A deletion of the gene encoding amino aldehyde dehydrogenase enhances the “pandan-like” aroma of winter melon (Benincasa hispida) and is a functional marker for the development of the aroma

ABSTRACT Encystment in Azotobacter vinelandii is induced byn-butanol or β-hydroxybutyrate (BHB). We identified a gene, encoding an aldehyde dehydrogenase, that was namedaldA. An aldA mutation impaired bacterial growth on n-butanol, ethanol, or hexanol as the sole carbon source. Expression of aldA increased in cells shifted from sucrose to n-butanol and was shown to be dependent on the alternative ς54 factor. A mutation in rpoNencoding the ς54 factor also impaired growth on alcohols. Encystment on n-butanol, but not on BHB, was impaired inaldA or rpoN mutants, indicating thatn-butanol is not an inducer of encystment by itself but must be catabolized in order to induce encystment.

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Expression of a Gene Encoding Mitochondrial Aldehyde Dehydrogenase in Rice Increases under Submerged Conditions

PLANT PHYSIOLOGY ◽

10.1104/pp.124.2.587 ◽

2000 ◽

Vol 124 (2) ◽

pp. 587-598 ◽

Cited By ~ 77

Author(s):

Mikio Nakazono ◽

Hiroyuki Tsuji ◽

Yuhua Li ◽

Daisuke Saisho ◽

Shin-ichi Arimura ◽

...

Keyword(s):

Aldehyde Dehydrogenase ◽

Gene Encoding ◽

Submerged Conditions

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Purification of an osmotin-like protein from the seeds of Benincasa hispida and cloning of the gene encoding this protein

Plant Science ◽

10.1016/s0168-9452(00)00450-7 ◽

2001 ◽

Vol 160 (5) ◽

pp. 817-826 ◽

Cited By ~ 23

Author(s):

Chao-Yun T. Shih ◽

Junlin Wu ◽

Shifang Jia ◽

Anwar A. Khan ◽

Kai-Li H. Ting ◽

...

Keyword(s):

Gene Encoding ◽

Benincasa Hispida

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Eliciting the Low-Activity Aldehyde Dehydrogenase Asian Phenotype by an Antisense Mechanism Results in an Aversion to Ethanol

Journal of Experimental Medicine ◽

10.1084/jem.194.5.571 ◽

2001 ◽

Vol 194 (5) ◽

pp. 571-580 ◽

Cited By ~ 22

Author(s):

Eric Garver ◽

Guang-chou Tu ◽

Qing-Na Cao ◽

Maria Aini ◽

Feng Zhou ◽

...

Keyword(s):

Aldehyde Dehydrogenase ◽

Antisense Oligonucleotide ◽

Mrna Levels ◽

Protective Effects ◽

Gene Encoding ◽

Osmotic Pumps ◽

Asian Populations ◽

Low Activity ◽

Antisense Effect ◽

Rat Hepatoma

A mutation in the gene encoding for the liver mitochondrial aldehyde dehydrogenase (ALDH2–2), present in some Asian populations, lowers or abolishes the activity of this enzyme and results in elevations in blood acetaldehyde upon ethanol consumption, a phenotype that greatly protects against alcohol abuse and alcoholism. We have determined whether the administration of antisense phosphorothioate oligonucleotides (ASOs) can mimic the low-activity ALDH2–2 Asian phenotype. Rat hepatoma cells incubated for 24 h with an antisense oligonucleotide (ASO-9) showed reductions in ALDH2 mRNA levels of 85% and ALDH2 (half-life of 22 h) activity of 55% equivalent to a >90% inhibition in ALDH2 synthesis. Glutamate dehydrogenase mRNA and activity remained unchanged. Base mismatches in the oligonucleotide rendered ASO-9 virtually inactive, confirming an antisense effect. Administration of ASO-9 (20 mg/kg/day for 4 d) to rats resulted in a 50% reduction in liver ALDH2 mRNA, a 40% inhibition in ALDH2 activity, and a fourfold (P < 0.001) increase in circulating plasma acetaldehyde levels after ethanol (1 g/kg) administration. Administration of ASO-9 to rats by osmotic pumps led to an aversion (−61%, P < 0.02) to ethanol. These studies provide a proof of principle that specific inhibition of gene expression can be used to mimic the protective effects afforded by the ALDH2–2 phenotype.

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Aldehyde dehydrogenase in fresh primordial germ cells as a marker of cell ‘stemness’

Zygote ◽

10.1017/s0967199418000631 ◽

2019 ◽

Vol 27 (1) ◽

pp. 46-48

Author(s):

Andrea Svoradová ◽

Jaromír Vašíček ◽

Alexander Ostró ◽

Peter Chrenek

Keyword(s):

Aldehyde Dehydrogenase ◽

Germ Cells ◽

Primordial Germ Cells ◽

Specific Inhibitor ◽

Cell Types ◽

Functional Marker ◽

Aldh Activity

SummaryChicken primordial germ cells (PGCs) are the primary pluripotent stem cell types that will differentiate towards germ cells. High aldehyde dehydrogenase (ALDH) activity is considered as a functional marker for the detection of cell ‘stemness’. In our study the ALDEFLUOR™ kit was used for determination of ALDH activity in PGCs. PGCs were co-stained with diethylaminobenzaldehyde (DEAB) and ALDH and analyzed by flow cytometry. Our results showed a small cell population (8.0 ± 3.3%) upon preincubation of the cells with the specific inhibitor DEAB, however cells without inhibitor staining showed a fluorescence shift as an ALDH-positive population (70.5 ± 1.6%). These findings indicate higher expression of ALDH in PGCs and ALDH activity can therefore be used as a new functional marker for the detection of cell ‘stemness’ in chicken PGCs. These results may have importance for characterization of PGCs as a potential genetic resource in poultry. Further research is necessary to elucidate the role of this functional marker in these cells.

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