LePage R N, Fosang A J, Fuller S J, Murphy G, Evin G, Beyreuther K, Masters C L, Small D H
Laboratory of Molecular Neurobiology, University of Melbourne, Parkville, Vic., Australia.
FEBS Lett. 1995 Dec 18;377(2):267-70. doi: 10.1016/0014-5793(95)01358-x.
The ability of the 72 kDa gelatinase A to cleave the amyloid protein precursor (APP) was investigated. HeLa cells were transfected with an APP695 plasmid. The cells were incubated with gelatinase A, which cleaved the 110 kDa cell-surface APP, releasing a 100 kDa form of the protein. A peptide homologous to the beta-secretase site was cleaved by gelatinase A adjacent to a glutamate residue at position -3 (beta A4 numbering system). A peptide homologous to the alpha-secretase site was not cleaved. The results demonstrate that 72 kDa gelatinase A is not an alpha-secretase, but that it may have a beta-secretase activity.
研究了72 kDa明胶酶A切割淀粉样蛋白前体（APP）的能力。用APP695质粒转染HeLa细胞。将细胞与明胶酶A一起孵育，明胶酶A切割110 kDa的细胞表面APP，释放出100 kDa形式的蛋白质。与β-分泌酶位点同源的肽在-3位谷氨酸残基（βA4编号系统）相邻处被明胶酶A切割。与α-分泌酶位点同源的肽未被切割。结果表明，72 kDa明胶酶A不是α-分泌酶，但可能具有β-分泌酶活性。
