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首页> 外文期刊>Biochemistry >Calcium-dependent stability studies of domains 1 and 2 of epithelial cadherin.
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Calcium-dependent stability studies of domains 1 and 2 of epithelial cadherin.

机译：钙依赖性上皮钙粘蛋白域1和2的稳定性研究。

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Epithelial cadherin is important in establishing and maintaining cell to cell interactions in epithelial cells, thereby playing an important role during morphogenesis. The epithelial cadherin molecules have three main regions: the N-terminal extracellular region, the transmembrane region that spans the cell membrane once, and the C-terminal cytoplasmic region that communicates with the cytoskeletal actin filaments through catenins. We report studies of the calcium-dependent stability of extracellular domains 1 and 2 of epithelial cadherin as a two-domain construct (MECAD12). Circular dichroism (CD) spectra of MECAD12 indicated a typical beta-sheet conformation in all solution conditions. Thermal- and denaturant-induced unfolding was monitored by CD. Distinct calcium stabilization was observed as a shift in T(m) from 40 (apo) to 65 degrees C (10 mM Ca(2+)). Spectroscopic experiments agreed well with calorimetric (DSC). In the absence of calcium, the unfolding transition was shallow (DeltaH(m) = 40 kcal/mol) but not obviously three state. Model-dependent analysis indicated that a second transition could be assigned to the unfolding of domain 2. A calcium-binding constant was derived from the calcium-dependent shift in temperature denaturation profiles. The K(d) that was obtained (55 muM) was consistent with literature values. Thus, the modular domains of epithelial cadherin exhibit context-dependent behavior in both the apo and calcium-bound states. This cooperativity between the modules is consistent with the physiological role of epithelial cadherin in signal transduction through cell-adhesive contacts.
机译：上皮钙粘蛋白在建立和维持上皮细胞中的细胞间相互作用中很重要，因此在形态发生中起重要作用。上皮钙粘蛋白分子具有三个主要区域：N末端细胞外区域，一次跨过细胞膜的跨膜区域和C末端细胞质区域，该区域通过连环蛋白与细胞骨架肌动蛋白丝连通。我们报告的钙依赖稳定性的细胞外域1和2的上皮钙粘蛋白作为两个域的构造（MECAD12）。 MECAD12的圆二色性（CD）光谱表明在所有溶液条件下均具有典型的β-折叠构象。通过CD监测热和变性剂诱导的展开。观察到不同的钙稳定度是T（m）从40（载脂蛋白）转变为65摄氏度（10 mM Ca（2+））。光谱实验与量热法（DSC）吻合得很好。在没有钙的情况下，展开转变是浅的（DeltaH（m）= 40 kcal / mol），但显然不是三态。依赖模型的分析表明，第二个跃迁可以分配给结构域2的折叠。钙结合常数源自温度变性曲线中钙依赖的变化。获得的K（d）（55μM）与文献值一致。因此，上皮钙粘蛋白的模块化结构域在载脂蛋白和钙结合状态下均表现出上下文相关的行为。模块之间的这种协同性与上皮钙粘蛋白在通过细胞粘附接触进行信号传导中的生理作用一致。

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