Introduction

CacyBP/SIP is a multifunctional protein present in various mammalian tissues, among them in brain. Recently, it has been shown that CacyBP/SIP exhibits phosphatase activity towards ERK1/2 and p38 kinases.

Objectives

The aim of our study was to analyze the localization and level of CacyBP/SIP and its substrates, phosphorylated ERK1/2 (p-ERK1/2) and phosphorylated p38 (p-p38) kinases, in an intact and transected rat spinal cord.

Methods

To achieve our goals we have performed Western blot/densitometric analysis and double immunofluorescence staining using rat spinal cord tissue, intact and after total transection at different time points.

Results

We have observed a decrease in the level of CacyBP/SIP and an increase in the level of p-ERK1/2 and of p-p38 in fragments of the spinal cord excised 1 and 3 months after transection. Moreover, immunofluorescence staining has shown that CacyBP/SIP, p-ERK1/2 or p-p38 co-localized with a neuronal marker, NeuN, and with an oligodendrocyte marker, Olig2.

Conclusion

The inverse correlation between CacyBP/SIP and p-ERK1/2 or p-p38 levels suggests that CacyBP/SIP may dephosphorylate p-ERK1/2 and p-p38 kinases and be involved in neural plasticity following spinal cord injury.

中文翻译：

---

正常和横断后大鼠脊髓中的 CacyBP/SIP - 对 ERK1/2 和 p38 激酶磷酸化状态的影响。

介绍

CacyBP/SIP 是一种多功能蛋白质，存在于各种哺乳动物组织中，其中包括大脑。最近，已经表明 CacyBP/SIP 对 ERK1/2 和 p38 激酶表现出磷酸酶活性。

目标

我们研究的目的是分析 CacyBP/SIP 及其底物、磷酸化 ERK1/2 (p-ERK1/2) 和磷酸化 p38 (p-p38) 激酶在完整和横断的大鼠脊髓中的定位和水平。

方法

为了实现我们的目标，我们使用完整的和在不同时间点完全横断后的大鼠脊髓组织进行了蛋白质印迹/光密度分析和双重免疫荧光染色。

结果

我们观察到在横断后 1 个月和 3 个月切除的脊髓碎片中 CacyBP/SIP 水平降低，p-ERK1/2 和 p-p38 水平增加。此外，免疫荧光染色显示 CacyBP/SIP、p-ERK1/2 或 p-p38 与神经元标记 NeuN 和少突胶质细胞标记 Olig2 共定位。

结论

CacyBP/SIP 和 p-ERK1/2 或 p-p38 水平之间的负相关表明 CacyBP/SIP 可能使 p-ERK1/2 和 p-p38 激酶去磷酸化，并参与脊髓损伤后的神经可塑性。