CD43 collaborates with P-selectin glycoprotein ligand-1 to mediate E-selectin-dependent T cell migration into inflamed skin
CD43 collaborates with P-selectin glycoprotein ligand-1 to mediate E-selectin-dependent T cell migration into inflamed skin
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DOI：
10.4049/jimmunol.178.4.2499
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发表时间：
2007-02-15
影响因子：
4.4
通讯作者：
Hirata, Takako
中科院分区：
文献类型：
--
作者：
Matsumoto, Masanori;Shigeta, Akiko;Hirata, Takako
活化的T细胞向非淋巴组织的迁移是由内皮细胞上表达的P-和E-选择素及其T细胞上的配体的相互作用启动的。P-selectin glycoprotein ligand-1（PSGL-1）是唯一一种在活化T细胞体内迁移过程中发挥作用的E-选择素配体。我们在这项研究中表明，CD 43缺陷型Th 1细胞，PSGL-1缺陷型细胞一样，表现出降低E-选择素结合活性与野生型细胞相比。具有PSGL-1和CD 43双重缺陷的Th 1细胞表现出更低的E-选择素结合活性。在迁移试验中，过继转移的细胞迁移到发炎的皮肤P-和E-选择素依赖性，CD 43显着PSGL-1-独立的Th 1细胞迁移。此外，来自PSGL-1和/或CD 43缺陷致敏小鼠引流淋巴结的体内活化T细胞显示出显著降低的E-选择素结合活性和迁移效率，其中来自双缺陷小鼠的T细胞显示出最显著的降低。总的来说，这些结果表明，在活化的T细胞上表达的CD 43作为E-选择素配体发挥作用，从而与PSGL-1合作介导T细胞迁移到发炎部位。
Activated T cell migration into nonlymphoid tissues is initiated by the interactions of P- and E-selectin expressed on endothelial cells and their ligands on T cells. P-selectin glycoprotein ligand-1 (PSGL-1) has been the only E-selectin ligand demonstrated to function during the in vivo migration of activated T cells. We show in this study that CD43-deficient Th1 cells, like PSGL-1-deficient cells, exhibited reduced E-selectin-binding activity compared with wild-type cells. Th1 cells with a PSGL-1 and CD43 double deficiency showed even less E-selectin-binding activity. In migration assays in which adoptively transferred cells migrate to inflamed skin P- and E-selectin dependently, CD43 contributed significantly to PSGL-1-independent Th1 cell migration. In addition, in vivo activated T cells from the draining lymph nodes of sensitized mice deficient in PSGL-1 and/or CD43 showed significantly decreased E-selectin-binding activity and migration efficiency, with T cells from double-deficient mice showing the most profound decrease. Collectively, these results demonstrate that the CD43 expressed on activated T cells functions as an E-selectin ligand and thereby mediates T cell migration to inflamed sites, in collaboration with PSGL-1.