CAP 37, a 37 kD human neutrophil granule cationic protein shares homology with inflammatory proteinases.
CAP 37, a 37 kD human neutrophil granule cationic protein shares homology with inflammatory proteinases.
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CAP 37 是一种 37 kD 的人中性粒细胞颗粒阳离子蛋白，与炎症蛋白酶具有同源性。
DOI：
10.1016/0024-3205(90)90104-y
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发表时间：
1990
期刊：
影响因子：
6.1
通讯作者：
Larrick,JW
中科院分区：
文献类型：
--
作者：
Pereira,HA;Spitznagel,JK;Pohl,J;Wilson,DE;Morgan,J;Palings,I;Larrick,JW
我们以前已经证明，来源于人PMN的主要颗粒相关阳离子蛋白CAP 37(Mr=37kD)是一种单核细胞特异性趋化物质。这种新型趋化蛋白的N末端氨基酸序列与许多具有蛋白酶活性的炎症分子有显著的同源性，包括弹性蛋白酶和组织蛋白G。然而，在第41位丝氨酸被组氨酸取代，导致其缺乏丝氨酸蛋白酶活性。
We have previously shown that a major granule-associated cationic protein CAP 37 (Mr = 37 kD) derived from human PMN is a monocyte-specific chemoattractant. The N-terminal amino acid sequence of this novel chemotactic protein shares significant homology with a number of inflammatory molecules with protease activity including elastase and cathepsin G. However, a critical substitution of a serine for a histidine at position 41, results in its lack of serine protease activity.