Molecular characterization, expression analysis, and role of ALDH3B1 in the cellular protection against oxidative stress

Marchitti, Satori A.; Brocker, Chad; Orlicky, David J.; Vasiliou, Vasilis

doi:10.1016/j.freeradbiomed.2010.08.004

Cited by 50 publications

(45 citation statements)

References 73 publications

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“…ALDH3B1 and ALDH3B3 may be responsible for removal of such oxidative stress-induced aldehydes in the plasma membrane. Consistent with this notion, ALDH3B1 protected cells from the cytotoxic, exogenously added aldehydes and oxidants [16].…”

Section: Discussionsupporting

confidence: 58%

“…ALDH3B1 is also expressed ubiquitously, and its protein levels are high in the kidney, liver, and ovary [15,16]. Similar to ALDH3A2, human ALDH3B1 exhibits activity toward medium-chain to long-chain aldehydes; in contrast to ALDH3A2, its subcellular localization is in the plasma membrane [17].…”

Section: Introductionmentioning

confidence: 99%

“…It follows that there is a clear distinction between the roles of ALDH3B1 and ALDH3A2: they act to detoxify aldehydes generated in the plasma membrane and the ER (and peroxisomes), respectively. Indeed, ALDH3B1 protects cells from the cytotoxicity of exogenously added aldehydes and oxidants [16]. We recently reported that human ALDH3B1 is dually lipidated (palmitoylation and prenylation) and that prenylation of ALDH3B1 is important for its plasma membrane localization and its activity toward long-chain aldehydes [17].…”

Section: Introductionmentioning

confidence: 99%

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Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via two C-terminal tryptophan residues and lipid modification

Kitamura

Takagi

Naganuma

et al. 2014

Biochemical Journal

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Short title: Lipid droplet localization of ALDH3B2Summary statement: The mouse aldehyde dehydrogenases ALDH3B2 and ALDH3B3 exhibit similar substrate specificity but distinct intracellular localization (ALDH3B2, lipid droplets; ALDH3B3, plasma membrane). The C-terminal prenylation and two Trp residues are important for the lipid droplet localization of ALDH3B2.2 ABSTRACT Aldehyde dehydrogenases (ALDHs) catalyze the conversion of toxic aldehydes to non-toxic carboxylic acids. Of the 21 ALDHs in mice, it is the ALDH3 family members (ALDH3A1, ALDH3A2, ALDH3B1, ALDH3B2, and ALDH3B3) that are responsible for the removal of lipid-derived aldehydes. However, ALDH3B2 and ALDH3B3 have yet to be characterized.Here, we examined the enzyme activity, tissue distribution, and subcellular localization of ALDH3B2 and ALDH3B3. Both were found to exhibit broad substrate preferences from medium-chain to long-chain aldehydes, resembling ALDH3A2 and ALDH3B1. Although ALDH3B2 and ALDH3B3 share extremely high sequence similarity, their localizations differed, with ALDH3B2 found in lipid droplets and ALDH3B3 localized to the plasma membrane. Both ALDH3B2 and ALDH3B3 were modified by prenylation at their C-termini; this modification greatly influenced their membrane localization and enzymatic activity toward hexadecanal. We found that their C-terminal regions, particularly the two Trp residues (Trp462 and Trp469) of ALDH3B2 and the two Arg residues (Arg462 and Arg463) of ALDH3B3, were important for the determination of their specific localization. Abnormal quantity and perhaps quality of lipid droplets are implicated in several metabolic diseases. We speculate that ALDH3B2 acts to remove lipid-derived aldehydes in lipid droplets generated via oxidative stress as a quality control mechanism.

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Section: Discussionsupporting

confidence: 58%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via two C-terminal tryptophan residues and lipid modification

Kitamura

Takagi

Naganuma

et al. 2014

Biochemical Journal

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“…ALDH3B1 is expressed in the kidney, liver, and brain and has been shown active in vitro toward C6 to C9 aldehydes [12]; however, its activity toward ≥C10 aldehydes is currently unknown. In addition, although ALDH3B1 is suggested to be localized in the plasma membrane and cytosol [13,14], the precise intracellular localization still remains to be elucidated. Unlike other ALDH3 family members, ALDH3B2 has so far not been well characterized.…”

Section: Introductionmentioning

confidence: 99%

Substrate specificity, plasma membrane localization, and lipid modification of the aldehyde dehydrogenase ALDH3B1

Kitamura

Naganuma

Abe

et al. 2013

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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The accumulation of reactive aldehydes is implicated in the development of several disorders. Aldehyde dehydrogenases (ALDHs) detoxify aldehydes by oxidizing them to the corresponding carboxylic acids. Among the 19 human ALDHs, ALDH3A2 is the only known ALDH that catalyzes the oxidation of long-chain fatty aldehydes including C16 aldehydes (hexadecanal and trans-2-hexadecenal) generated through sphingolipid metabolism. In the present study, we have identified that ALDH3B1 is also active in vitro toward C16 aldehydes and demonstrated that overexpression of ALDH3B1 restores the sphingolipid metabolism in the ALDH3A2-deficient cells. In addition, we have determined that ALDH3B1 is localized in the plasma membrane through its C-terminal dual lipidation (palmitoylation and prenylation) and shown that the prenylation is required particularly for the activity toward hexadecanal. Since knockdown of ALDH3B1 does not cause further impairment of the sphingolipid metabolism in the ALDH3A2-deficient cells, the likely physiological function of ALDH3B1 is to oxidize lipid-derived aldehydes generated in the plasma membrane and not to be involved in the sphingolipid metabolism in the endoplasmic reticulum.

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“…tive stress (35). CPT-cAMP also increases expression of pyruvate dehydrogenase 1 (Pdha1), glutamate dehydrogenase 1 (Glud1), and NAD ϩ -dependent malic acid enzyme (Me2), proteins providing substrates to the TCA cycle.…”

Section: Quantitative Proteomic Analysis Of Mitochondrial Proteins-mentioning

confidence: 99%

Proteomic and Metabolic Analyses of S49 Lymphoma Cells Reveal Novel Regulation of Mitochondria by cAMP and Protein Kinase A

Wilderman

Guo

Divakaruni

et al. 2015

Journal of Biological Chemistry

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Molecular characterization, expression analysis, and role of ALDH3B1 in the cellular protection against oxidative stress

Cited by 50 publications

References 73 publications

Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via two C-terminal tryptophan residues and lipid modification

Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via two C-terminal tryptophan residues and lipid modification

Substrate specificity, plasma membrane localization, and lipid modification of the aldehyde dehydrogenase ALDH3B1

Proteomic and Metabolic Analyses of S49 Lymphoma Cells Reveal Novel Regulation of Mitochondria by cAMP and Protein Kinase A

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