neoFroxx® Acetic Acid 96% for analysis, CAS: 64-19-7

Used to manufacture acetic anhydride and other organic chemicals used in the plastic, pharmaceutical, dye, insecticide, textile, rubber, and photographic industries; [ACGIH] Used in photography (stop bath); [www.ci.tucson.az.us/arthazards/medium.html] Used as a wet etchant in semiconductor manufacturing at standard concentrations of 36% or 99.5%; [CSH, p. 46] Used in the bating and tanning stages of leather production; [PMID 21938525]

ACGIH - Documentation of the TLVs and BEIs, 7th Ed. Cincinnati: ACGIH Worldwide, 2020.

Haz-Map, Information on Hazardous Chemicals and Occupational Diseases

Although acetic acid has been shown to induce apoptosis in yeast, the exact apoptotic mechanisms remain unknown. Here, /the study examined/ the effects of acetic acid treatment on yeast cells by 2-DE, revealing alterations in the levels of proteins directly or indirectly linked with the target of rapamycin (TOR) pathway: amino-acid biosynthesis, transcription/translation machinery, carbohydrate metabolism, nucleotide biosynthesis, stress response, protein turnover and cell cycle. The increased levels of proteins involved in amino-acid biosynthesis presented a counteracting response to a severe intracellular amino-acid starvation induced by acetic acid. Deletion of GCN4 and GCN2 encoding key players of general amino-acid control (GAAC) system caused a higher resistance to acetic acid indicating an involvement of Gcn4p/Gcn2p in the apoptotic signaling. Involvement of the TOR pathway in acetic acid-induced apoptosis was also reflected by the higher survival rates associated to a terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling (TUNEL)-negative phenotype and lower reactive oxygen species levels of Deltator1 cells. In addition, deletion mutants for several downstream mediators of the TOR pathway revealed that apoptotic signaling involves the phosphatases Pph21p and Pph22p but not Sit4p. Altogether, /these/ results indicate that GAAC and TOR pathways (Tor1p) are involved in the signaling of acetic acid-induced apoptosis.

PMID:19137548

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Acetic acid was found to have actions on urinary bladder smooth muscle in /the/ routine ion channel screening assays. Numerous studies have examined the mechanisms of bladder irritation by acetic acid; however, the direct effect of acetic acid on ion channels in detrusor smooth muscle cells has not been evaluated. /The study/ used whole-cell patch-clamp techniques to examine the effect of acetic acid on large-conductance Ca2+-activated K+ channels (BKCa) from guinea pig detrusor smooth muscle cells and CHO cells expressing recombinant human BKCaalphabeta1 (CHO BKCaalphabeta1) and human BKCaalpha (CHO BKCaalpha). Acetic acid activated BKCa currents in a concentration-dependent (0.01% to 0.05% v/v) manner in all the cell systems studied. Acetic acid (0.05%) increased BKCa current at +30 mV by 2764 +/- 918% (n=8) in guinea pig detrusor smooth muscle cells. Acetic acid (0.03%) shifted the V1/2 of conductance-voltage curve by 64 +/- 14 (n=5), 128 +/- 14 (n=5), and 126 +/- 12 mV (n=4) in CHO BKCaalpha, CHO BKCaalphabeta1 and detrusor smooth muscle cells, respectively. This effect of acetic acid was found to be independent of pH and was also not produced by its salt form, sodium acetate. Automated patch-clamp experiments also showed similar activation of CHO BKCaalphabeta1 by acetic acid. In conclusion, acetic acid directly activates BKCa channels in detrusor smooth muscle cells. This novel study necessitates caution while interpreting the results from acetic acid bladder irritation model.

PMID:17382925

Hazardous Substances Data Bank (HSDB)

/It was/ previously shown that acetic acid activates a mitochondria-dependent death process in Saccharomyces cerevisiae and that the ADP/ATP carrier (AAC) is required for mitochondrial outer membrane permeabilization and cytochrome c release. Mitochondrial fragmentation and degradation have also been shown in response to this death stimulus. Herein, /the study/ show that autophagy is not active in cells undergoing acetic acid-induced apoptosis and is therefore not responsible for mitochondrial degradation. Furthermore, /the study/ found that the vacuolar protease Pep4p and the AAC proteins have a role in mitochondrial degradation using yeast genetic approaches. Depletion and overexpression of Pep4p, an orthologue of human cathepsin D, delays and enhances mitochondrial degradation respectively. Moreover, Pep4p is released from the vacuole into the cytosol in response to acetic acid treatment. AAC-deleted cells also show a decrease in mitochondrial degradation in response to acetic acid and are not defective in Pep4p release. Therefore, AAC proteins seem to affect mitochondrial degradation at a step subsequent to Pep4p release, possibly triggering degradation through their involvement in mitochondrial permeabilization. The finding that both mitochondrial AAC proteins and the vacuolar Pep4p interfere with mitochondrial degradation suggests a complex regulation and interplay between mitochondria and the vacuole in yeast programmed cell death.

PMID:20345665

Hazardous Substances Data Bank (HSDB)