Structure of the human macrophage MARCO receptor and characterization of its bacteria-binding region
Structure of the human macrophage MARCO receptor and characterization of its bacteria-binding region
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DOI：
10.1074/jbc.273.8.4530
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发表时间：
1998-02-20
影响因子：
4.8
通讯作者：
Tryggvason, K
中科院分区：
文献类型：
--
作者：
Elomaa, O;Sankala, M;Tryggvason, K
从cDNA克隆中确定了具有胶原结构的人巨噬细胞受体（MARCO）的一级结构，并显示其与小鼠的一级结构高度相似（Elomaa，O.，Kangas，M.，Sahlberg，C.，Tuukkanen，J.，索尔穆嫩河Liakka，A.，塞斯莱夫岛，Kraal，G.，Tryggvason，H.（1995）Cell 80，603-609）。在两个物种之间，诸如细胞外间隔区结构域III中的潜在碳水化合物附着位点和胶原结构域IV中Gly-Xaa-Yaa重复的中断的特征是保守的。然而，人MARCO多肽链缺乏小鼠中存在的细胞内半胱氨酸，以及在鼠蛋白质中形成链间二硫键的两个细胞外半胱氨酸，FIT原位杂交显示MARCO在患有脓毒症的人个体的几种组织的巨噬细胞中强烈表达，在其他细胞类型中未观察到表达。MARCO的细菌结合区域在MARCO的全长和截短变体的结合研究中确定，并且定位于靠近COOH末端结构域V的富含半胱氨酸的部分的区域。建立了结构域V的链内二硫键模式，表明这些键在半胱氨酸对C1-C5、C2-C6和C3-C4之间。
The primary structure of human macrophage receptor with collagenous structure (MARCO) was determined from cDNA clones and shown to be highly similar to that of mouse (Elomaa, O., Kangas, M., Sahlberg, C., Tuukkanen, J., Sormunen, R., Liakka, A., Thesleff, I., Kraal, G., and Tryggvason, H. (1995) Cell 80, 603-609), Features such as potential carbohydrate attachment sites in the extracellular spacer domain III and the interruption of Gly-Xaa-Yaa repeats in the collagenous domain IV were conserved between the two species, However, the human MARCO polypeptide chain lacked the intracellular cysteine present in mouse, as well as two extracellular cysteines that form interchain disulfide bonds in the murine protein, fit situ hybridization showed MARCO to be strongly expressed in macrophages of several tissues of human individuals with sepsis, No expression was observed in other cell types. The bacteria-binding region of MARCO was determined in binding studies with full-length and truncated variants of MARCO, and localized to a region proximal to the cysteine-rich part of the COOH-terminal domain V, The intrachain disulfide bond pattern of domain V was established showing that these bonds are between cysteine pairs C1-C5, C2-C6, and C3-C4.