Zanetti M, Gennaro R, Romeo D
Laboratorio Nazionale Consorzio Interuniversitario Biotecnologie, AREA Science Park, Trieste, Italy.
FEBS Lett. 1995 Oct 23;374(1):1-5. doi: 10.1016/0014-5793(95)01050-o.
A novel protein family, showing a conserved proregion and a variable C-terminal antimicrobial domain, and named cathelicidin, has been identified in mammalian myeloid cells. The conserved proregion shows sequence similarity to members of the cystatin superfamily of cysteine proteinase inhibitors. Cathelicidins are stored in the cytoplasmic granules of neutrophil leukocytes and release the antimicrobial peptides upon leukocyte activation. Some of these peptides can assume an alpha-helical conformation, others contain one or two disulfide bonds, still others are Pro- and Arg-rich, or Trp-rich. In addition to bacterial killing, some of these peptides exert additional functions related to host defense such as LPS-neutralization and promotion of wound healing.
在哺乳动物髓细胞中已鉴定出一个新的蛋白质家族，其具有保守的前区和可变的C端抗菌结构域，被命名为cathelicidin。保守的前区与半胱氨酸蛋白酶抑制剂的胱抑素超家族成员具有序列相似性。Cathelicidin储存在中性粒细胞的细胞质颗粒中，并在白细胞激活时释放抗菌肽。其中一些肽可以呈现α-螺旋构象，其他肽含有一个或两个二硫键，还有一些富含脯氨酸和精氨酸或富含色氨酸。除了杀灭细菌外，这些肽中的一些还发挥与宿主防御相关的其他功能，如LPS中和和促进伤口愈合。
