A new class of membrane-bound chemokine with a CX(3)C motif
A new class of membrane-bound chemokine with a CX(3)C motif
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DOI：
10.1038/385640a0
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发表时间：
1997-02-13
期刊：
影响因子：
64.8
通讯作者：
Schall, TJ
中科院分区：
文献类型：
--
作者：
Bazan, JF;Bacon, KB;Schall, TJ
趋化因子在免疫监视中指导白细胞的运输，在艾滋病等炎症和传染病中发挥着关键作用(1-5)。迄今为止研究的所有趋化因子都是相对分子质量类似于 7K-15K 的分泌蛋白，并且属于：由半胱氨酸特征基序定义的三个家族：CXC、CC 和 C（参考文献 3、6、7），其中 C 是半胱氨酸，X 是任何氨基酸残基。我们在这里报告了第四种人类趋化因子类型的鉴定和表征，该趋化因子类型源自 hbn 造血细胞并具有新的 CX(3)C 指纹。与其他趋化因子类型不同，人类 CX(3)C 趋化因子的多肽链预计是 373 个氨基酸蛋白质的一部分，该蛋白质在延伸的粘蛋白样茎顶部携带趋化因子结构域。该分子可以两种形式存在：膜锚定或脱落的 95K 糖蛋白。可溶性 CX(3)C 趋化因子对 T 细胞和单核细胞具有强大的趋化活性，而在活化的原代内皮细胞上诱导的细胞表面结合蛋白可促进这些白细胞的强烈粘附。 CX(3)C趋化因子的结构、生化特征、组织分布和染色体定位都表明它代表了一类独特的趋化因子，可能构成内皮细胞白细胞运输分子控制的一部分。
Chemokines direct the trafficking of white blood cells in immune surveillance, playing a key role in inflammatory and infectious diseases such as AIDS(1-5). All chemokines studied so far are secreted proteins of relative molecular mass similar to 7K-15K and fall into:three families that are defined by a cysteine signature motif: CXC, CC and C (refs 3, 6, 7), where C is a cysteine and X any amino-acid residue. We report here the identification and characterization of a fourth human chemokine type, derived from hbn-haemopoietic cells and bearing a new CX(3)C fingerprint. Unlike other chemokine types, the polypeptide chain of the human CX(3)C chemokine is predicted to be part of a 373-amino-acid protein that carries the chemokine domain on top of an extended mucin-like stalk. This molecule can exist in two forms: either membrane-anchored or as a shed 95K glycoprotein. The soluble CX(3)C chemokine has potent chemoattractant activity for T cells and monocytes, and the cell-surface-bound protein, which is induced on activated primary endothelial cells, promotes strong adhesion of those leukocytes. The structure, biochemical features, tissue distribution and chromosomal localization of CX(3)C chemokine all indicate that it represents a unique class of chemokine that may constitute part of the molecular control of leukocyte traffic at the endothelium.