Chemotactic activity and receptor binding of neutrophil attractant/activation protein-1 (NAP-1) and structurally related host defense cytokines: interaction of NAP-2 with the NAP-1 receptor.
Chemotactic activity and receptor binding of neutrophil attractant/activation protein-1 (NAP-1) and structurally related host defense cytokines: interaction of NAP-2 with the NAP-1 receptor.
复制标题
中性粒细胞吸引剂/激活蛋白-1 (NAP-1) 和结构相关的宿主防御细胞因子的趋化活性和受体结合：NAP-2 与 NAP-1 受体的相互作用。
DOI：
10.1002/jlb.49.3.258
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发表时间：
1991
影响因子：
5.5
通讯作者：
Castor,CW
中科院分区：
文献类型：
--
作者：
Leonard,EJ;Yoshimura,T;Rot,A;Noer,K;Walz,A;Baggiolini,M;Walz,DA;Goetzl,EJ;Castor,CW
中性粒细胞吸引/活化蛋白-1（NAP-1）与血小板因子-4（PF-4）和NAP-2（结缔组织活化蛋白-III的截短形式[CTAP-III（des 1-15）]具有序列相似性。我们比较了这些相关蛋白对中性粒细胞的趋化活性。为了比较，我们还包括CTAP-III、CTAP-III（des 1-13）、PF-4的C-末端十二肽[PF-4（59-70）]和C5 a。NAP-1和C5 a的趋化效力（EC 50）最高。尽管C5 a、NAP-1和NAP-2的趋化功效（中性粒细胞迁移的峰值百分比）相当，但NAP-2反应仅在浓度比NAP-1 EC 50（10 - 8 M）高100倍时发生。CTAP-III蛋白的数据证实CTAP-III不是引诱剂，并且趋化活性是由于N末端残基裂解产生CTAP-III（des 1-13）或NAP-2 [CTAP-III（des 1-15）]而出现的。PF-4的趋化活性较低且可变，9例受试者中有6例的中性粒细胞无显著反应。相比之下，PF-4（59-70）经常诱导高趋化反应，尽管1.6 × 10 - 5 M的EC 50比NAP-1高1,000倍。未标记的NAP-1或NAP-2可抑制荧光标记的NAP-1与中性粒细胞的结合，而PF-4或PF-4则不抑制（59-70）。这表明NAP-2与中性粒细胞NAP-1受体相互作用。尽管NAP-2的趋化效力较低，但它是损伤部位的潜在引诱剂，因为从血小板中释放出相对大量的母体CTAP-III，血清浓度约为10 - 6 M。
Neutrophil attractant/activation protein‐1 (NAP‐1) has sequence similarity to platelet factor‐4 (PF‐4) and to NAP‐2 (a truncated form of connective tissue activating protein‐Ill [CTAP‐III(des 1–15)]. We compared chemotactic activity for neutrophils of these related proteins. We also included for comparison CTAP‐III, CTAP‐III(des 1–13), the C‐terminal dodecapeptide of PF‐4 [PF‐4(59–70)], and C5a. Chemotactic potency (EC50) was highest for NAP‐1 and C5a. Although chemotactic efficacy (peak percentage of neutrophils migrating) was comparable for C5a, NAP‐1, and NAP‐2, the NAP‐2 response occurred only at concentrations 100‐fold higher than the NAP‐1 EC50of 10‐8M. Data for the CTAP‐III proteins confirmed that CTAP‐III is not an attractant and that chemotactic activity appears as a result of cleavage of residues at the N‐terminus to make CTAP‐III(des 1–13) or NAP‐2 [CTAP‐III(des 1–15)]. Chemotactic activity of PF‐4 was low and variable, with no significant response by neutrophils from six of nine subjects. In contrast, PF‐4(59–70) regularly induced high chemotactic responses, although the EC50of 1.6 × 10‐5M was 1,000‐fold greater than that of NAP‐1. The binding of fluoresceinated NAP‐1 to neutrophils was inhibited by unlabeled NAP‐1 or NAP‐2 but not by PF‐4 or PF‐4 (59–70). This suggests that NAP‐2 interacts with the neutrophil NAP‐1 receptor. Despite the low chemotactic potency of NAP‐2, it is a potential attractant at sites of injury because of the relatively large amounts of the parent CTAP‐III released from platelets, as indicated by a serum concentration of approximately 10‐6M.