STRUCTURE DETERMINATION OF A HUMAN-LYMPHOCYTE DERIVED NEUTROPHIL ACTIVATING PEPTIDE (LYNAP)
STRUCTURE DETERMINATION OF A HUMAN-LYMPHOCYTE DERIVED NEUTROPHIL ACTIVATING PEPTIDE (LYNAP)
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DOI：
10.1016/s0006-291x(88)80364-4
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发表时间：
1988-03-15
影响因子：
3.1
通讯作者：
CHRISTOPHERS, E
中科院分区：
文献类型：
--
作者：
GREGORY, H;YOUNG, J;CHRISTOPHERS, E
植物血凝素或刀豆蛋白A刺激的人T淋巴细胞产生一种因子(LYNAP)，在人外周中性粒细胞中具有强大的趋化和酶脱颗粒活性。LYNAP的序列分析建立了一个明显新的72个残基的多肽结构。对蛋白质数据库的分析表明，LYNAP与最近由血小板产生的结缔组织激活蛋白具有约30%的序列同源性。此外，随后发现，该氨基酸序列与从有丝分裂原刺激的人外周血白细胞中上调的mRNA衍生的cDNA克隆预测的氨基酸序列基本相同。
Phytohemagglutinin or Concanavalin A-stimulated human T-lymphocytes produce a factor (LYNAP) with potent chemotactic and enzyme degranulating activity in peripheral human neutrophils. Sequence analysis of LYNAP established an apparently novel 72 residue polypeptide structure. Examination of protein data bases showed tht LYNAP had about 30% sequence homology with recently characterised connective tissue activating proteins produced by platelets. Furthermore, it was subsequently found that the amino acid sequence is largely the same as that predicted from a cDNA clone derived from mRNA elevated in peripheral human leukocytes stimulated by mitogens.