Structure and neutrophil-activating properties of a novel inflammatory peptide (ENA-78) with homology to interleukin 8.
Structure and neutrophil-activating properties of a novel inflammatory peptide (ENA-78) with homology to interleukin 8.
复制标题
与白介素8具有同源性的新型炎症肽(ENA-78)的结构和中性粒细胞激活特性。
DOI:
10.1084/jem.174.6.1355
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发表时间:
1991-12-01
影响因子:
15.3
通讯作者:
Strieter, R M
中科院分区:
文献类型:
--
作者:
Walz, A;Burgener, R;Car, B;Baggiolini, M;Kunkel, S L;Strieter, R M
A new neutrophil-activating peptide, termed ENA-78, was identified in the conditioned media of stimulated human type II epithelial cell line A549. In response to stimulation with either interleukin 1 beta (IL-1 beta) or tumor necrosis factor alpha (TNF-alpha), ENA-78 was produced and secreted concomitantly with IL-8, GRO alpha, and GRO gamma. ENA-78 consists of 78 amino acids [sequence; see text] and has a molecular weight of 8,357. It has four cysteines positioned identically to those of IL-8 and analogues, and thus belongs to the CXC family of peptides. ENA-78 is related to neutrophil-activating peptide 2 (NAP-2) and GRO alpha (sequence identity, 53% and 52%, respectively) and IL-8 (22% identity). Like NAP-2 and GRO alpha, ENA-78 stimulates neutrophils, inducing chemotaxis, a rise in intracellular free calcium and exocytosis. Cross-desensitization experiments indicate that ENA-78 acts through the same type of receptors as IL-8, NAP-2, and GRO alpha.