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Last update 08 May 2025

ALDH1A3

Last update 08 May 2025

Basic Info

Synonyms

aldehyde dehydrogenase 1 family member A3, Aldehyde dehydrogenase 6, Aldehyde dehydrogenase family 1 member A3

+ [5]

Introduction

Catalyzes the NAD-dependent oxidation of aldehyde substrates, such as all-trans-retinal and all-trans-13,14-dihydroretinal, to their corresponding carboxylic acids, all-trans-retinoate and all-trans-13,14-dihydroretinoate, respectively (By similarity) (PubMed:27759097). High specificity for all-trans-retinal as substrate, can also accept acetaldehyde as substrate in vitro but with lower affinity (PubMed:27759097). Required for the biosynthesis of normal levels of retinoate in the embryonic ocular and nasal regions; a critical lipid in the embryonic development of the eye and the nasal region (By similarity).

Drugs associated with ALDH1A3

NR6

Target

ALDH1A3

Mechanism

ALDH1A3 inhibitors

Active Org.

Università degli Studi del Piemonte Orientale Amedeo Avogadro

Originator Org.

Università degli Studi del Piemonte Orientale Amedeo Avogadro

Active Indication

Malignant Pleural Mesothelioma

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

US20240174634

Patent Mining

Target

ALDH1A3 x ALDH2

Mechanism

ALDH2 inhibitors

Active Org.

Cancer Research Technology Ltd.

Originator Org.

Cancer Research Technology Ltd.

Active Indication

Cardiovascular Diseases [+3]

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

ABD-3171

Target

ALDH1A3

Mechanism

ALDH1A3 inhibitors

Active Org.

Advanced BioDesign SAS

Originator Org.

Advanced BioDesign SAS

Active Indication

Colorectal Cancer [+3]

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with ALDH1A3

100 Translational Medicine associated with ALDH1A3

0 Patents (Medical) associated with ALDH1A3

514

Literatures (Medical) associated with ALDH1A3

01 Dec 2025·Molecular Genetics and Genomics

PPAR γ changing ALDH1A3 content to regulate lipid metabolism and inhibit lung cancer cell growth

Article

Author: Peng, Meiling ; Tian, Xinyuan ; Li, Kai ; Cui, Hongwei ; Bai, Xiaoping ; Ye, Yu ; Han, Yunqi

PPAR γ, as a widely present receptor in tissues, plays a key role in lipid metabolism, energy balance, inflammatory response, and cell differentiation. It plays an important role in the occurrence and development of various tumors, including prostate cancer, gastric cancer, lung cancer, etc., by regulating lipid metabolism. However, the specific mechanism by which it affects lung cancer growth is not yet clear. To investigate how PPAR γ affects lung cancer cell growth by altering ALDH1A3 levels through its impact on lipid metabolism. Bioinformatics analysis was used to predict the correlation between PPAR γ, ALDH1A3 and lung cancer. Based on the results of bioinformatics analysis, PPAR γ activator (Pioglitazone, Pio) and ALDH1A3 inhibitor (diethylaminobenzaldehyde, DEAB) were used to act on lung cancer cells and observe their growth. After measuring the IC50 value of the drug in vitro experiments, lipid metabolomics analysis was conducted to identify the significant changes in differential metabolites and metabolic pathways under the combined influence of Pio and DEAB. Through bioinformatics analysis, it was found that there were significant differences in the levels of PPAR γ and ALDH1A3 between lung cancer and normal lung tissues, and ALDH1A3 was positively correlated with PPAR γ. AUC analysis found that PPAR γ and ALDH1A3 have good predictive value in the diagnosis and prognosis of lung cancer. GSEA enrichment analysis showed that PPAR γ and ALDH1A3 were significantly correlated with lipid oxidation. Combining relevant literature to demonstrate the inhibitory effect of PPAR γ receptors on lung cancer cells and the ability of PPAR γ activation to inhibit ALDH1A3 levels. Further in vitro CCK-8 and IC50 measurements of lung cancer cells A549 and H1299 were conducted, followed by non targeted lipidomics analysis. It was found that the metabolic pathways upregulated by activation of PPAR γ and inhibition of ALDH1A3 included glycerophospholipid metabolism, cholesterol metabolism, arachidonic acid metabolism, and fat digestion and absorption, with glycerophospholipid metabolism pathway accounting for the highest percentage. Conclusion: PPAR γ activation can inhibit the production of ALDH1A3, alter the glycerophospholipid metabolism pathway, and thus inhibit the proliferation of lung cancer cells. This study confirms that PPAR γ affects lung cancer proliferation by influencing the glycerophospholipid metabolism pathway.

22 Apr 2025·The Journal of Clinical Endocrinology & Metabolism

β-Cell Dedifferentiation in HOMA-βlow and HOMA-βhigh Subjects

Article

Author: Zhang, Zhuo ; Kang, Fuyun ; Zhang, Jun ; Sun, Jiajun ; Wang, Qidi ; Fu, Hui

AbstractContextβ-Cell dedifferentiation ratio is increased in type 2 diabetes; but its direct link to in vivo β-cell function in human remains unclear.ObjectiveThe present study was designed to investigate whether β-cell dedifferentiation in situ was closely associated with β-cell function in vivo and to identify targets crucial for β-cell dedifferentiation/function in human.MethodsWe acquired homeostasis model assessment of β-cell function (HOMA-β) values, calculated the number of hormone-negative endocrine cells, and evaluated important markers and novel candidates for β-cell dedifferentiation/function on paraneoplastic pancreatic tissues from 13 patients with benign pancreatic cystic neoplasm or intrapancreatic accessory spleen.ResultsBoth the β-cell dedifferentiation ratio and the dedifferentiation marker (Aldh1a3) were inversely related to in vivo β-cell function (HOMA-β) and in situ β-cell functional markers Glut2 and Ucn3 in humans. Moreover, the islets from HOMA-βlow subjects were manifested as (1) increased β-cell dedifferentiation ratio, (2) enriched dedifferentiation maker Aldh1a3, and (3) lower expression of Glut2 and Ucn3 compared with those from HOMA-βhigh subjects. We found that basic leucine zipper transcription factor 2 (Bach2) expression was significantly induced in islets from HOMA-βlow patients and was positively correlated with the ratio of β-cell dedifferentiation in humans.ConclusionOur findings emphasize the contribution of β-cell dedifferentiation to β-cell dysfunction in humans. Bach2 induction in β-cells with higher frequency of dedifferentiation observed in HOMA-βlow subjects reinforces its distinctive role as a pharmaceutical target of β-cell dedifferentiation for the treatment of people with diabetes.

04 Mar 2025·Ophthalmic Genetics

Two novel variants in ALDH1A3 associated with anophthalmia and congenital cystic eye

Article

Author: Parente Freixo, João ; Rodrigues, Rita ; Leal, Vítor ; Lemos, José Alberto ; Estrela-Silva, Sérgio ; Meira, Jorge ; Magalhães, Augusto ; Brandão, Ana Filipa

PURPOSEWe present the case of a newborn with right anophthalmia, left congenital cystic eye, and two novel variants in the ALDH1A3 gene. This report provides a comprehensive discussion of the clinical presentation, management strategies, and long-term follow-up for this rare condition.METHODSA thorough ophthalmic examination was performed. Genetic analysis employed next-generation sequencing targeting a panel of 50 genes implicated in microphthalmia, anophthalmia, and coloboma.RESULTSA one-day-old female, born to unrelated parents, was referred due to bilateral ocular malformations. Prenatal ultrasound in the third trimester had raised concerns about a congenital ocular developmental anomaly, and fetal magnetic resonance imaging suggested right anophthalmia and left eye aphakia. Postnatal examination revealed an empty right orbital cavity and a bluish lesion bulging from the left lower lid. Orbital imaging confirmed the bilateral absence of ocular structures and identified a cystic lesion in the left orbit. At three months of age, an orbital expander was placed in the right anophthalmic socket. At fifteen months, the left orbital cyst was excised due to rapid growth. Histopathological analysis revealed neuroglial tissue lining the cyst, consistent with a congenital cystic eye. A delay in psychomotor development has been noted, but no other signs of systemic conditions have been identified to date. Genetic testing identified two previously unreported ALDH1A3 variants: c.1036C>A (p.Pro346Thr) and c.981C>G (p.Tyr327*).CONCLUSIONOur study identifies two previously unreported variants in the ALDH1A3 gene, broadening the understanding of its phenotypic spectrum. We report the first association between ALDH1A3 variants and congenital cystic eye.

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ALDH1A3

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