Is PPARbeta/delta a Retinoid Receptor?
Is PPARbeta/delta a Retinoid Receptor?
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作者：
Berry DC;Noy N
PPAR广泛的配体结合特性长期以来阻碍了对该受体有生理意义的配体的鉴定。观察到PPAR的活性由脂肪酸结合蛋白5 （FABP5）支持，它直接将配体从细胞质溶胶传递到受体，这表明真正的PPAR配体既激活受体，又触发FABP5的核易位。利用这些标准，最近证明了全反式维甲酸（RA），经典维甲酸受体RAR的激活剂，也可作为PPAR的配体。研究发现，RA在两个受体之间的分配受FABP5和细胞RA结合蛋白II （CRABP-II）的调控，前者将RA传递到PPAR，后者将RA靶向到RAR。因此，RA在FABP5/CRABP-II高表达比例的细胞中激活PPAR。目前还不清楚RA以外的化合物是否也可以作为这种高度混杂蛋白的内源性激活剂。
The broad ligand-binding characteristic of PPAR has long hampered identification of physiologically-meaningful ligands for the receptor. The observations that the activity of PPAR is supported by fatty acid binding protein 5 (FABP5), which directly delivers ligands from the cytosol to the receptor, suggest that bona fide PPAR ligands both activate the receptor, and trigger the nuclear translocation of FABP5. Using these criteria, it was recently demonstrated that all-trans-retinoic acid (RA), the activator of the classical retinoic acid receptor RAR, also serves as a ligand for PPAR. Partitioning of RA between its two receptors was found to be regulated by FABP5, which delivers it to PPAR, and cellular RA binding protein II (CRABP-II), which targets it to RAR. Consequently, RA activates PPAR in cells that display a high FABP5/CRABP-II expression ratio. It remains to be clarified whether compounds other than RA may also serve as endogenous activators for this highly promiscuous protein.
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影响因子：
4.1
作者：
Gutiérrez-González, LH;Ludwig, C;Lücke, C
通讯作者：
Lücke, C
影响因子：
11.2
作者：
Donato, Leslie J.;Suh, Jean H.;Noy, Noa
通讯作者：
Noy, Noa
影响因子：
4.8
作者：
Dong, D;Ruuska, SE;Noy, N
通讯作者：
Noy, N
影响因子：
8
作者：
Le, Q;Dawson, MI;Soprano, KJ
通讯作者：
Soprano, KJ
影响因子：
4.8
作者：
Kersten, S;Mandard, S;Wahli, W
通讯作者：
Wahli, W