Department of Internal Medicine, The University of Texas Medical Branch at Galveston, Galveston, Texas 77555-1083, USA.
Am J Physiol Gastrointest Liver Physiol. 2011 Jan;300(1):G154-63. doi: 10.1152/ajpgi.00393.2010. Epub 2010 Nov 4.
Chronic stress elevates plasma norepinephrine, which enhances expression of the α(1C)-subunit of Ca(v)1.2b channels in colonic smooth muscle cells within 1 h. Transcriptional upregulation usually does not explain such rapid protein synthesis. We investigated whether chronic stress-induced release of norepinephrine utilizes posttranscriptional mechanisms to enhance the α(1C)-subunit. We performed experiments on colonic circular smooth muscle strips and in conscious rats, using a 9-day chronic intermittent stress protocol. Incubation of rat colonic muscularis externa with norepinephrine enhanced α(1C)-protein expression within 45 min, without a concomitant increase in α(1C) mRNA, indicating posttranscriptional regulation of α(1C)-protein by norepinephrine. We found that norepinephrine activates the PI3K/Akt/GSK-3β pathway to concurrently enhance α(1C)-protein translation and block its polyubiquitination and proteasomal degradation. Incubation of colonic muscularis externa with norepinephrine or LiCl, which inhibits GSK-3β, enhanced p-GSK-3β and α(1C)-protein time dependently. Using enrichment of phosphoproteins and ubiquitinated proteins, we found that both norepinephrine and LiCl decrease α(1C) phosphorylation and polyubiquitination. Concurrently, they suppress eIF2α (Ser51) phosphorylation and 4E-BP1 expression, which stimulates gene-specific translation. The antagonism of two upstream kinases, PI3K and Akt, inhibits the induction of α(1C)-protein by norepinephrine. Cyanopindolol (β(3)-AR-antagonist) almost completely suppresses and propranolol (β(1/2)-AR antagonist) partially suppresses norepinephrine-induced α(1C)-protein expression, whereas phentolamine and prazosin (α-AR and α(1)-AR antagonist, respectively) have no significant effect. Experiments in conscious animals showed that chronic stress activates the PI3K/Akt/GSK-3β signaling. We conclude that norepinephrine released by chronic stress rapidly enhances the protein expression of α(1C)-subunit of Ca(v)1.2b channels by concurrently suppressing its degradation and enhancing translation of existing transcripts to maintain homeostasis.
慢性应激会使血浆去甲肾上腺素升高,在 1 小时内增强结肠平滑肌细胞中 Ca(v)1.2b 通道的 α(1C)-亚基的表达。转录上调通常不能解释这种快速的蛋白质合成。我们研究了慢性应激诱导的去甲肾上腺素释放是否利用转录后机制来增强 α(1C)-亚基。我们使用 9 天慢性间歇性应激方案在结肠环形平滑肌条和清醒大鼠上进行了实验。用去甲肾上腺素孵育大鼠结肠外肌层可在 45 分钟内增强 α(1C)-蛋白表达,而 α(1C)mRNA 没有同时增加,表明去甲肾上腺素对 α(1C)-蛋白的转录后调节。我们发现去甲肾上腺素激活 PI3K/Akt/GSK-3β 途径,同时增强 α(1C)-蛋白翻译并阻止其多泛素化和蛋白酶体降解。用去甲肾上腺素或抑制 GSK-3β 的 LiCl 孵育结肠外肌层可使 p-GSK-3β 和 α(1C)-蛋白时间依赖性增加。通过富集磷酸化蛋白和泛素化蛋白,我们发现去甲肾上腺素和 LiCl 均降低 α(1C)的磷酸化和多泛素化。同时,它们抑制 eIF2α(Ser51)磷酸化和 4E-BP1 表达,从而刺激基因特异性翻译。两种上游激酶 PI3K 和 Akt 的拮抗作用抑制了去甲肾上腺素诱导的 α(1C)-蛋白的诱导。Cyanopindolol(β(3)-AR 拮抗剂)几乎完全抑制,普萘洛尔(β(1/2)-AR 拮抗剂)部分抑制去甲肾上腺素诱导的 α(1C)-蛋白表达,而酚妥拉明和哌唑嗪(α-AR 和 α(1)-AR 拮抗剂)则无显著影响。在清醒动物的实验中,慢性应激激活了 PI3K/Akt/GSK-3β 信号。我们得出结论,慢性应激释放的去甲肾上腺素通过同时抑制其降解和增强现有转录物的翻译来快速增强 Ca(v)1.2b 通道的 α(1C)-亚基的蛋白表达,以维持体内平衡。