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Inventory Resources and Risks for Recovery
Published in Sandra Rasmussen, Developing Competencies for Recovery, 2023
We accept as a fact that “addiction runs in families.” Scientists estimate that genetic factors account for 40 to 60% of a person’s risk to develop an addiction. More than one in three people with East Asian heritage (Chinese, Japanese and Korean) experience facial flushing when drinking beer, wine, or spirits. In Asian populations, flushing is due to an inherited deficiency in one of the enzymes involved in the breakdown of alcohol: aldehyde dehydrogenase. This type of reaction is very rare, but not unknown, in other ethnic groups.
Critical Appraisal of Animal Models for Antibiotic Toxicity
Published in Adorjan Aszalos, Modern Analysis of Antibiotics, 2020
Patricia D. Williams, Girard H. Hottendorf
The disulfiramlike activity associated with some of the newer cephalosporins has been described as an “acetaldehyde syndrome” relating to inhibition of liver aldehyde dehydrogenases. A rat model has been reported that demonstrates elevated blood acetaldehyde levels and decreased activity of liver aldehyde dehydrogenase following administration of alcohol in conjunction with disulfiram or cephalosporins, such as moxalactam, cefoperazone, and cefaman-dole [138,139]. Comparative pharmacokinetic and metabolic profiles of these cephalosporins in the human and the rat are necessary prior to determiningthe validated use of the rat in predicting risk to the human and in comparative assessments of potency. A key issue is the comparative degree of liberationof the methyltetrazolethiol substituent of these cephalosporins that is presumably responsible for the effects observed.
Liver Diseases
Published in George Feuer, Felix A. de la Iglesia, Molecular Biochemistry of Human Disease, 2020
George Feuer, Felix A. de la Iglesia
Two enzyme systems are involved in the metabolism of alcohol; one is cytosolic, and the other is microsomal. Alcohol and aldehyde dehydrogenases are cytosolic components mainly responsible for the first two steps of alcohol oxidation.57,233,288,544 The second alcohol oxidizing enzyme complex is bound to the microsomal fraction.36,549 Alcohol dehydrogenase is found mainly in the liver. This enzyme is the rate-limiting step in the metabolism of alcohol (Figure 34). In the human liver, there are three to seven active alcohol dehydrogenase isoenzyme fractions with variable activity.280,565,610 The isoenzymes composition varies widely from and with different turnover rates, thus explaining the individual and ethnic variations. Aldehyde dehydrogenase is present in many tissues,564 and several isoenzymes have been identified.234,246,425,474 Animal experiments have shown that with alcohol pretreatment the activity of alcohol dehydrogenase increases. This adaptive change may be important in the development of tolerance in alcoholism.
Improving mitochondrial function in preclinical models of heart failure: therapeutic targets for future clinical therapies?
Published in Expert Opinion on Therapeutic Targets, 2023
Anna Gorący, Jakub Rosik, Joanna Szostak, Bartosz Szostak, Szymon Retfiński, Filip Machaj, Andrzej Pawlik
Mitochondrial dysfunction also leads to increased lipid peroxidation, resulting in the production of highly reactive carbonyls, such as various ketones, alkanes, and aldehydes. A key role in these processes is played by aldehyde dehydrogenase (ALDH2). ALDH2 is involved in the removal and metabolism of exogenous chemicals and endogenous reactive aldehydes to maintain homeostasis and normal mitochondrial function [200]. This enzyme appears to be a promising target for therapy aimed at improving mitochondrial function in patients with HF. In an animal model of HF induced by myocardial infarction, ALDH2 activation was shown to reduce the concentration of reactive aldehydes in cardiomyocytes and limited. Most therapies to date affecting mitochondrial metabolism have focused on single factors or processes disrupted in HF. However, in this disease, there are multidirectional disorders improve mitochondrial bioenergetics [201]. Moreover, sustained ALDH2 activation prevented myocardial hypertrophy, fibrosis, and cardiac dysfunction.
Caudatin blocks the proliferation, stemness and glycolysis of non-small cell lung cancer cells through the Raf/MEK/ERK pathway
Published in Pharmaceutical Biology, 2022
Juan Hou, Qing Chen, Yufeng Huang, Zhiwei Wu, De Ma
Cancer stem cells have the abilities of unlimited proliferation, self-renewal and multidirectional differentiation, which easily induce tumour residue and recurrence (Yanamoto et al. 2014). Besides, CSCs weaken the efficacy of radiotherapy through DNA damage repair and cytoprotective autophagy, resulting in poor prognosis (Lin et al. 2015; Vitale et al. 2017). Thus, CSCs related biological markers have been taken as therapeutic targets in cancer treatment (Sun JH et al. 2016; Eun et al. 2017). ALDH1A1, SOX2, NANOG and OCT-4 are all acknowledged biomarkers of lung cancer (Lu et al. 2020; Masciale et al. 2020). Overexpressed OCT4 always presages tumour occurrence, metastasis, recurrence and drug resistance (Jen et al. 2017). Aldehyde dehydrogenase participates in the self-protection, differentiation and expansion of CSCs, and affects the prognosis of malignant tumours (Tomita et al. 2016). Liu X et al. (2016) reported that ALDH1A1 inhibition suppressed the recurrence of NSCLC driven by ALDH-positive CSCs. Yang et al. (2021) reported that XMD-17-51 blocked the progression of lung cancer by reducing the expression of SOX2, NANOG and OCT4. In our study, caudatin treatment markedly suppressed cell viability and induced cell apoptosis. Caudatin treatment effectively weakened the sphere formation efficiency of H1299 and H520 cells and decreased the ratio of ALDH positive cells, indicating that cell stemness was sharply weakened. At the protein level, the expression of SOX2, OCT4 and Nanog was all down-regulated by caudatin. Thus, the antitumor effects of caudatin on NSCLC were related to stemness inhibition.
Incomplete penetrance of autosomal recessive anophthalmia in a large consanguineous family
Published in Ophthalmic Genetics, 2021
Masoud Dehghan Tezerjani, Behdokht Fathi Dizaji, Zahra Metanat, Mohammad Yahya Vahidi Mehrjardi
Anophthalmia (absence of eyes) and microphthalmia (small eyes) or A/M represents severe congenital defects of eye development. A/M can be uni- or bilateral and is prevalent at 3:100,000 to 30:100,000 (1). Both environmental and genetic factors contribute to A/M. However, genetic mutations are the predominant etiology including chromosomal abnormalities and mutations in over 100 genes with all patterns of Mendelian inheritance. In addition, variable expressivity between and within families has been reported. Mutations in most genes have shown full penetrance, but incomplete penetrance has been described in few genes (2). Numerous mutations in the aldehyde dehydrogenase 1 family member A3 (ALDH1A3) on chromosome 15q26.3 have been identified, which are believed to be responsible for approximately 10% of autosomal recessive A/M in consanguineous families of different ethnicities (3). This gene encodes an aldehyde dehydrogenase enzyme that biosynthesizes retinoic acid. The retinoic acid gradient along with the dorsoventral axis is essential for eye development (4). Genetic analysis of three Iranian patients suffering from non-syndromic bilateral anophthalmia using genome-wide SNP genotyping and autozygosity mapping revealed a novel homozygous missense mutation c.709 G>A in exon 7 of ALDH1A3 gene causing p.Gly237Arg substitution (5). Nevertheless, here we report a non-penetrance case who is a relative of our studied family with the same homozygous mutation in the ALDH1A3 gene without ocular involvement.