Primary structures of three human neutrophil defensins.
Primary structures of three human neutrophil defensins.
复制标题
DOI：
10.1172/jci112121
复制
发表时间：
1985-10
期刊：
影响因子：
--
通讯作者：
M. Selsted;S. Harwig;T. Ganz;J. Schilling;R. Lehrer
中科院分区：
文献类型：
--
作者：
M. Selsted;S. Harwig;T. Ganz;J. Schilling;R. Lehrer
测定了3种人中性粒细胞抗菌肽（HNP）的一级结构。我们将HNP-1、HNP-2和HNP-3称为防御素，它们富含胱氨酸、精氨酸和芳香残基，但缺乏游离巯基和碳水化合物。它们的长度为29-30个残基，除氨基末端残基外，其余残基的序列相同。这些防御蛋白与先前从兔多形核白细胞中纯化的大小和生物活性相似的肽序列同源，但与已知序列的其他中性粒细胞蛋白无关。人类防御素的11个氨基酸残基，包括所有6个半胱氨酸残基，在这个多基因肽家族的6个兔子成员中不变地保守。兔和人白细胞中都存在类似结构的抗菌肽，这支持了它们在吞噬细胞介导的宿主防御中作为杀灭剂的作用。
The primary structures of three human neutrophil antimicrobial peptides (HNP) were determined. The peptides, HNP-1, HNP-2, and HNP-3, which we have termed defensins, were rich in cystine, arginine, and aromatic residues, but were devoid of free sulfhydryl groups and carbohydrate moieties. They were 29-30 residues in length and identical in sequence in all but their amino terminal residues. The defensins were homologous in sequence to peptides of similar size and biological activity previously purified from rabbit polymorphonuclear leukocytes, but unrelated to other neutrophil proteins of known sequence. 11 amino acid residues of the human defensins, including all six cysteinyl residues, were invariantly conserved in the six rabbit members of this multigene peptide family. That similarly structured antimicrobial peptides are present in both rabbit and human leukocytes supports their purported role as cidal agents in phagocyte-mediated host defense.