Transfer of retinoic acid from its complex with cellular retinoic acid-binding protein to the nucleus.
Transfer of retinoic acid from its complex with cellular retinoic acid-binding protein to the nucleus.
复制标题
将视黄酸从其与细胞视黄酸结合蛋白的复合物转移至细胞核。
DOI：
10.1016/0003-9861(86)90591-6
复制
发表时间：
1986
影响因子：
3.9
通讯作者：
Chytil,F
中科院分区：
文献类型：
--
作者：
Takase,S;Ong,DE;Chytil,F
细胞视黄酸结合蛋白（CRABP），视黄酸作用的潜在介质，使视黄酸以特定的方式结合细胞核和染色质分离的控制和维生素A缺乏大鼠的睾丸。[~ 3 H]维甲酸与从大鼠睾丸中纯化的CRABP络合后，维甲酸的结合。结合是特异性的、可饱和的和温度依赖性的。如果CRABP充电与未标记的视黄酸包括在孵育中，结合的放射性减少，而列入游离视黄酸，或复合物的视黄醇与细胞视黄醇结合蛋白（CRBP）或血清视黄醇结合蛋白没有影响。在缺失动物的每个细胞核中检测到约4.0 × 104个维甲酸特异性结合位点。观察到的结合位点的数量受到维生素A状态的影响。再喂维生素A缺乏大鼠（4小时）与视黄酸降低的数量可检测的结合位点的核。CRABP本身并没有保持绑定到这些网站，表明视黄酸从其复杂的CRABP转移到核网站。此外，CRBP，视黄醇作用的假定介质，被发现能够使视黄醇结合到睾丸细胞核，在类似于先前描述的视黄醇结合到肝细胞核的相互作用。
Cellular retinoic acid-binding protein (CRABP), a potential mediator of retinoic acid action, enables retinoic acid to bind in a specific manner to nuclei and chromatin isolated from testes of control and vitamin A-deficient rats. The binding of retinoic acid was followed after complexing [3H]retinoic acid with CRABP purified from rat testes. The binding was specific, saturable, and temperature dependent. If CRABP charged with nonlabeled retinoic acid was included in the incubation, binding of radioactivity was diminished, whereas inclusion of free retinoic acid, or the complex of retinol with cellular retinol binding protein (CRBP) or serum retinol binding protein had no effect. Approximately 4.0 × 104specific binding sites for retinoic acid were detected per nucleus from deficient animals. The number of binding sites observed was influenced by vitamin A status. Refeeding vitamin A-deficient rats (4 h) with retinoic acid lowered the amount of detectable binding sites in the nucleus. CRABP itself did not remain bound to these sites, indicating a transfer of retinoic acid from its complex with CRABP to the nuclear sites. Further, CRBP, the putative mediator of retinol action, was found to enable retinol to be bound to testicular nuclei, in an interaction similar to the binding of retinol to liver nuclei described previously.