Oxidation of the 17-aldol (20β hydroxy-21-aldehyde) intermediate of corticosteroid metabolism to hydroxy acids by homogeneous human liver aldehyde dehydrogenases

Monder, Carl; Purkaystha, Auditi; Pietruszko, Regina

doi:10.1016/0022-4731(82)90590-8

Cited by 20 publications

(5 citation statements)

References 22 publications

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“…Other physiological roles of aldehyde dehydrogenases include lipid peroxidation [2], the metabolism of amino acids and biogenic amines [3,4], corticosteroids [5], retinoids [6,7] and protein deglycation [8]. The superfamily also participate in detoxification of exogenous aldehydes from beverages, foods, industrial pollutants etc [9,10].…”

Section: Introductionmentioning

confidence: 99%

Different specificities of two aldehyde dehydrogenases from Saccharomyces cerevisiae var. boulardii

2017

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Aldehyde dehydrogenases play crucial roles in the detoxification of exogenous and endogenous aldehydes by catalysing their oxidation to carboxylic acid counterparts. The present study reports characterization of two such isoenzymes from the yeast Saccharomyces cerevisiae var. boulardii (NCYC 3264), one mitochondrial (Ald4p) and one cytosolic (Ald6p). Both Ald4p and Ald6p were oligomeric in solution and demonstrated positive kinetic cooperativity towards aldehyde substrates. Wild-type Ald6p showed activity only with aliphatic aldehydes. Ald4p, on the contrary, showed activity with benzaldehyde along with a limited range of aliphatic aldehydes. Inspection of modelled structure of Ald6p revealed that a bulky amino acid residue (Met177, compared with the equivalent residue Leu196 in Ald4p) might cause steric hindrance of cyclic substrates. Therefore, we hypothesized that specificities of the two isoenzymes towards aldehyde substrates were partly driven by steric hindrance in the active site. A variant of wild-type Ald6p with the Met177 residue replaced by a valine was also characterized to address to the hypothesis. It showed an increased specificity range and a gain of activity towards cyclohexanecarboxaldehyde. It also demonstrated an increased thermal stability when compared with both the wild-types. These data suggest that steric bulk in the active site of yeast aldehyde dehydrogenases is partially responsible for controlling specificity.

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Section: Introductionmentioning

confidence: 99%

Different specificities of two aldehyde dehydrogenases from Saccharomyces cerevisiae var. boulardii

2017

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“…They participate in the detoxification of acetaldehyde (1, 2), the metabolism of biogenic amines (3), corticosteroids (4) and retinoic acid (5, 6). To date, 17 isoforms of ALDH had been described (7).…”

Section: Introductionmentioning

confidence: 99%

ALDH1 expression correlates with favorable prognosis in ovarian cancers

et al. 2009

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Aldehyde dehydrogenase 1 (ALDH1), a detoxifying enzyme responsible for the oxidation of intracellular aldehydes, was shown to play a role in the early differentiation of stem cells, through its role in oxidizing retinol to retinoic acid. It has been shown that ALDH1 is a predictor of poor clinical outcome in breast cancer. The authors hypothesized that the level of ALDH1 expression may be correlated with the clinical outcome of patients with ovarian cancer. Immunohistochemical staining of ALDH1 expression was analyzed in 442 primary ovarian carcinomas using tissue microarray. The associations between the expression of the ALDH1 and clinical factors (diagnosis, tumor grade, stage, and clinical response to chemotherapy), as well overall and disease-free survival were analyzed. Expression of ALDH1 was found in 48.9% of the samples. Fisher's exact test suggested that high expression of ALDH1 was significantly associated with endometrioid adenocarcinoma (P < 0.0001), early-stage disease (P = 0.006), complete response to chemotherapy (P <0.05) and a low serum level of CA125 (P = 0.02). High percentage of cells expressing ALDH1 was associated with a longer overall survival time (P =0.01) and disease free survival time (P = 0.006) by Log rank test. In contrast to its role in breast cancer, ALDH1 was a favorable prognostic factor in ovarian carcinoma. ALDH1 therefore may play a different role in ovarian cancer than it does in breast cancer.

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“… 33 Furthermore, ALDH enzymes have been shown to oxidize corticosteroids. 34 , 35 This suggests the hypothesis that plasma ALDH preemptively degrades GCs and potentiates GC resistance. Our observation of higher plasma ALDH1B1 levels in patients with SRNS is consistent with this hypothesis.…”

Section: Discussionmentioning

confidence: 99%

Multiomics Analysis of Plasma Proteomics and Metabolomics of Steroid Resistance in Childhood Nephrotic Syndrome Using a “Patient-Specific” Approach

Bhayana¹,

Zhao²,

Merchant³

et al. 2023

Kidney International Reports

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Oxidation of the 17-aldol (20β hydroxy-21-aldehyde) intermediate of corticosteroid metabolism to hydroxy acids by homogeneous human liver aldehyde dehydrogenases

Cited by 20 publications

References 22 publications

Different specificities of two aldehyde dehydrogenases from Saccharomyces cerevisiae var. boulardii

Different specificities of two aldehyde dehydrogenases from Saccharomyces cerevisiae var. boulardii

ALDH1 expression correlates with favorable prognosis in ovarian cancers

Multiomics Analysis of Plasma Proteomics and Metabolomics of Steroid Resistance in Childhood Nephrotic Syndrome Using a “Patient-Specific” Approach

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