Histone Acetylation is not Affected by Chloroacetamides in vitro

Kring, Friedhelm; Böger, Peter

doi:10.1515/znc-1994-5-605

Cited by 5 publications

(3 citation statements)

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“…Recently, the possible inhibition of histone acetylation in vitro by these herbicides was ruled out. 6 In S. acutus, micromolar concentrations of alachlor or metazachlor were found to cause a sharp decrease in fatty acid desaturation. 7,8 The primary target site could not be convincingly ascribed to any of these e †ects, and it has been proposed that these herbicides could be multifunctional.…”

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confidence: 99%

A specific and sensitive assay to quantify the herbicidal activity of chloroacetamides

1998

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: Based on a recently discovered property of chloroacetamide herbicidesÈthe inhibition of the incorporation of oleic acid into sporopollenin of Scenedesmus acutusÈa rapid quantitative test was developed for chloroacetamide-type herbicidal activity. In this test, algal cells are incubated for 3 h with [14C]oleic acid, saponiÐed and the lipids (including non-saponiÐable ones) extracted and discarded. The radioactivity incorporated into the residual non-lipid fraction is determined, and inhibition of this incorporation is used as a marker of chloroacetamide-type activity. Twenty-two agrochemical compounds were screened in this assay, which was found to be very sensitive, a 50% inhibition being reached with submicromolar herbicide concentrations. It is speciÐc to chloroacetamides and related amides, since all these herbicides tested were potent inhibitors, while other herbicides were not. Highest inhibition was shown by cafenstrole followed by butachlor, Ñuthiamid, metazachlor, alachlor, dimethenamid, metolachlor and mefenacet. For these herbicides (with the exception of butachlor) sensitivity in the test was positively correlated (r \ 0É984) with their phytotoxic e †ect on the alga.1998 SCI ( Pestic. Sci., 52, 381È387 (1998)

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Section: Introductionmentioning

confidence: 99%

A specific and sensitive assay to quantify the herbicidal activity of chloroacetamides

1998

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“…Therefore the functionality as a free radical scavenger should not be excluded for phenyl acetate, acetanilide and 4-acetamidophenylacetic acid. On the other hand, there is also evidence that acetamides do not affect the activity of cell enzymes like histone acetyltransferase and histone deacetylase which have a crucial role in the regulation of transcription and replication (Kring and Böger, 1994).…”

Section: Discussionmentioning

confidence: 99%

Inhibitory Effect of Some Acetyl Esters and Acetamides on Glycation of the Histone H1

Stoynev

Srebreva

Gugova

et al. 2008

Zeitschrift Für Naturforschung C

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Non-enzymatic glycosylation (glycation) is a spontaneous set of reactions between reducing sugars and free amino groups in proteins or other biomolecules leading to the formation of fluorescent and coloured compounds known as advanced glycation end products (AGEs). AGEs cause structural changes of key proteins in humans, and therefore they are related with a number of physiological processes and diseases such as aging, atherosclerosis, cataract, arthritis, Alzheimer's disease. Two main strategies have been employed to prevent the formation of AGEs: a) low carbohydrate diet and b) pharmacological intervention. The latter includes treatment with reactive compounds which might be either sugar competitors (type A), carbonyl traps (type B) or free radical trapping antioxidants (type C). Acetylsalicylic acid (ASA, aspirin) is a good example of sugar competitor capable of inhibiting glycation by acetylating ε-amino groups of lysine residues in proteins. Taking into consideration the inhibiting effect of ASA on glycation we designed to study the antiglycation activity of other acetyl group-containing compounds (acetamides and acetyl esters) using the lysine-rich protein histone H1 as a model. The glycation of the histone H1 was carried out by either fructose or a complex mixture of glycating agents obtained from E. coli and monitored by fluorescent spectroscopy, SDS-PAGE and measurement of the content of reactive carbonyl groups in the target protein. Our results showed that the inhibitory effect of phenyl acetate, acetanilide, 4-acetamidophenylacetic acid and isopropenyl acetate was comparable to that of ASA. Based on the obtained results we conclude that these compounds act as free radical scavengers protecting proteins from the damaging effect of reactive oxygen species produced during the formation of AGEs.

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“…17 It has been shown that concentrations below 1 j M exerted lethal phytotoxicity in metazachlor-treated maize leaves18 or rice seedlings. 19 So, a sensitive target site appears to be present in the (meristematic) plant cell and the primary mode of action may be located in the lipid At the moment our studies are guided by the hypothesis that a key target is responsible for several subsequent metabolic disturbances.…”

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