LEUKOCYTE GELATINASE-B CLEAVAGE RELEASES ENCEPHALITOGENS FROM HUMAN MYELIN BASIC-PROTEIN
LEUKOCYTE GELATINASE-B CLEAVAGE RELEASES ENCEPHALITOGENS FROM HUMAN MYELIN BASIC-PROTEIN
复制标题
DOI：
10.1006/bbrc.1993.1540
复制
发表时间：
1993-05-14
影响因子：
3.1
通讯作者：
OPDENAKKER, G
中科院分区：
文献类型：
--
作者：
PROOST, P;VANDAMME, J;OPDENAKKER, G
明胶酶B是类风湿性关节炎和多发性硬化症等慢性炎症性疾病的标志酶，可裂解人髓鞘碱性蛋白（MBP）。用明胶酶B从白细胞中消化人MBP。通过RP-HPLC分离MBP肽段，并通过氨基末端序列分析确定明胶酶B切割位点。发现了几个新的明胶酶B的P1-P1′切割位点，在人MBP中，切割位点的位置至少有一个肽段与已知的主要MBP自身抗原相一致。这项研究诠释了人MBP作为人明胶酶B的底物，确定了新的P1-P′ 1切割位点，并将其中一种金属蛋白酶确定为脱髓鞘疾病（如MS）发病机制中的可能环节。
Gelatinase B, a marker enzyme for chronic inflammatory diseases such as rheumatoid arthritis and multiple sclerosis (MS), was found to cleave human myelin basic protein (MBP). Human MBP was digested with gelatinase B from leukocytes. The MBP peptide fragments were separated by RP-HPLC and the gelatinase B cleavage sites established by aminoterminal sequence analysis. Several novel P1-P1′ cleavage sites for gelatinase B were found. The positions of the cleavage sites in human MBP were such that at least one peptide coincided with a documented major MBP-autoantigen. This study annotates human MBP as a substrate for human gelatinase B, determines novel P1-P′1cleavage sites and defines one of the metalloproteinases as a possible link in the pathogenesis of demyelinating diseases such as MS.