):37637-46.
CrossRef
PubMed
- Yu Y, Prassas I, Diamandis EP. Putative kallikrein substrates and their (patho) biological functions. Biol Chem. 2014; 395(9): 931-43.
CrossRef
PubMed
|