St-Arnaud R, Prud'homme J, Leung-Hagesteijn C, Dedhar S
Genetics Unit, Shriners Hospital, Montréal, Québec, Canada.
J Cell Biol. 1995 Dec;131(5):1351-9. doi: 10.1083/jcb.131.5.1351.
Recent studies have shown that the multifunctional protein calreticulin can localize to the cell nucleus and regulate gene transcription via its ability to bind a protein motif in the DNA-binding domain of nuclear hormone receptors. A number of known modulators of bone cell function, including vitamin D, act through this receptor family, suggesting that calreticulin may regulate their action in bone cells. We have used a gain-of-function strategy to examine this putative role of calreticulin in MC3T3-E1 osteoblastic cells. Purified calreticulin inhibited the binding of the vitamin D receptor to characterized vitamin D response elements in gel retardation assays. This inhibition was due to direct protein-protein interactions between the vitamin D receptor and calreticulin. Expression of calreticulin transcripts declined during MC3T3-E1 osteoblastic differentiation. MC3T3-E1 cells were transfected with calreticulin expression vectors; stably transfected cell lines overexpressing recombinant calreticulin were established and assayed for vitamin D-induced gene expression and the capacity to mineralize. Constitutive calreticulin expression inhibited basal and vitamin D-induced expression of the osteocalcin gene, whereas osteopontin gene expression was unaffected. This pattern mimicked the gene expression pattern observed in parental cells before down-regulation of endogenous calreticulin expression. In long-term cultures of parental or vector-transfected cells, 1 alpha,25-dihydroxyvitamin D3 (1,25[OH]2D3) induced a two- to threefold stimulation of 45Ca accumulation into the matrix layer. Constitutive expression of calreticulin inhibited the 1,25(OH)2D3-induced 45Ca accumulation. This result correlated with the complete absence of mineralization nodules in long-term cultures of calreticulin-transfected cells. These data suggest that calreticulin can regulate bone cell function by interacting with specific nuclear hormone receptor-mediated pathways.
最近的研究表明,多功能蛋白钙网蛋白可定位于细胞核,并通过其与核激素受体DNA结合域中的蛋白质基序结合的能力来调节基因转录。许多已知的骨细胞功能调节剂,包括维生素D,都是通过这个受体家族发挥作用的,这表明钙网蛋白可能调节它们在骨细胞中的作用。我们采用功能获得策略来研究钙网蛋白在MC3T3-E1成骨细胞中的这一假定作用。在凝胶阻滞试验中,纯化的钙网蛋白抑制了维生素D受体与特征性维生素D反应元件的结合。这种抑制是由于维生素D受体与钙网蛋白之间直接的蛋白质-蛋白质相互作用。在MC3T3-E1成骨细胞分化过程中,钙网蛋白转录本的表达下降。用钙网蛋白表达载体转染MC3T3-E1细胞;建立稳定转染的过表达重组钙网蛋白的细胞系,并检测维生素D诱导的基因表达和矿化能力。组成型钙网蛋白表达抑制了骨钙素基因的基础表达和维生素D诱导的表达,而骨桥蛋白基因表达未受影响。这种模式与内源性钙网蛋白表达下调前在亲本细胞中观察到的基因表达模式相似。在亲本或载体转染细胞的长期培养中,1α,25-二羟基维生素D3(1,25[OH]2D3)诱导基质层中45Ca积累增加两到三倍。钙网蛋白组成型表达抑制了1,25(OH)2D3诱导的45Ca积累。这一结果与钙网蛋白转染细胞长期培养中完全没有矿化结节相关。这些数据表明,钙网蛋白可通过与特定的核激素受体介导的途径相互作用来调节骨细胞功能。