Proceedings of the International scientific and practical conference ― Cambridge Science and Education Conference‖ (February 23-25, 2026) / Publisher website: www.naukainfo.com. – Cambridge, United Kingdom, 2026. - 289 p.

74 PGs are a family of 20-carbon lipids derived from polyunsaturated fatty acids, especially arachidonic acid (AA). The carbon atoms C8-C12 form a cyclopentane ring, while the carbons C1-C7 and C12-C20 form two parallel aliphatic chains (R1 and R2, respectively). PGs are not produced by specialized glands, but by various types of cells in the body, acting as autocrine and paracrine messengers. In addition, they have a short half-life. Together with thromboxanes, they are known as prostanoid lipids and share the same carbon skeleton. They, in turn, belong to a larger group called eicosanoids, together with leukotrienes, lipoxins, hydreicosateroids, and epoxyeicosatrienoic acids [8]. Regarding the nomenclature of PG, it is summarized as follows: the accompanying letter to the abbreviation PG indicates the components of the cyclopentane ring and its solubility in various solvents (A: unsaturated ketones, soluble in cold acetone; E: β-hydroxyketones, soluble in ether; F: 1,3-diols, soluble in phosphate buffer); the numerical index indicates the number of double bonds in parallel rows; and the symbolic index indicates other structural details (α: OH group C9, located in the same plane as the R1 ring; β: OH group in a plane different from R1). PGs are formed from the oxidation of AA, a process catalyzed by enzymes called cyclooxygenases (COX) or PGH (prostaglandin H) synthases. In humans, there are two isoforms, COX-1 and COX-2. Both share 60% of their amino acid sequence and have a similar three-dimensional structure, although COX-1 and COX-2 are encoded by different chromosomes (9 and 1, respectively). COX enzymes are membrane proteins with a molecular weight of approximately 70–74 kDa that have four protein domains: (1) an amino-terminal signal peptide domain that directs the protein to its destination in membranes. This domain is longer and more hydrophobic in the COX-1 isoform; (2) a dimerization domain that provides stability to the protein through disulfide bridges connecting it to the catalytic domain and salt bridges; (3) a membrane-binding domain formed by four amphipathic helices that allow it to penetrate the lipid bilayer; (4) a catalytic domain (carboxyl-terminal), which has two separate catalytic sites with different functions (peroxidase and cyclooxygenase