Tag Archives: proteolysis
Proteins of plasminogen/plasmin system: multifaceted roles in health and disease
A. O. Tykhomyrov*, O. I. Yusova, L. G. Kapustianenko, I. I. Patalakh,
T. A. Yatsenko, V. L. Bilous, T. V. Grynenko
Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine,
Department of Enzyme Chemistry and Biochemistry, Kyiv;
*e-mail: artem_tykhomyrov@ukr.net
Received: 20 April 2025; Revised: 02 June 2025;
Accepted: 30 October 2025; Available on-line: 2025
The plasminogen/plasmin (Pg/Pm) system is a cornerstone of various biological processes, encompassing roles in fibrinolysis, angiogenesis, inflammation, wound healing, and tumor biology. This review consolidates knowledge on the multifaceted functions of the Pg/Pm system proteins in health and disease, highlighting historical developments, recent advancements, and the contributions of the Department of Enzyme Chemistry and Biochemistry to the understanding of their molecular mechanisms of function. We have explored the regulation of fibrinolysis and its intricate interplay with proteins of the Pg/Pm system, delving into their pivotal role in hemostatic balance. Reciprocal interactions between Pg/Pm system proteins and platelets underscore their contribution to thrombosis, fibrinolysis, inflammation, and vascular remodeling. In oncology, Pg/Pm system proteins orchestrate tumor growth and metastasis through their involvement in extracellular matrix remodeling, angiogenesis, and cancer cell survival. However, angiostatins – proteolytically-derived fragments of Pg/Pm – emerge as multifunctional polypeptides, which are known to affect cell migration, angiogenesis, and inflammation, suppress tumor growth and metastasis. Contribution of Pg/Pm to reparative processes, including wound healing, further emphasizes their therapeutic potential in regenerative medicine. Moreover, these proteins play crucial roles in ocular health, where their dysregulation may lead to the pathogenesis of ophthalmic diseases. In conclusion, advancement of our understanding of this versatile system functions through continued research is pivotal for applications of these proteins as diagnostic and prognostic biomarkers for cardiovascular disorders, inflammatory pathologies, cancer, autoimmune conditions, and various diabetic complications, offering insights into early detection of disease and development of innovative therapeutic strategies, ultimately driving progress in personalized medicine.
Activity of trypsin-like enzymes and gelatinases in rats with doxorubicin cardiomyopathy
Iu. А. Gordiienko1, Ya. V. Babets2, А. О. Kulinich1,
А. І. Shevtsova1, G. О. Ushakova2
1SE Dnipropetrovsk Medical Academy of Health Ministry of Ukraine;
2Oles’ Honchar Dnipropetrovs’k National University, Ukraine;
e-mail: gordienko.ju@gmail.com
Activity of trypsin-like enzymes (ATLE) and gelatinases A and B were studied in the blood plasma and extracts from cardiac muscle, cerebral cortex and cerebellum of rats with cardiomyopathy caused by anthracycline antibiotic doxorubicin against the background of preventive application of corvitin and α-ketoglutarate. ATLE significantly increased in blood plasma and extracts from cerebral cortex but decreased in extracts from cardiac muscle and cerebellum in doxorubicin cardiomyopathy (DCMP). In addition, a significant increase of activity of both gelatinases in plasma and tissue extracts was observed. Preventive administration of corvitin and α-ketoglutarate resulted in differently directed changes of activity of the above mentioned enzymes in heart and brain tissues. Obtained data confirm the hypothesis about activation of proteolysis under the influence of anthracycline antibiotics and testify to selective effect of corvitin and α-ketoglutarate on ATLE and gelatinases.