Anhalt University of Applied Sciences, Molecular Biotechnology, Köthen, Germany.
Martin Luther University Halle, Medical Faculty, Institute for Medical Immunology, Halle, Germany.
Eur J Immunol. 2018 Sep;48(9):1592-1594. doi: 10.1002/eji.201747452. Epub 2018 Aug 22.
Chemokine CCL14 is inactive in its proform. Here, we show that inflammation- and cancer-associated kallikrein-related peptidases KLK5 and KLK8 remove the N-terminal eight amino acids from the proform thereby converting CCL14 to its active state. Activity of the chemokine is demonstrated by migration of myeloid cells expressing relevant receptors.
趋化因子 CCL14 以前体形式无活性。在这里,我们表明炎症和癌症相关的激肽释放酶相关肽酶 KLK5 和 KLK8 从前体中去除 N 端的八个氨基酸,从而将 CCL14 转化为其活性状态。通过表达相关受体的髓样细胞的迁移来证明趋化因子的活性。