Uptake and metabolism of retinol in cultured Sertoli cells: evidence for a kinetic model

Bishop, Paul D.; Griswold, Michael D.

doi:10.1021/bi00397a046

Cited by 43 publications

(28 citation statements)

References 34 publications

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“…This is consistent with peroxisome proliferators possibly countering the effects of endogenous retinoids in primary Sertoli cells. Sertoli cells are known to store retinoids [40]. Considered together, these results clearly suggest that peroxisome proliferators disrupt the retinoid signaling pathway also in primary Sertoli cells.…”

Section: Effect Of Peroxisome Proliferators On the Transcriptional Acmentioning

confidence: 65%

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Peroxisome Proliferators Disrupt Retinoic Acid Receptor Alpha Signaling in the Testis1

Dufour

Bhattacharya

et al. 2003

Biology of Reproduction

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Peroxisome proliferators include a diverse group of chemicals, some of which have been demonstrated to be testicular toxicants. However, the mechanism by which peroxisome proliferators, such as phthalates, cause testicular damage is not clear. It is known that retinoic acid receptor alpha (RARalpha) and its retinoic acid ligand, the acid form of vitamin A, are required for spermatogenesis. It has been demonstrated that the absence of RARalpha gene or vitamin A in the animal leads to testis degeneration and sterility. Therefore, any compound that disrupts the action of vitamin A in the testis could potentially be damaging to male fertility. The current investigation examined a novel hypothesis that a mechanism of degeneration by peroxisome proliferators in the testis is due, in part, to disruption of the critical RARalpha signaling pathway. We show that peroxisome proliferators were able to disrupt the retinoic acid-induced nuclear localization of RARalpha and the retinoic acid-stimulated increase in transcriptional activity of a retinoic acid-responsive reporter gene in Sertoli cells. Concomitantly, peroxisome proliferators increased the nuclear localization of PPARalpha and the transcriptional activity of a peroxisome proliferator-responsive reporter gene in these cells. These results indicate that peroxisome proliferators can indeed shift the balance of nuclear localization for RARalpha and PPARalpha, resulting in deactivation of the critical RARalpha transcriptional activity in Sertoli cells.

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Section: Effect Of Peroxisome Proliferators On the Transcriptional Acmentioning

confidence: 65%

“…3). Although primary Sertoli cells are known to store retinoids [40], it was clear that extracellularly added tRA further increased the nuclear RAR␣ compared with that seen for vehicle-treated primary Sertoli cells (Fig. 3; compare C with A).…”

Section: Effect Of Peroxisome Proliferators On Rar␣ Subcellular Localmentioning

confidence: 87%

Peroxisome Proliferators Disrupt Retinoic Acid Receptor Alpha Signaling in the Testis1

Dufour

Bhattacharya

et al. 2003

Biology of Reproduction

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“…In many ways, the liver and Sertoli cells appear to function similarly in the uptake of retinol and the maintenance of large pools of this retinoid (35,43). However, it seems that spermatids and testicular and epididymal sperm also store retinoids (44).…”

Section: Ra Initiates Meiosis and May Generate The Cycle Of The Seminmentioning

confidence: 99%

The key role of vitamin A in spermatogenesis

Hogarth¹,

Griswold²

2010

J. Clin. Invest.

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221

180

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Spermatogenesis in adult mammals is highly organized, with the goal being continual sperm production. Vertebrate testes are arranged into recurring cellular associations that vary with time and distance along the tubule. These changes over time and distance are designated the cycle of the seminiferous epithelium and the spermatogenic wave, respectively. In this Review, we briefly outline the roles that follicle-stimulating hormone (FSH) and testosterone play in regulating spermatogenesis and describe our current understanding of how vitamin A regulates germ cell differentiation and how it may lead to the generation of both the cycle of the seminiferous epithelium and the spermatogenic wave.

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“…Based on measures made in rat liver and testis that show CRBP I is present at concentrations in excess of those of retinol, it is believed that all retinol present within these tissues is bound to CRBP I (HARRISON et al 1987;BISHOP and GRISWOLD 1987). It is generally accepted that CRBP I plays an important role in retinol metabolism (ONG et al 1994a).…”

Section: Cellular Retinol-binding Protein Type Imentioning

confidence: 99%

Biosynthesis, Absorption, Metabolism and Transport of Retinoids

Vogel¹,

Gamble²,

Blaner³

1999

Retinoids

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All retinoids (vitamin A and its analogs) in the body originate in the diet either as preformed vitamin A, usually from animal food sources, or as provitamin A carotenoids, usually from plant food sources or as supplements or additives to processed foods. Both preformed vitamin A and provitamin A undergo metabolism within the intestine (BLANER and OLSON 1994), including a series of metabolic conversions, extracellularly in the lumen of the intestine and intracellularly in the intestinal mucosa, which result in the preponderance of the dietary vitamin A being converted to retinol (vitamin A alcohol). The retinol, along with other dietary lipids in the intestinal mucosa, is packaged as retinyl ester in nascent chylomicrons. The chylomicrons are secreted into the lymphatic system, and approximately 75% of chylomicron retinoid is eventually taken up as part of the chylomicron remnants by the liver, where the majority of the body's retinoid reserves are stored. Some retinoid is delivered to extrahepatic tissues where this retinoid is either stored as retinyl ester, released back into the circulation for delivery to the liver and other tissues, metabolized to active retinoid forms such as retinoic acid or metabolized to catabolic forms destined for excretion from the body.The predominant retinoid present in the fasting circulation is the retinoic acid precursor, retinol. Since retinol is not soluble in aqueous environments, all circulating retinol is bound to retinol-binding protein (RBP). Other retinoids are also present in blood, albeit at much lower concentrations than retinol. Both all-trans-and 13-cis-retinoic acid can be found in fasting plasma of both animals and humans. Some retinyl ester is present as a component of lipoproteins, especially in very low density lipoprotein (VLDL) and low density lipoprotein (LDL). Glucuronides of both retinol and retinoic acid can be found in the circulation along with low levels of retro-metabolites of retinol.This chapter focuses primarily on recent advances in our understanding of the uptake and metabolism of dietary retinoid and provitamin A carotenoids, retinoid storage and metabolism in the liver and the delivery of retinoid to target tissues. Thus this review is concerned primarily with the metabolism and transport of the precursor retinol and its storage form, retinyl ester. Later chapters review the formation and catabolism of active retinoid forms such as retinoic acid and retro-retinoids from retinol.

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Uptake and metabolism of retinol in cultured Sertoli cells: evidence for a kinetic model

Cited by 43 publications

References 34 publications

Peroxisome Proliferators Disrupt Retinoic Acid Receptor Alpha Signaling in the Testis1

Peroxisome Proliferators Disrupt Retinoic Acid Receptor Alpha Signaling in the Testis1

The key role of vitamin A in spermatogenesis

Biosynthesis, Absorption, Metabolism and Transport of Retinoids

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