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9-Cis-Retinoic Acid

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Sheng-cai Lin – One of the best experts on this subject based on the ideXlab platform.

  • RXRα acts as a carrier for TR3 nuclear export in a 9-cis retinoic Acid-dependent manner in gastric cancer cells
    Journal of Cell Science, 2004
    Co-Authors: Xiao-feng Lin, Bi-xing Zhao, Hang-zhi Chen, Chao-yi Yang, Hai-ying Zhou, Ming-qing Zhang, Sheng-cai Lin
    Abstract:

    Retinoid X receptor (RXR) plays a crucial role in the cross talk between retinoid receptors and other hormone receptors including the orphan receptor TR3, forming different heterodimers that transduce diverse steroid/thyroid hormone signaling. Here we show that RXRα exhibits nucleocytoplasmic shuttling in MGC80-3 gastric cancer cells and that RXRα shuttling is energy-dependent through a nuclear pore complex (NPC)-mediated pathway for its import and an intact DNA binding domain-mediated pathway for its export. In the presence of its ligand 9-cis retinoic Acid, RXRα was almost exclusively located in the cytoplasm. More importantly, we also show that RXRα acts as a carrier to assist translocation of TR3, which plays an important role in apoptosis. Both RXRα and TR3 colocalized in the nucleus; however, upon stimulation by 9-cis retinoic Acid they cotranslocated to the cytoplasm and then localized in the mitochondria. TR3 export depends on RXRα, as in living cells GFP-TR3 alone did not result in export from the nucleus even in the presence of 9-cis retinoic Acid, whereas GFP-TR3 cotransfected with RXRα was exported out of the nucleus in response to 9-cis retinoic Acid. Moreover, specific reduction of RXRα levels caused by anti-sense RXRα abolished TR3 nuclear export. In contrast, specific knockdown of TR3 by antisense-TR3 or TR3-siRNA did not affect RXRα shuttling. These results indicate that RXRα is responsible for TR3 nucleocytoplasmic translocation, which is facilitated by the RXRα ligand 9-cis retinoic Acid. In addition, mitochondrial TR3, but not RXRα, was critical for apoptosis, as TR3 mutants that were distributed in the mitochondria induced apoptosis in the presence or absence of 9-cis retinoic Acid. These data reveal a novel aspect of RXRα function, in which it acts as a carrier for nucleocytoplasmic translocation of orphan receptors.

  • RXRalpha acts as a carrier for TR3 nuclear export in a 9-cis retinoic Acid-dependent manner in gastric cancer cells.
    Journal of cell science, 2004
    Co-Authors: Xiao-feng Lin, Bi-xing Zhao, Hang-zhi Chen, Chao-yi Yang, Hai-ying Zhou, Ming-qing Zhang, Sheng-cai Lin
    Abstract:

    Retinoid X receptor (RXR) plays a crucial role in the cross talk between retinoid receptors and other hormone receptors including the orphan receptor TR3, forming different heterodimers that transduce diverse steroid/thyroid hormone signaling. Here we show that RXRalpha exhibits nucleocytoplasmic shuttling in MGC80-3 gastric cancer cells and that RXRalpha shuttling is energy-dependent through a nuclear pore complex (NPC)-mediated pathway for its import and an intact DNA binding domain-mediated pathway for its export. In the presence of its ligand 9-cis retinoic Acid, RXRalpha was almost exclusively located in the cytoplasm. More importantly, we also show that RXRalpha acts as a carrier to assist translocation of TR3, which plays an important role in apoptosis. Both RXRalpha and TR3 colocalized in the nucleus; however, upon stimulation by 9-cis retinoic Acid they cotranslocated to the cytoplasm and then localized in the mitochondria. TR3 export depends on RXRalpha, as in living cells GFP-TR3 alone did not result in export from the nucleus even in the presence of 9-cis retinoic Acid, whereas GFP-TR3 cotransfected with RXRalpha was exported out of the nucleus in response to 9-cis retinoic Acid. Moreover, specific reduction of RXRalpha levels caused by anti-sense RXRalpha abolished TR3 nuclear export. In contrast, specific knockdown of TR3 by antisense-TR3 or TR3-siRNA did not affect RXRalpha shuttling. These results indicate that RXRalpha is responsible for TR3 nucleocytoplasmic translocation, which is facilitated by the RXRalpha ligand 9-cis retinoic Acid. In addition, mitochondrial TR3, but not RXRalpha, was critical for apoptosis, as TR3 mutants that were distributed in the mitochondria induced apoptosis in the presence or absence of 9-cis retinoic Acid. These data reveal a novel aspect of RXRalpha function, in which it acts as a carrier for nucleocytoplasmic translocation of orphan receptors.

Xiao-feng Lin – One of the best experts on this subject based on the ideXlab platform.

  • RXRα acts as a carrier for TR3 nuclear export in a 9-cis retinoic Acid-dependent manner in gastric cancer cells
    Journal of Cell Science, 2004
    Co-Authors: Xiao-feng Lin, Bi-xing Zhao, Hang-zhi Chen, Chao-yi Yang, Hai-ying Zhou, Ming-qing Zhang, Sheng-cai Lin
    Abstract:

    Retinoid X receptor (RXR) plays a crucial role in the cross talk between retinoid receptors and other hormone receptors including the orphan receptor TR3, forming different heterodimers that transduce diverse steroid/thyroid hormone signaling. Here we show that RXRα exhibits nucleocytoplasmic shuttling in MGC80-3 gastric cancer cells and that RXRα shuttling is energy-dependent through a nuclear pore complex (NPC)-mediated pathway for its import and an intact DNA binding domain-mediated pathway for its export. In the presence of its ligand 9-cis retinoic Acid, RXRα was almost exclusively located in the cytoplasm. More importantly, we also show that RXRα acts as a carrier to assist translocation of TR3, which plays an important role in apoptosis. Both RXRα and TR3 colocalized in the nucleus; however, upon stimulation by 9-cis retinoic Acid they cotranslocated to the cytoplasm and then localized in the mitochondria. TR3 export depends on RXRα, as in living cells GFP-TR3 alone did not result in export from the nucleus even in the presence of 9-cis retinoic Acid, whereas GFP-TR3 cotransfected with RXRα was exported out of the nucleus in response to 9-cis retinoic Acid. Moreover, specific reduction of RXRα levels caused by anti-sense RXRα abolished TR3 nuclear export. In contrast, specific knockdown of TR3 by antisense-TR3 or TR3-siRNA did not affect RXRα shuttling. These results indicate that RXRα is responsible for TR3 nucleocytoplasmic translocation, which is facilitated by the RXRα ligand 9-cis retinoic Acid. In addition, mitochondrial TR3, but not RXRα, was critical for apoptosis, as TR3 mutants that were distributed in the mitochondria induced apoptosis in the presence or absence of 9-cis retinoic Acid. These data reveal a novel aspect of RXRα function, in which it acts as a carrier for nucleocytoplasmic translocation of orphan receptors.

  • RXRalpha acts as a carrier for TR3 nuclear export in a 9-cis retinoic Acid-dependent manner in gastric cancer cells.
    Journal of cell science, 2004
    Co-Authors: Xiao-feng Lin, Bi-xing Zhao, Hang-zhi Chen, Chao-yi Yang, Hai-ying Zhou, Ming-qing Zhang, Sheng-cai Lin
    Abstract:

    Retinoid X receptor (RXR) plays a crucial role in the cross talk between retinoid receptors and other hormone receptors including the orphan receptor TR3, forming different heterodimers that transduce diverse steroid/thyroid hormone signaling. Here we show that RXRalpha exhibits nucleocytoplasmic shuttling in MGC80-3 gastric cancer cells and that RXRalpha shuttling is energy-dependent through a nuclear pore complex (NPC)-mediated pathway for its import and an intact DNA binding domain-mediated pathway for its export. In the presence of its ligand 9-cis retinoic Acid, RXRalpha was almost exclusively located in the cytoplasm. More importantly, we also show that RXRalpha acts as a carrier to assist translocation of TR3, which plays an important role in apoptosis. Both RXRalpha and TR3 colocalized in the nucleus; however, upon stimulation by 9-cis retinoic Acid they cotranslocated to the cytoplasm and then localized in the mitochondria. TR3 export depends on RXRalpha, as in living cells GFP-TR3 alone did not result in export from the nucleus even in the presence of 9-cis retinoic Acid, whereas GFP-TR3 cotransfected with RXRalpha was exported out of the nucleus in response to 9-cis retinoic Acid. Moreover, specific reduction of RXRalpha levels caused by anti-sense RXRalpha abolished TR3 nuclear export. In contrast, specific knockdown of TR3 by antisense-TR3 or TR3-siRNA did not affect RXRalpha shuttling. These results indicate that RXRalpha is responsible for TR3 nucleocytoplasmic translocation, which is facilitated by the RXRalpha ligand 9-cis retinoic Acid. In addition, mitochondrial TR3, but not RXRalpha, was critical for apoptosis, as TR3 mutants that were distributed in the mitochondria induced apoptosis in the presence or absence of 9-cis retinoic Acid. These data reveal a novel aspect of RXRalpha function, in which it acts as a carrier for nucleocytoplasmic translocation of orphan receptors.

Angel R. De Lera – One of the best experts on this subject based on the ideXlab platform.

  • New retinoid chemotypes: 9-Cis-Retinoic Acid analogs with hydrophobic rings derived from terpenes as selective RAR agonists.
    Bioorganic & medicinal chemistry, 2008
    Co-Authors: Susana Alvarez, Hinrich Gronemeyer, Yolanda Pazos-randulfe, Harshal Khanwalkar, Pierre Germain, Rosana Alvarez, Angel R. De Lera
    Abstract:

    Abstract A series of 9-Cis-Retinoic Acid analogs modified at the hydrophobic ring with a (bi)cyclohexenyl moiety derived from natural terpenes has been stereoselectively prepared using a Suzuki cross-coupling as key step. Transient transactivation studies indicate that modification of the hydrophobic ring impacts dramatically on RXR-binding and transactivation, with most retinoids being inactive on RXRβ, while preserving their RAR pan-agonist profile. Furthermore, only the RARγ subtype was capable of enantiomeric discrimination with some pairs of enantiomeric terpene-retinoids.

  • Stereoselective synthesis of 9-Cis-Retinoic Acid by suzuki reaction
    Tetrahedron Letters, 1999
    Co-Authors: Yolanda Pazos, Angel R. De Lera
    Abstract:

    Abstract The entire polyenic side chain of ethyl 9- cis -retinoate (7) has been stereoselectively synthesized and attached to the hydrophobic ring by a high-yielding thallium-accelerated Suzuki cross-coupling reaction. The Suzuki reaction partners, tetraenyl iodide 18 and alkenyl organoborane 19. are more conveniently used immediately after generation from their precursors. Alternative approaches using either the Stille reaction or a Suzuki reaction with a shorter polyenic component proved less efficient. The highly convergent sequence can be adapted to the preparation of analogs of 9- cis -retinoic Acid (2), the natural ligand for the retinoid X (RXR) subfamily of nuclear receptors.

Chao-yi Yang – One of the best experts on this subject based on the ideXlab platform.

  • RXRα acts as a carrier for TR3 nuclear export in a 9-cis retinoic Acid-dependent manner in gastric cancer cells
    Journal of Cell Science, 2004
    Co-Authors: Xiao-feng Lin, Bi-xing Zhao, Hang-zhi Chen, Chao-yi Yang, Hai-ying Zhou, Ming-qing Zhang, Sheng-cai Lin
    Abstract:

    Retinoid X receptor (RXR) plays a crucial role in the cross talk between retinoid receptors and other hormone receptors including the orphan receptor TR3, forming different heterodimers that transduce diverse steroid/thyroid hormone signaling. Here we show that RXRα exhibits nucleocytoplasmic shuttling in MGC80-3 gastric cancer cells and that RXRα shuttling is energy-dependent through a nuclear pore complex (NPC)-mediated pathway for its import and an intact DNA binding domain-mediated pathway for its export. In the presence of its ligand 9-cis retinoic Acid, RXRα was almost exclusively located in the cytoplasm. More importantly, we also show that RXRα acts as a carrier to assist translocation of TR3, which plays an important role in apoptosis. Both RXRα and TR3 colocalized in the nucleus; however, upon stimulation by 9-cis retinoic Acid they cotranslocated to the cytoplasm and then localized in the mitochondria. TR3 export depends on RXRα, as in living cells GFP-TR3 alone did not result in export from the nucleus even in the presence of 9-cis retinoic Acid, whereas GFP-TR3 cotransfected with RXRα was exported out of the nucleus in response to 9-cis retinoic Acid. Moreover, specific reduction of RXRα levels caused by anti-sense RXRα abolished TR3 nuclear export. In contrast, specific knockdown of TR3 by antisense-TR3 or TR3-siRNA did not affect RXRα shuttling. These results indicate that RXRα is responsible for TR3 nucleocytoplasmic translocation, which is facilitated by the RXRα ligand 9-cis retinoic Acid. In addition, mitochondrial TR3, but not RXRα, was critical for apoptosis, as TR3 mutants that were distributed in the mitochondria induced apoptosis in the presence or absence of 9-cis retinoic Acid. These data reveal a novel aspect of RXRα function, in which it acts as a carrier for nucleocytoplasmic translocation of orphan receptors.

  • RXRalpha acts as a carrier for TR3 nuclear export in a 9-cis retinoic Acid-dependent manner in gastric cancer cells.
    Journal of cell science, 2004
    Co-Authors: Xiao-feng Lin, Bi-xing Zhao, Hang-zhi Chen, Chao-yi Yang, Hai-ying Zhou, Ming-qing Zhang, Sheng-cai Lin
    Abstract:

    Retinoid X receptor (RXR) plays a crucial role in the cross talk between retinoid receptors and other hormone receptors including the orphan receptor TR3, forming different heterodimers that transduce diverse steroid/thyroid hormone signaling. Here we show that RXRalpha exhibits nucleocytoplasmic shuttling in MGC80-3 gastric cancer cells and that RXRalpha shuttling is energy-dependent through a nuclear pore complex (NPC)-mediated pathway for its import and an intact DNA binding domain-mediated pathway for its export. In the presence of its ligand 9-cis retinoic Acid, RXRalpha was almost exclusively located in the cytoplasm. More importantly, we also show that RXRalpha acts as a carrier to assist translocation of TR3, which plays an important role in apoptosis. Both RXRalpha and TR3 colocalized in the nucleus; however, upon stimulation by 9-cis retinoic Acid they cotranslocated to the cytoplasm and then localized in the mitochondria. TR3 export depends on RXRalpha, as in living cells GFP-TR3 alone did not result in export from the nucleus even in the presence of 9-cis retinoic Acid, whereas GFP-TR3 cotransfected with RXRalpha was exported out of the nucleus in response to 9-cis retinoic Acid. Moreover, specific reduction of RXRalpha levels caused by anti-sense RXRalpha abolished TR3 nuclear export. In contrast, specific knockdown of TR3 by antisense-TR3 or TR3-siRNA did not affect RXRalpha shuttling. These results indicate that RXRalpha is responsible for TR3 nucleocytoplasmic translocation, which is facilitated by the RXRalpha ligand 9-cis retinoic Acid. In addition, mitochondrial TR3, but not RXRalpha, was critical for apoptosis, as TR3 mutants that were distributed in the mitochondria induced apoptosis in the presence or absence of 9-cis retinoic Acid. These data reveal a novel aspect of RXRalpha function, in which it acts as a carrier for nucleocytoplasmic translocation of orphan receptors.

Hang-zhi Chen – One of the best experts on this subject based on the ideXlab platform.

  • RXRα acts as a carrier for TR3 nuclear export in a 9-cis retinoic Acid-dependent manner in gastric cancer cells
    Journal of Cell Science, 2004
    Co-Authors: Xiao-feng Lin, Bi-xing Zhao, Hang-zhi Chen, Chao-yi Yang, Hai-ying Zhou, Ming-qing Zhang, Sheng-cai Lin
    Abstract:

    Retinoid X receptor (RXR) plays a crucial role in the cross talk between retinoid receptors and other hormone receptors including the orphan receptor TR3, forming different heterodimers that transduce diverse steroid/thyroid hormone signaling. Here we show that RXRα exhibits nucleocytoplasmic shuttling in MGC80-3 gastric cancer cells and that RXRα shuttling is energy-dependent through a nuclear pore complex (NPC)-mediated pathway for its import and an intact DNA binding domain-mediated pathway for its export. In the presence of its ligand 9-cis retinoic Acid, RXRα was almost exclusively located in the cytoplasm. More importantly, we also show that RXRα acts as a carrier to assist translocation of TR3, which plays an important role in apoptosis. Both RXRα and TR3 colocalized in the nucleus; however, upon stimulation by 9-cis retinoic Acid they cotranslocated to the cytoplasm and then localized in the mitochondria. TR3 export depends on RXRα, as in living cells GFP-TR3 alone did not result in export from the nucleus even in the presence of 9-cis retinoic Acid, whereas GFP-TR3 cotransfected with RXRα was exported out of the nucleus in response to 9-cis retinoic Acid. Moreover, specific reduction of RXRα levels caused by anti-sense RXRα abolished TR3 nuclear export. In contrast, specific knockdown of TR3 by antisense-TR3 or TR3-siRNA did not affect RXRα shuttling. These results indicate that RXRα is responsible for TR3 nucleocytoplasmic translocation, which is facilitated by the RXRα ligand 9-cis retinoic Acid. In addition, mitochondrial TR3, but not RXRα, was critical for apoptosis, as TR3 mutants that were distributed in the mitochondria induced apoptosis in the presence or absence of 9-cis retinoic Acid. These data reveal a novel aspect of RXRα function, in which it acts as a carrier for nucleocytoplasmic translocation of orphan receptors.

  • RXRalpha acts as a carrier for TR3 nuclear export in a 9-cis retinoic Acid-dependent manner in gastric cancer cells.
    Journal of cell science, 2004
    Co-Authors: Xiao-feng Lin, Bi-xing Zhao, Hang-zhi Chen, Chao-yi Yang, Hai-ying Zhou, Ming-qing Zhang, Sheng-cai Lin
    Abstract:

    Retinoid X receptor (RXR) plays a crucial role in the cross talk between retinoid receptors and other hormone receptors including the orphan receptor TR3, forming different heterodimers that transduce diverse steroid/thyroid hormone signaling. Here we show that RXRalpha exhibits nucleocytoplasmic shuttling in MGC80-3 gastric cancer cells and that RXRalpha shuttling is energy-dependent through a nuclear pore complex (NPC)-mediated pathway for its import and an intact DNA binding domain-mediated pathway for its export. In the presence of its ligand 9-cis retinoic Acid, RXRalpha was almost exclusively located in the cytoplasm. More importantly, we also show that RXRalpha acts as a carrier to assist translocation of TR3, which plays an important role in apoptosis. Both RXRalpha and TR3 colocalized in the nucleus; however, upon stimulation by 9-cis retinoic Acid they cotranslocated to the cytoplasm and then localized in the mitochondria. TR3 export depends on RXRalpha, as in living cells GFP-TR3 alone did not result in export from the nucleus even in the presence of 9-cis retinoic Acid, whereas GFP-TR3 cotransfected with RXRalpha was exported out of the nucleus in response to 9-cis retinoic Acid. Moreover, specific reduction of RXRalpha levels caused by anti-sense RXRalpha abolished TR3 nuclear export. In contrast, specific knockdown of TR3 by antisense-TR3 or TR3-siRNA did not affect RXRalpha shuttling. These results indicate that RXRalpha is responsible for TR3 nucleocytoplasmic translocation, which is facilitated by the RXRalpha ligand 9-cis retinoic Acid. In addition, mitochondrial TR3, but not RXRalpha, was critical for apoptosis, as TR3 mutants that were distributed in the mitochondria induced apoptosis in the presence or absence of 9-cis retinoic Acid. These data reveal a novel aspect of RXRalpha function, in which it acts as a carrier for nucleocytoplasmic translocation of orphan receptors.