RESUMO
Objective: Poor distillation practices in the production of spirits have historically resulted in many instances of adverse health outcomes including death. Concern has focused on lead and copper contamination as well as unhealthy levels of methanol and glyphosate. This study assesses home-distilled and commercially distilled alcohols from Texas for these substances of concern, highlighting their potential risks to public health. Methods: Atomic absorption spectroscopy, gas chromatography, and enzyme-linked immunosorbent assay were employed to determine lead and copper, methanol, and glyphosate levels in 12 commercial and 36 home-distilled alcohol samples. Results: Our findings showed that 11 % of the home-distilled alcohols exceeded the U.S. Alcohol and Tobacco Tax and Trade Bureau's copper safety limits of 0.5 mg/L for wine. Additionally, 36 % of these samples surpassed the European Commission (EC)'s lead legal threshold of 0.15 mg/L set for wine products. Results from commercial alcohols indicated that no samples exceeded the same safety limits for copper, and 33 % exceeded the same legal threshold for lead. Both commercial and home-distilled alcohols exhibited methanol concentrations remarkably below the 0.35 % limit for brandy set by the U.S. Food and Drug Administration. Only two home-distilled samples contained detectable glyphosate concentrations well below 100 µg/L, the maximum residue level in beer and wine established by the EC. Conclusions: Our findings suggested that consumption of alcohol in Texas may pose potential health risks associated with the elevated content of lead and copper. There is a need for increased focus on alcohol as a potential source of exposure to heavy metals.
RESUMO
A20 binding inhibitor of nuclear factor kappa B (NF-κB)-1 (ABIN-1), a polyubiquitin-binding protein, is a signal-induced autophagy receptor that attenuates NF-κB-mediated inflammation and cell death. The present study aimed to elucidate the potential role of ABIN-1 in mitophagy, a biological process whose outcome is decisive in diverse physiological and pathological settings. Microtubule-associated proteins 1A/1B light chain 3B-II (LC3B-II) was found to be in complex with ectopically expressed hemagglutinin (HA)-tagged-full length (FL)-ABIN-1. Bacterial expression of ABIN-1 and LC3A and LC3B showed direct binding of ABIN-1 to LC3 proteins, whereas mutations in the LC3-interacting region (LIR) 1 and 2 motifs of ABIN-1 abrogated ABIN-1/LC3B-II complex formation. Importantly, induction of autophagy in HeLa cells resulted in colocalization of ABIN-1 with LC3B-II in autophagosomes and with lysosomal-associated membrane protein 1 (LAMP-1) in autophagolysosomes, leading to degradation of ABIN-1 with p62. Interestingly, ABIN-1 was found to translocate to damaged mitochondria in HeLa-mCherry-Parkin transfected cells. In line with this observation, clustered regularly interspaced short palindromic repeats (CRISPR)/CRISPR-associated protein 9 (Cas9)-mediated deletion of ABIN-1 significantly inhibited the degradation of the mitochondrial outer membrane proteins voltage-dependent anion-selective channel 1 (VDAC-1), mitofusin-2 (MFN2), and translocase of outer mitochondrial membrane (TOM)20. In addition, short interfering RNA (siRNA)-mediated knockdown of ABIN-1 significantly decreased lysosomal uptake of mitochondria in HeLa cells expressing mCherry-Parkin and the fluorescence reporter mt-mKEIMA. Collectively, our results identify ABIN-1 as a novel and selective mitochondrial autophagy regulator that promotes mitophagy, thereby adding a new player to the complex cellular machinery regulating mitochondrial homeostasis.