Dong Chen, Chua Annabelle, Ganguly Bishu, Krensky Alan M, Clayberger Carol
Division of Immunology and Transplantation Biology, Department of Pediatrics, Stanford University, Stanford, CA 94305-5164, USA.
J Immunol Methods. 2005 Jul;302(1-2):136-44. doi: 10.1016/j.jim.2005.05.008.
Chemokines are a family of small, secreted chemoattractant cytokines that regulate distribution and function of leukocytes during immune responses. While most chemokines are members of the CC or CXC subgroups, XCL1, also known as lymphotactin, is the sole member of the C subgroup. XCL1 is produced by activated CD8(+) T cells, NK cells, gammadelta T cells, and mast cells. XCL1 differs from other chemokines in that it contains only a single disulfide bond and a mucin-like domain at its carboxy terminus that is glycosylated. Understanding the biologic functions of chemokines has largely depended upon expression of these recombinant molecules in E. coli. To examine the effects of glycosylation on the biologic activity of XCL1, we designed constructs for expression of human XCL1 in insect S2 cells. Comparison of this material with that expressed in E. coli reveals that glycosylation significantly increases the biologic activity of XCL1.
趋化因子是一类小的、分泌型的化学引诱细胞因子，在免疫反应过程中调节白细胞的分布和功能。虽然大多数趋化因子是CC或CXC亚组的成员，但XCL1（也称为淋巴细胞趋化因子）是C亚组的唯一成员。XCL1由活化的CD8(+) T细胞、自然杀伤细胞、γδ T细胞和肥大细胞产生。XCL1与其他趋化因子的不同之处在于，它仅含有一个二硫键，并且在其糖基化的羧基末端有一个粘蛋白样结构域。对趋化因子生物学功能的了解在很大程度上依赖于这些重组分子在大肠杆菌中的表达。为了研究糖基化对XCL1生物学活性的影响，我们设计了在昆虫S2细胞中表达人XCL1的构建体。将这种材料与在大肠杆菌中表达的材料进行比较，结果显示糖基化显著提高了XCL1的生物学活性。
