Peptides generated from C-reactive protein by a neutrophil membrane protease. Amino acid sequence and effects of peptides on neutrophil oxidative metabolism and chemotaxis.
Peptides generated from C-reactive protein by a neutrophil membrane protease. Amino acid sequence and effects of peptides on neutrophil oxidative metabolism and chemotaxis.
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由中性粒细胞膜蛋白酶从 C 反应蛋白产生的肽。
DOI：
10.4049/jimmunol.145.5.1469
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发表时间：
1990
影响因子：
4.4
通讯作者：
F. C. D. Beer
中科院分区：
文献类型：
--
作者：
E. Shephard;R. Anderson;O. Rosen;M. Myer;Mati Fridkin;A. Strachan;F. C. D. Beer
我们最近提供的证据表明，C-反应蛋白（CRP）可以作为一个可上调的基板膜相关的中性粒细胞丝氨酸蛋白酶（S）。CRP的降解产生小的可溶性生物活性肽，其抑制活化的中性粒细胞的许多促炎功能，并可对抗这些细胞的组织破坏潜力。我们报告的反相高效液相色谱分离的小TCA可溶性肽时，CRP与nonstimulated或PMA刺激的中性粒细胞和纯化的中性粒细胞膜降解。已确定从CRP消化物中分离的七种肽的氨基酸序列，并合成了与这些序列同源的合成肽。对应于完整蛋白的残基201-206（CRP-III）、83-90（CRP-IV）和77-82（CRP-V）的三种合成肽被鉴定为在50 μ M下显著抑制活化的嗜中性粒细胞产生超氧化物，而CRP-III和CRP-V另外在该浓度下抑制嗜中性粒细胞趋化性。这些肽的作用是相加的，它们的作用可能涉及中性粒细胞活化的信号转导途径。
We have recently provided evidence that C-reactive protein (CRP) could act as an up-regulatable substrate for membrane-associated neutrophil serine protease(s). The resultant degradation of CRP yielded small soluble bioactive peptides that inhibit many of the proinflammatory functions of activated neutrophils and could oppose the tissue destructive potential of these cells. We report on the reverse phase HPLC separation of the small TCA-soluble peptides obtained when CRP is degraded with nonstimulated or PMA-stimulated neutrophils and purified neutrophil membranes. The amino acid sequence of seven peptides isolated from the CRP digest has been ascertained and synthetic peptides homologous to these sequences have been synthesized. Three of the synthetic peptides corresponding to residues 201-206 (CRP-III), 83-90 (CRP-IV), and 77-82 (CRP-V) of the intact protein were identified to significantly inhibit superoxide production from activated neutrophils at 50 microM whereas CRP-III and CRP-V in addition inhibited neutrophil chemotaxis at this concentration. These peptides act additively and their action likely involves the signal transduction pathways for neutrophil activation.