Purification and primary amino acid sequence of a novel neutrophil chemotactic factor LECT2
Purification and primary amino acid sequence of a novel neutrophil chemotactic factor LECT2
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DOI：
10.1016/0165-2478(96)02572-2
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发表时间：
1996-08-01
影响因子：
4.4
通讯作者：
Suzuki, K
中科院分区：
文献类型：
--
作者：
Yamagoe, S;Yamakawa, Y;Suzuki, K
我们从PHA激活的人T细胞白血病SKW-3细胞的培养液中纯化了中性粒细胞趋化因子。经Tricin-SDS-聚丙烯酰胺凝胶电泳和氨基酸组成分析，该因子为一个分子量为16 kDa的碱性蛋白。一级氨基酸序列显示，该趋化因子与其他已知的趋化因子显著不同，表明命名为LECT 2的新蛋白。该序列与鸡未成熟粒细胞和正常粒细胞中表达的myb诱导的髓样蛋白-1（Mim-1）具有同源性。其生物学功能尚未确定。LECT 2和Mim-1可能以一种尚未确定的方式参与调节中性粒细胞功能。
We purified a neutrophil chemotactic factor from a culture fluid of the PHA-activated human T-cell leukemia SKW-3 cells. The factor showed a 16-kDa basic protein by Tricin-SDS-polyacrylamide gel electorophoresis and analysis of amino acid composition. The primary amino acid sequence revealed that the chemotactic factor was significantly different from other known chemotactic factors, indicating a novel protein designated LECT2. The sequence revealed homology with the myb-induced myeloid protein-1 (Mim-1), which is expressed from gene in immature and normal granulocytes of chicken. Its biological function had not yet been identified. LECT2 and Mim-1 may be involved in the regulation of neutrophil functions in an as yet unidentified way.