Assessment of the effect of monohydroxy alcohols, unsaturated fatty acids, organophosphate compounds on the enzymatic ATP-hydrolysis in the cell membranes of the smooth muscle of rat colon
The differences of the structural-functional stability of ATP-hydrolases to the action of the short-chain aliphatic monohydroxy alcohols and long-chain unsaturated fatty acids (UFAs) with wide range of the membrane-acting effectiveness were evaluated in the colonic smooth muscle (CSM) cellular membr...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry
2018-07-01
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| Series: | The Ukrainian Biochemical Journal |
| Subjects: | |
| Online Access: | http://ukrbiochemjournal.org/wp-content/uploads/2018/06/Kaplia_4_18.pdf |
| Summary: | The differences of the structural-functional stability of ATP-hydrolases to the action of the short-chain aliphatic monohydroxy alcohols and long-chain unsaturated fatty acids (UFAs) with wide range of the membrane-acting effectiveness were evaluated in the colonic smooth muscle (CSM) cellular membranes. It was shown that Mg2+,ATP-hydrolase was more resistant to all tested aliphatic compounds than Na+,K+-ATPase. There was a clear relationship between inhibitory efficiency, chain length (number of carbons) increase and relative polarity decrease in the series of straight-chain alcohols. Secondary alcohol 2-propanol turned out to be the weaker inhibitor than primary alcohol 1-propanol. The I50 value (мМ) for ATРases decreased in the following succession: ethanol > 2-propanol > 1-propanol > 1-butanol. UFAs were the stronger inhibitors (I50 of μM range) than alcohols (mM range). Oleic acid inhibited Na+,K+-ATPase with lower efficiency than was detected for arachidonic acid according to the differences in double bonds number; I50 for Mg2+,ATP-hydrolase activity was the same for studied UFAs. As well, the organophosphate pesticide fenamiphos proved to be a weak ATPase inhibitor. Comparison of the enzymatic pair of the CSM ATP-hydrolases seems applicable for evaluation of the specific membrane-acting effect of bioactive compounds on Na+,K+-ATРase activity from the standpoint of its role in mediating of electro-mechanical coupling in intestinal smooth muscles. |
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| ISSN: | 2409-4943 2413-5003 |