Takasugi H, Mori M, Chikuma T, Kato T
Laboratory of Molecular Recognition, Graduate School of Integrated Science, Yokohama City University, Japan.
Neurochem Int. 1996 Oct;29(4):397-403. doi: 10.1016/0197-0186(95)00165-4.
Since peptidylglycine alpha-amidating monooxygenase (PAM) and carboxypeptidase H (CPH) are transported by a rapid anterograde axonal flow in rat sciatic nerves, different properties of those enzymes were examined in the cell body (dorsal root ganglia) and axon (sciatic nerves) of rat. The relative enzyme activities of soluble to membrane-associated forms in the sciatic nerves were higher than those in the ganglia. On a gel permeation chromatogram, 3 peaks (100, 70 and 30 kDa) of PAM activity appeared in both tissues. There are main peaks at 70 kDa in the ganglia and at 30 kDa in the sciatic nerves. From these data, we suppose that PAM in rat sciatic nerves is proteolytically processed during the axonal transport of secretion granules.
由于肽基甘氨酸α-酰胺化单加氧酶(PAM)和羧肽酶H(CPH)在大鼠坐骨神经中通过快速的顺行轴突运输进行转运,因此我们研究了这些酶在大鼠的细胞体(背根神经节)和轴突(坐骨神经)中的不同特性。坐骨神经中可溶性形式与膜相关形式的相对酶活性高于神经节中的相对酶活性。在凝胶渗透色谱图上,两种组织中均出现了3个PAM活性峰(100、70和30 kDa)。神经节中主要峰位于70 kDa,坐骨神经中主要峰位于30 kDa。根据这些数据,我们推测大鼠坐骨神经中的PAM在分泌颗粒的轴突运输过程中经过了蛋白水解加工。