Gschwend T P, Krueger S R, Kozlov S V, Wolfer D P, Sonderegger P
Institute of Biochemistry, University of Zürich, Switzerland.
Mol Cell Neurosci. 1997;9(3):207-19. doi: 10.1006/mcne.1997.0616.
We have cloned a novel murine cDNA encoding a multidomain serine protease, termed neurotrypsin, which exhibits an unprecedented domain composition. The deduced amino acid sequence defines a mosaic protein of 761 amino acids consisting of a kringle domain, followed by three scavenger receptor cysteine-rich repeats, and a serine protease domain. Based on comparisons of the primary structure, the protease domain belongs to the subfamily of trypsin-like serine proteases. In situ hybridization revealed that the expression of neurotrypsin in the adult murine nervous system is confined to distinct subsets of neurons. The most prominent expression was found in the cerebral cortex, the hippocampus, and the amygdala. Le., structures engaged in the processing and storage of learned behaviors and memories. Together with the recently obtained evidence that extracellular serine proteases play a role in neural plasticity, this expression pattern suggests that the extracellular proteolytic action of neurotrypsin subserves structural reorganizations associated with learning and memory operations.
我们克隆了一种编码多结构域丝氨酸蛋白酶的新型小鼠cDNA，该蛋白酶被称为神经胰蛋白酶，其结构域组成前所未见。推导的氨基酸序列定义了一个由761个氨基酸组成的镶嵌蛋白，该蛋白由一个kringle结构域、三个富含半胱氨酸的清道夫受体重复序列和一个丝氨酸蛋白酶结构域组成。基于一级结构的比较，该蛋白酶结构域属于类胰蛋白酶样丝氨酸蛋白酶亚家族。原位杂交显示，神经胰蛋白酶在成年小鼠神经系统中的表达局限于不同的神经元亚群。最显著的表达出现在大脑皮层、海马体和杏仁核中。即参与学习行为和记忆的处理与存储的结构。连同最近获得的细胞外丝氨酸蛋白酶在神经可塑性中起作用的证据，这种表达模式表明神经胰蛋白酶的细胞外蛋白水解作用有助于与学习和记忆操作相关的结构重组。
