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At least 19 recordsLinked to original sources
PubMed2026

Diving Deeper Into Mechanisms of Acrylamide-Induced Toxicity: RNA Sequencing Reveals Transcriptomic Alteration and Retrotransposon Expression in Drosophila melanogaster.

Given the inevitability of human and animal exposure to acrylamide, there is increasing concern regarding its potential health risks. While a number of molecular mechanisms have been proposed, the complexity of acrylamide toxicological pathways and interactions remains incompletely characterized. In this study, we employed a transcriptomic approach to investigate the transcriptional responses of Drosophila melanogaster following exposure to acrylamide (100 mg/kg). Our analysis identified 634 differentially expressed genes (DEGs), with 362 upregulated and 272 downregulated. Functional analysis revealed these DEGs are enriched in pathways related to reproduction, detoxification, cellular and metabolic processes, signaling, synaptic formation and organization. Notably, acrylamide exposure upregulated the expression of tau and beta-amyloid protein precursor-like genes, both implicated in Alzheimer's disease pathology. An aversive memory test further demonstrated that acrylamide impaired the short-term memory of treated flies. Additionally, acrylamide-induced toxicity altered the expression of nine long terminal repeat retrotransposons, belonging to the gypsy and pao superfamilies. By exploring the potential role of transposable element activity in acrylamide-mediated toxicity, this study provides novel insights into the molecular mechanisms underlying its effects. Collectively, these findings offer a more comprehensive understanding of the mechanisms and pathways associated with the toxic action and detoxification of acrylamide in D. melanogaster.

Animals↗
PubMed2026

Changes in the chick liver structure and blood plasma biochemical properties following in ovo administration of acrylamide.

This study analyzed the effects of acrylamide administration during the embryonic period on liver microstructure and blood plasma biochemical parameters in hatched chicks. On day 6 of incubation, 96 embryonated eggs per group were injected with acrylamide (ACR) at doses of 0.0, 0.25, 0.5, 1.0, 2.0 and 4.0 mg ACR/egg dissolved in 0.9% saline solution (100 µL). Embryo development, hatchability and quality of chicks were evaluated. The ten chicks per group (0.0, 0.25, 0.5 and 1.0 mg ACR/egg) were euthanized immediately after hatching, and blood and liver samples were collected for further analysis. Hatchability was 74.0, 67.7, 66.7 and 49.5% in groups treated with 0.0, 0.25, 0.5, 1.0 mg ACR/egg, respectively, while all embryos died in 2.0 and 4.0 mg ACR/egg groups. Acrylamide intoxication affected only a few biochemical parameters of blood, including a significant decrease in glucose and globulin levels in the group injected with a dose of 1 mg/egg and a significant increase in blood urea nitrogen concentration in the group treated with a dose of 0.5 mg/egg. However, this substance caused negative changes in the microarchitecture of the liver of one-day-old chicks, as indicated by the results of histomorphometric analysis, such as an increase in total hepatocyte nuclei, binucleated hepatocytes, cell nucleus size, collagen area, and other cells. Furthermore, abnormalities in liver structure were confirmed by trace elements content results. Thus, in individuals treated with acrylamide (0.25 and 0.5 mg/egg), a decrease in copper levels and (0.25 mg/egg) nickel and iron levels and an increase in cadmium levels were observed. An increase in lead content was similarly observed in the group exposed to acrylamide at a dose of 0.5 mg/egg, as well as an increase in zinc levels in groups administered various doses of this toxic substance. Overall, the results suggest an inconsistent and dose-dependent toxic effect of acrylamide on liver structure and selected blood plasma parameters in one-day-old chicks.

Acrylamide↗
PubMed2026

Furanic compounds in different coffee extraction systems: Analysis of the main influencing factors and correlation with acrylamide.

This study investigates how different coffee types representative of distinct roast profiles and brewing methods jointly affect the occurrence of furanic compounds and acrylamide in brewed coffee. Coffees were prepared using eight extraction methods (AeroPress, Clever, Chemex, French Press, Moka, Pure Brew, Turkish and V60). Five furanic compounds (furfural, furfuryl acetate, 5-methylfurfural, furfuryl alcohol and 5-hydroxymethylfurfural) were quantified in coffee powders and brews by HS-SPME-GC-MS, while acrylamide was determined by UHPLC-MS/MS. Moka and Turkish brews consistently exhibited the highest concentrations of furanic compounds, whereas paper-filtered pour-over methods (V60 and Chemex) showed the lowest levels. Pearson correlation analysis revealed coffee-dependent relationships between furanic compounds, acrylamide and extraction parameters with the strongest associations observed in dark-roasted coffee, reflecting advanced Maillard reaction chemistry. Overall, these results demonstrate that contaminant levels arise from the combined effects of intrinsic coffee chemistry and brewing mechanics and support targeted mitigation strategies: such as roast selection and brewing method optimization.

Acrylamide↗
PubMed2026

Advanced mitigation strategies for acrylamide formation in foods: Mechanistic insights, emerging innovations, and future perspectives.

Acrylamide is a heat-induced contaminant formed predominantly in carbohydrate-rich foods during high-temperature processing, posing significant concerns due to its potential carcinogenic, neurotoxic, and genotoxic effects. This review critically examines the mechanisms of acrylamide formation, emphasizing the role of the Maillard reaction and key precursors such as asparagine and reducing sugars, along with the influence of processing conditions including temperature, time, pH, and moisture. Various mitigation strategies are comprehensively discussed, ranging from raw material selection and genetic approaches to enzymatic treatments such as asparaginase and the application of natural and chemical inhibitors. Advances in processing technologies, including optimization of conventional thermal methods and emerging non-thermal techniques such as cold plasma and ultrasound, are evaluated for their effectiveness. The review also highlights the role of food additives, functional ingredients, and fermentation in reducing acrylamide formation. Furthermore, recent developments in analytical techniques, including chromatographic methods, biosensors, and artificial intelligence-based predictive models, are explored for improved detection and control. Risk assessment, toxicological implications, and global regulatory frameworks are also examined. Finally, future perspectives focusing on genetic engineering, personalized nutrition, and digital technologies such as AI and blockchain are discussed to support sustainable and industry-applicable mitigation strategies.

Acrylamide↗
PubMed1976

Enzymatic attack on side chains of synthetic polymers. Chymotrypsin-catalyzed hydrolysis of specific substrate groups attached to acrylamide or acrylic acid co-polymers.

Three vinyl monomers, M-1, M-3, and M-5, in which L-phenylalanine p-nitroanilide was acylated with CH2==CHCONH(CH2)nCO--(n = 1, 3, 5) were synthesized. They were co-polymerized with a large excess of acrylamide (co-polymers PAm-1, PAm-3, and PAm-5) and with a large excess of acrylic acid (co-polymers PAc=1, PAc-3, and PCc-5). In addition, M-5 was co-polymerized with acrylamide containing 2.8 mol % of the hydrophobic monomer N-acrylyl-1-naphthylamine (co-polymer PAm-5N). The rates of the chymotrypsin-catalyzed hydrolysis of the nitroanilide groups of M-5 and the various co-polymers were determined over a range of pH. For some of the systems data were also obtained over a range of substrate concentrations to derive values for Vmax and Km. Results obtained with PAm-5 were found to be independent of the chain length of the co-polymer. At pH 7, 25 degrees and with 2.7 X 10(-6) M enzyme, Vmax values for M-5, PAm-k, PAm-5N, and PAc-5 were 5.5, 5.5, 10, and 3.6 X 10(-8) M/S, while Km values were 8.5, 16.5, 10, and 2.2 X 10(-5),respectively, With PAc-5, the pH activity profile was shifted to higher acidities as compared to the profiles obtained with M-5 and PAm-5. The susceptibility of the co-polymers to chymotrypsin attack decreases sharply with a decreasing spacing of the L-phenylalanine p-nitroanilide residue from the backbone of the polymer chains.

Acrylamides↗
PubMed1977

A cis-trans isomerising activity of Escherichia coli. Isomerization from 2-(2-furyl)-3-cis-(5-nitro-2-furyl) acrylamide (furylfuramide) to its trans isomer.

The soluble enzyme fraction derived from Escherichia coli K-12 JE2100 cells was found to exhibit, in addition to Nadh- and NADPH-dependent reductase activities, NADH-dependent cis-trans isomerising activity toward 2-(2-furyl-3-(5-nitro-2-furyl)acrylamide leading to a specific change in geometrical configuration of the vinyl group at the 2-position from cis to trans but not in the reverse direction. This furylfuramide-isomerising action of bacteria was dicoumarol insensitive, and did not require glutathione for full activity. The particulate enzyme fraction derived from JE2100 cells, although it showed little reductase activity toward furylfuramide in the presence of either NADH or NADPH, revealed an isomerising activity in the presence of NADH.

Acrylamides↗
PubMed1979

trans-alpha, beta-Diformamido-beta-(5'-phosphoribosylamino)acrylamide: a possible new intermediate in de novo purine biosynthesis.

The nucleotide trans-alpha, beta-diformamido-beta-(5'-phosphoribosylamino)acrylamide (DAR) has been chemically synthesized and is converted to inosine 5'-phosphate (IMP) by enzyme activities found in chicken, rat, and human liver. The increase in optical density at 250 nm when DAR is converted to IMP is used as the basis of the assay. The Km values for DAR at pH 7.4 were 2.8 and 4.2 microM with the chicken and rat liver enzymes, respectively. The integrated Michaelis--Menten equation was used to determine the kinetic parameters of the chicken liver enzyme from pH 5.6 to 10.1. The pH--activity profiles show ionizations with pKa values of 6.1, 7.1, and 8.8. The possibilities that DAR is a substrate analogue or a new intermediate in the pathway of purine biosynthesis de novo are discussed.

Acrylamides↗
PubMed1977

Isoelectric focus analysis of rat anti-phosphocholine antibodies.

Anti-phosphocholine (PC) antibodies in sera from four strains of rats were examined before and afterimmunization with either Streptococcus pneumoniae R36A, which contains PC as a cell wall component, or with PC-coupled keyhole limpet hemocyanin (PC-KLH). PC-specific protein was purified from pooled immune sera and shown by a combination of isoelectric focus (IEF) in acrylamide and crossed immunoelectrophoresis, as well as by molecular weight determination in NaDodSO4-acrylamide, to be immunoglobulin. An additional, small molecular weight, nonimmunoglobulin protein (pI = 7.1-7.3) was present in sera from normal and germ-free rats which had the ability to bind the C-carbohydrate of S. pneumoniae R36A, but without specificity for PC. The IEF profile of normal and immune sera showed marked sharing of bands of anti-PC antibody between individual rats as well as between strains. In addition, other anti-PC antibodies which focused between pH 8.5 and 9.5 were less regularly shared. The uniformity of IEF profile of the bulk of anti-PC antibodies in rats is most consistent with their being the products of germ line genes.

Animals↗
PubMed1977

Purification and properties of the pyrrolidonecarboxylate peptidase of Streptococcus faecium.

Pyrrolidonecarboxylate peptidase (EC 3.4.11.8) from Streptococcus faecium was purified by fractionation with streptomycin sulphate and ammonium sulphate, by chromatography on Sephadex G200 and DEAE-cellulose, and by preparative electrophoresis on Sephadex G25. The purified enzyme on acrylamide gel showed a strong protein band which contained enzyme activity and a very faint band which had no activity. The subunit molecular weight of the purified enzyme was estimated by acrylamide gel electrophoresis in sodium dodecyl sulphate to be 42,000 +/- 1,000. The enzyme showed optimum activity at pH 7.6 and was unstable in the absence of 2-mercaptoethanol. The sensitivity of the enzyme to alkylating agents (N-ethylmaleimide and iodoacetamide) suggested that free sulphydryl groups were essential for enzyme activity. The enzyme was rapidly inactivated above 45 degrees C. The values of the Michaelis constants (Km) obtained with various L-pyrrolidonecarboxylyl dipeptides were similar although there was a 10-fold range in the maximal rates of hydrolysis of these substrates. Inhibition studies showed that the substrate analogues 2-pyrrolidone and pyrrolidonecarboxylate are competitive inhibitors of the enzyme. The binding of substrates and inhibitors to the active site of the enzyme is discussed.

Aminopeptidases↗
PubMed1978

Isolation of gamma-glutamyltransferase from human liver, and comparison with the enzyme from human kidney.

We isolated gamma-glutamyltransferase [(gamma-glutamyl)-peptide:amino acid gamma-glutamyltransferase, EC 2.3.2.2] from human liver and compared some of its properties with the same enzyme prepared from human kidney. The enzymes from these two sources are very similar with respect to initial velocity kinetic constants, pH optima of the transpeptidation and autotransfer reactions, heat stability, competitive inhibition by glutathione of the colorimetric assay in which gamma-glutamyl-4-nitroanilide is substrate, stability of catalytic activity to trypsinization, and relative rates of transfer of the gamma-glutamyl moiety from gamma-glutamyl-4-nitroanilide and L-[glycine-2-3/]glutathione to some amino acids and small peptides. The kidney enzyme is inhibited more by the gamma-glutamyl acceptor substrate, glycylglycine, as reflected in a sevenfold lower value for the inhibition constant KiA. Major differences were observed in the lectin-binding properties of liver gamma-glutamyltransferase compared to the kidney enzyme. Lectin-binding property differences are retained for the trypsinized form of the liver and kidney enzymes, although the degree of precipitation was less for certain lectins as compared to the untreated enzyme. Lectin-binding properties were reversed by carbohydrates specific for each lectin. We adapted the histochemical staining technique of Rutenberg et al. [J. Histochem. Cytochem. 17, 517 (1969)] to the detection of gamma-glutamyltransferase activity in acrylamide gels; diffusion artifacts are minimized and the color produced is stable for several days. Untreated and trypsinized forms of the liver enzyme both migrated faster in acrylamide gels (as single bands) than did the corresponding forms of the kidney enzyme.

Humans↗
PubMed2026

The science of Arabic coffee (Qahwa): from phytochemistry and nutritional profile to health benefits and safety evaluation.

Arabic coffee (Qahwa), a traditional beverage widely consumed in the Middle East, has attracted increasing scientific attention due to its distinctive phytochemical composition and associated health effects. This review provides an integrated analysis of Qahwa's nutritional profile, focusing on its key bioactive constituents, including chlorogenic acids, caffeine, diterpenes (cafestol and kahweol), and phenolic compounds. These constituents contribute to a range of biological activities, notably antioxidant, anti-inflammatory, hepatoprotective, and metabolic regulatory effects. The influence of technological variables, including roasting degree, brewing method, and bean origin, on the chemical composition and functional properties is critically examined. Safety concerns, particularly acrylamide formation and mycotoxin contamination, are also discussed. Although emerging data support Qahwa's potential as a functional beverage, further research is required to clarify dose-response relationships, synergistic interactions, and long-term health outcomes. This work highlights Qahwa as a promising candidate for food and nutraceutical applications, warranting standardized compositional profiling and toxicological evaluation.

Humans↗
PubMed1975

[Erythrocyte stroma included in polyacrylamide gel. Applications to affinity chromatography].

Stromata prepared with human or animal red blood cells are suspended in acrylamide solution. Gel as prepared for electrophoresis is dispersed, before use, and can be used in chromatographic columns for the retention of agglutinins. Lectins, e.g., where first absorbed and then eluted with solution of inhibitory sugar or with acid buffer. Some applications are mentioned.

Acrylamides↗
PubMed2025

Dynamic Evolution of Poly-A Tail Lengths Visualized by RNAse H Assay and Northern Blot Using Nonradioactive Probes in Yeast.

Poly-A tail length dynamics have been extensively studied from yeast to human, mostly using reporter transcripts. Recent studies have been carried out genome-wide to determine the status of poly-A tails at steady state. However, poly-A tail measurement at equilibrium gives an overall length that reflects a mixture of the different poly-A tail sizes for a single transcript. New genome-scale techniques are emerging to estimate dynamic of poly-A tails lengths, but they are not yet routine and individual validation experiments are useful. In this chapter we describe a protocol for visualizing poly-A tail lengths following transcription inhibition for a reporter mRNA using denaturing poly-acrylamide gel electrophoresis and northern blot assay. This protocol is quick to set up, requires the purchase of only a few specific reagents, does not rely on radioactivity for RNA monitoring, and can be easily implemented in any molecular biology laboratory.

Poly A↗
PubMed1978

Studies of rat alkaline phosphatase I. Development of methods for detecting isoenzymes.

A manual system of various estimations of rat plasma alkaline phosphatase activity has been devised for small volumes of plasma which uses different inhibitors, compares the utilisation of two substrates and includes acrylamide gel electrophoresis. The different inhibitors etc. allow a degree of discrimination between alkaline phosphatase extracts of rat organs. The properties of isoenzymes, e.g. intestinal phosphatase, differ depending upon the environment in which they are studied. In conjunction, if necessary, with the methods described for the estimation of liver and intestinal alkaline phosphatase activity, it is hoped to use the system to discriminate between the isoenzymes present in the plasma alkaline phosphatase of rats in toxicological studies.

Alkaline Phosphatase↗