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It was demonstrated that the process of hemolysis of erythrocytes induced by resorcinolic lipids is inhibited by divalent cations present in the incubation medium. The extent of inhibition is dependent on the nature of both type of the cation and the hemolytic agent. Lysis most susceptible to divalent cations is that induced by short (C15) and medium-chained (C19) 5-n-alkylresorcinols, which also have the highest observed hemolytic potencies. Furthermore, the protection was the stronger the stronger lytic activity was exerted by studied compound. The homologs with the longest side chain studied, although exhibiting the lowest hemolytic activity by themself, were the least susceptible to inhibition of their hemolytic activity by cations. The effect of cobalt cation has been found to be intermediate between the effect of Mn2+ and Zn2+. The most effective in protection of erythrocytes was Zn2+ which almost completely protected the cells against alkylresorcinol-induced lysis at the concentrations of 10-6 M and above.
Cereal grain resorcinolic lipids (S-n-alk(en)ylresorcinols) at micromolar concentrations are able to protect the erythrocyte membrane against hydrogen peroxide-induced lipid oxidation. The antioxidative effect is dependent upon chain length of alkylresorcinol molecules. The C15:0 homolog (IC50 of 10 uM) exhibited strongest activity whereas for long chain homologs (C19: 0 and C23 : 0) IC50 values were higher, 32.5 and 59 uM, respectively. The protective effect of alkylresorcinolic antioxidants was also dependent on their incorporation into the membrane, that is governed by their water-membrane partition coefficient The results obtained show that alkylresorcinols should be recognized as hydrophobic, membrane-localised antioxidants.
It was found that 5-n-alk(en)ylresorcinols isolated from high-fiber diet, wheat or rye bran, effectively inhibit glycerol-3-phosphate dehydrogenase (GPDH, EC 1.1.1.8), the key enzyme of triacylglycerol synthesis in adipocytes. The concentration of alk(en)ylresorcinols necessary for 50 per cent inhibition of GPDH vary from 3.8 µM to 6.4 µM. The effectiveness of the inhibition depends on the length of alk(en)enylresorcinol side chain and hydrophilic ring substitutions. The effectivity of homologs with long side chain (C17 and C19) in apparent inhibition of GPDH is slightly higher than that reported previously for adipostatin A (5-n-pentadecylresorcinol) isolated from Streptomyces (Tsuge, N., Mizokami, M., Imai, S., Shimazu, A., & Seto, H. (1992) J. Antibiot. 45, 886- 891). The fact that the studied resorcinols are natural components of high-fiber human diet, such as porridge and bran products, suggests their possible participation in prevention of the risk of corpulence.
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