牛脑组织组织蛋白酶D对神经丝的降解作用

Neurofilament degradation by bovine brain cathepsin D.

作者信息

Suzuki H, Takeda M, Nakamura Y, Kato Y, Tada K, Hariguchi S, Nishimura T

机构信息

Department of Neuropsychiatry, Osaka University Medical School, Japan.

出版信息

Neurosci Lett. 1988 Jun 29;89(2):240-5. doi: 10.1016/0304-3940(88)90388-6.

DOI:10.1016/0304-3940(88)90388-6

PMID:3134625

Abstract

The effect of cathepsin D on bovine neurofilament protein was studied biochemically, immunologically, and morphologically. Degradation products of each neurofilament triplet by bovine brain cathepsin D at neutral pH were identified by electrophoresis and immunoblotting with anti-neurofilament antibodies. The 68-kDa subunit was the most susceptive to cathepsin D proteolysis among the triplet proteins. All of the triplet gave rise to partial degradates of the 50-kDa size. The reconstituted fiber from neurofilament triplet proteins and the 68-kDa subunit protein were attacked by cathepsin D and the mode of disruption of the fiber structure was studied by electronmicroscopy.

摘要

我们从生化、免疫和形态学角度研究了组织蛋白酶D对牛神经丝蛋白的作用。通过电泳和使用抗神经丝抗体进行免疫印迹，鉴定了牛脑组蛋白酶D在中性pH条件下对每个神经丝三联体的降解产物。在三联体蛋白中，68 kDa亚基对组织蛋白酶D的蛋白水解作用最为敏感。所有三联体都产生了50 kDa大小的部分降解产物。用神经丝三联体蛋白和68 kDa亚基蛋白重构的纤维受到组织蛋白酶D的攻击，并通过电子显微镜研究了纤维结构的破坏模式。