POSITIVE FEEDBACK LOOP OF ADHESION DISEASE: FIBRIN AND OTHERS

Author:

Dieiev ValeriiORCID,Bulyk IvanORCID,Dovbeshko GalynaORCID,Gnatyuk OlenaORCID,Timchenko MarinaORCID,Verevka SerhijORCID

Abstract

Adhesion disease is a common complication of abdominal operations, which is often manifested by acute adhesion obstruction of the intestine with a high rate of recurrence on surgical treatment. Mechanical damage to the peritoneum, which leads to uncontrolled leakage of blood from the damaged vessels and the formation of blood clots with the loss of fibrin at the site of damage, is recognized as the leading trigger of adhesion disease.The stability of the formed adhesions, their ability to grow and regenerate are in conflict with the known data on the mechanisms of the hemostasis system. The latter, as is known, consists of two divergent activation cascades, which ensure the blocking of hemorrhage in case of damage to vessels due to the formation of a fibrin clot with its subsequent splitting into large soluble blocks.An imbalance between the coagulation and fibrinolytic links of the hemostasis system causes various functional complications. The formation of adhesions can be considered as an extreme example of such an imbalance. This leads to the search for the reasons for the inefficiency of the fibrinolytic system in relation to fibrin deposits in adhesions. The aim of the work: study of the structure of fibrin deposits in adhesions using histological methods and infrared spectroscopy. Results and discussion. It is shown that adhesions of the peritoneum are a complex structure formed by protein and cellular components. The protein component is formed by fibrin and collagen, and the difference in the structure of these proteins from the native one with a pronounced content of β-structured aggregates is noted. The cellular component is mainly represented by fibroblasts - the main cells of connective tissue that synthesize collagen, elastin, proteoglycans and glycoproteins. Such composition ensures resistance of adhesions to fibrinolysis and their ability to regenerate.

Publisher

European Scientific Platform (Publications)

Subject

General Agricultural and Biological Sciences

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