A New Pathway for Vitamin A

Levin, Arthur A.; Sturzenbecker, Laurie J.; Kazmer, Sonja; Bosakowski, Thomas; Huselton, Christine; Allenby, Gary; Speck, J; Kratzeisen, C; Rosenberger, Michael; Lovey, Allen; Grippo, Joseph F.

doi:10.1111/j.1749-6632.1992.tb17090.x

Cited by 46 publications

(50 citation statements)

References 46 publications

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“…A consequence of this metabolic scheme would be that generation of the two isomers of RA is carried out by two independent pathways, each of which may be under separate metabolic control. This provides an alternative to the view where all-trans RA is believed to be the precursor in 9-cis RA biosynthesis (8,33).…”

Section: Discussionmentioning

confidence: 99%

The identification of a 9- cis retinol dehydrogenase in the mouse embryo reveals a pathway for synthesis of 9- cis retinoic acid

Romert

Tuvendal

Simon

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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The ligand-controlled retinoic acid (RA) receptors and retinoid X receptors are important for several physiological processes, including normal embryonic development, but little is known about how their ligands, all-trans and 9-cis RA, are generated. Here we report the identification of a stereo-specific 9-cis retinol dehydrogenase, which is abundantly expressed in embryonic tissues known to be targets in the retinoid signaling pathway. The membranebound enzyme is a member of the short-chain alcohol dehydrogenase͞reductase superfamily, able to oxidize 9-cis retinol into 9-cis retinaldehyde, an intermediate in 9-cis RA biosynthesis. Analysis by nonradioactive in situ hybridization in mouse embryos shows that expression of the enzyme is temporally and spatially well controlled during embryogenesis with prominent expression in parts of the developing central nervous system, sensory organs, somites and myotomes, and several tissues of endodermal origin. The identification of this enzyme reveals a pathway in RA biosynthesis, where 9-cis retinol is generated for subsequent oxidation to 9-cis RA.

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Section: Discussionmentioning

confidence: 99%

The identification of a 9- cis retinol dehydrogenase in the mouse embryo reveals a pathway for synthesis of 9- cis retinoic acid

Romert

Tuvendal

Simon

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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“…Similar to the RARs, three forms of RXR have been identi®ed (RXR-a, RXR-b and RXR-g). 9-cis RA, an isomer of all-trans RA, has been reported to be a natural ligand for RXR (Heyman et al, 1992;Levin et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Modulation of retinoic acid receptor function alters the growth inhibitory response of oral SCC cells to retinoids

Dawson

Soprano

et al. 2000

Oncogene

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“…It can bind to a subset of retinoic acid receptors known as RXR receptors, as well as binding to RAR receptors [1][2][3]. The biological activity of 9-cis-retinoic acid is presumed to be distinct from that of the well-described alt-trans-retinoic acid [4][5][6].…”

Section: Introduction 2 Experimentalmentioning

confidence: 99%

“…Recent studies have identified 9-cis-retinoic acid as a novel hormone which may be important in mammalian development [1][2][3]. It can bind to a subset of retinoic acid receptors known as RXR receptors, as well as binding to RAR receptors [1][2][3].…”

Section: Introduction 2 Experimentalmentioning

confidence: 99%

Thiol dependent isomerization of all‐trans‐retinoic acid to 9‐cis‐retinoic acid

Urbach

Rando

1994

FEBS Letters

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The important biological effector 9-cis-retinoic acid can be generated by liver microsomes or by bovine serum albumin in detergent. The mechanism of this isomerization reaction is the subject of these studies. The protein mediated isomerization process is shown to be thiol-and pH-dependent. Moreover, the retinoic acids are also isomerized by 1-dodecanethiol in the presence of detergents. This isomerization process is pH-dependent as well, with isomerization rates increasing with pH. The isomerization reactions are quenched with free radical traps, such as ~-tocopherol and ascorbic acid, suggesting that a thiol radical mechanism, rather than a thiolate anion-dependent mechanism, is implicated here. The pH dependence can be understood in terms of a thiol radical mechanism, because thiol radicals are produced from thiolate anions in the presence of oxygen. The facile thiol-mediated isomerization of the retinoic acids suggests that this could be a physiologically relevant mechanism for the formation of 9-cis-retinoic acid from all-trans-retinoic acid.

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A New Pathway for Vitamin A

Cited by 46 publications

References 46 publications

The identification of a 9- cis retinol dehydrogenase in the mouse embryo reveals a pathway for synthesis of 9- cis retinoic acid

The identification of a 9- cis retinol dehydrogenase in the mouse embryo reveals a pathway for synthesis of 9- cis retinoic acid

Modulation of retinoic acid receptor function alters the growth inhibitory response of oral SCC cells to retinoids

Thiol dependent isomerization of all‐trans‐retinoic acid to 9‐cis‐retinoic acid

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