CD167 Acts as a Novel Costimulatory Receptor in T-Cell Activation

Dang, Nana; Hu, Jinsong; Liu, Xinping; Li, Xia; Ji, Shaoping; Zhang, Wei; Lü, Fan; Yang, Angang; Han, Hua; Han, Wei; Jin, Boquan; Yao, Libo

doi:10.1097/cji.0b013e3181acea46

Cited by 9 publications

(7 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Activated human T cells are known to express two collagen-binding integrin namely a1b1 and a2b1, which promote T cell adhesion to collagens [Pribila et al, 2004]. In addition to collagen-binding integrins, we and others have reported that activated T cells can also express DDR1 [Kamohara et al, 2001;Dang et al, 2009;Hachehouche et al, 2010], a nonintegrin collagen receptor [Vogel et al, 2006;Heino et al, 2009]. In this study, we show that activated T cells bind collagen I in a DDR1-dependent manner but that DDR1 did not enhance their adhesion to collagen I, which is dependent on b1 integrins [Boisvert et al, 2007] and (data not shown).…”

Section: Discussionmentioning

confidence: 95%

“…Despite these findings, it remains unknown how DDR1 promotes T cell interactions with collagen. In addition, although TCR-engagement [Hachehouche et al, 2010] or phytohemagglutinin A [Kamohara et al, 2001;Dang et al, 2009] enhance DDR1 expression in human primary T cells, the signaling pathways that regulate DDR1 expression in T cells have not yet been identified.…”

mentioning

confidence: 96%

See 1 more Smart Citation

Discoidin domain receptor 1 expression in activated T cells is regulated by the ERK MAP kinase signaling pathway

et al. 2011

View full text Add to dashboard Cite

The expression and function of discoidin domain receptor 1 (DDR1) in T cells are still poorly explored. We have recently shown that activation of primary human T cells via their T cell receptor leads to increased expression of DDR1, which promoted their migration in three-dimensional collagen. In the present study, we provide evidence that activated T cells bind collagen through DDR1. We found that the DDR1:Fc blocking molecule significantly reduced the ability of activated T cells to bind soluble biotinylated collagen. However, DDR1:Fc had no impact on the adhesion of activated T cells to collagen and overexpression of DDR1 in Jurkat T cells did not enhance their adhesion. Together, our results indicate that DDR1 can promote T cell migration without enhancing adhesion to collagen, suggesting that it can contribute to the previously described amoeboid movement of activated T cells in collagen matrices. Our results also show that CD28, in contrast to IL-2 expression, did not costimulate the expression of DDR1 in primary human T cells. Using specific inhibitors, we demonstrated that TCR-induced expression of DDR1 in T cells is regulated by the Ras/Raf/ERK MAP Kinase and PKC pathways but not by calcium/calcineurin signaling pathway or the JNK and P38 MAP Kinases. Thus, our study provides additional insights into the physiology of DDR1 in T cells and may therefore further our understanding of the regulatory mechanisms of T cell migration.

show abstract

Section: Discussionmentioning

confidence: 95%

mentioning

confidence: 96%

Discoidin domain receptor 1 expression in activated T cells is regulated by the ERK MAP kinase signaling pathway

et al. 2011

View full text Add to dashboard Cite

show abstract

“…DDR1 also stimulates the collective migration of cancer cells via the Giα13 pathway [15, 16]. In addition to epithelial and carcinoma cells, short-term activated human T cells also express DDR1 [17-19] and the blocking recombinant receptor DDR1:Fc reduces their migration across collagen gel-coated transwells [18]. Moreover, DDR1 overexpression enhances THP-1 monocytic cell line migration in 3D collagen [19].…”

Section: Introductionmentioning

confidence: 99%

Discoidin domain receptor 1 promotes Th17 cell migration by activating the RhoA/ROCK/MAPK/ERK signaling pathway

et al. 2016

View full text Add to dashboard Cite

Effector T cell migration through the tissue extracellular matrix (ECM) is an important step of the adaptive immune response and in the development of inflammatory diseases. However, the mechanisms involved in this process are still poorly understood. In this study, we addressed the role of a collagen receptor, the discoidin domain receptor 1 (DDR1), in the migration of Th17 cells. We showed that the vast majority of human Th17 cells express DDR1 and that silencing DDR1 or using the blocking recombinant receptor DDR1:Fc significantly reduced their motility and invasion in three-dimensional (3D) collagen. DDR1 promoted Th17 migration by activating RhoA/ROCK and MAPK/ERK signaling pathways. Interestingly, the RhoA/ROCK signaling module was required for MAPK/ERK activation. Finally, we showed that DDR1 is important for the recruitment of Th17 cells into the mouse dorsal air pouch containing the chemoattractant CCL20. Collectively, our results indicate that DDR1, via the activation of RhoA/ROCK/MAPK/ERK signaling axis, is a key pathway of effector T cell migration through collagen of perivascular tissues. As such, DDR1 can contribute to the development of Th17-dependent inflammatory diseases.

show abstract

“…10 However, DDR1 is not expressed in circulating neutrophils and lymphocytes and is only expressed hours after cell activation. 10,30 We speculate that, when neutrophils migrate in vivo toward an inflammation site, DDR1 is not present at the cell surface. By contrast, in physiologic conditions, DDR2 is readily expressed in naive neutrophils.…”

mentioning

confidence: 99%

Discoidin domain receptor 2 regulates neutrophil chemotaxis in 3D collagen matrices

Afonso

McCann

Kapnick

et al. 2013

Blood

View full text Add to dashboard Cite

Key Points• DDR2 regulates the directional migration of neutrophils in 3D collagen matrices, but not on 2D surfaces. • DDR2 regulates directionality through increased metalloproteinase secretion and generation of collagen-derived chemotactic peptide gradients.Neutrophils express a variety of collagen receptors at their surface, yet their functional significance remains unclear. Although integrins are essential for neutrophil adhesion and migration on 2-dimensional (2D) surfaces, neutrophils can compensate for the absence of integrins in 3-dimensional (3D) lattices. In contrast, we demonstrate that the inhibition of the tyrosine-kinase collagen receptor discoidin domain receptor 2 (DDR2) has no impact on human primary neutrophil migration on 2D surfaces but is an important regulator of neutrophil chemotaxis in 3D collagen matrices. In this context, we show that DDR2 activation specifically regulates the directional migration of neutrophils in chemoattractant gradients. We further demonstrate that DDR2 regulates directionality through its ability to increase secretion of metalloproteinases and local generation of collagen-derived chemotactic peptide gradients. Our findings highlight the importance of collagen-derived extracellular signaling during neutrophil chemotaxis in 3D matrices. (Blood. 2013;121(9):1644-1650) IntroductionNeutrophils exhibit the ability to maintain robust migration under a wide array of distinct environmental conditions. For example, by increasing the rate of actin polymerization, neutrophils lacking integrins are able to retain normal migration speeds in 3D environments. 1,2 We set out to determine the role of another collagen receptor family, the discoidin domain receptors (DDRs), during neutrophil chemotaxis. The DDR family is composed of 2 members, DDR1 and DDR2. DDRs are homodimeric receptor tyrosine kinases that bind to triple-helical collagen fibers through a domain similar to discoidin 1 of the social amoeba Dictyostelium discoideum. 3,4 On binding to collagen, DDRs become activated and serve as docking sites for many signaling pathways. 5 A common outcome after DDR activation is the increase in metalloproteinase (MMP) secretion and collagen rearrangement. [6][7][8][9] As a consequence, DDR1 and DDR2 have both been associated with metastasis during tumor progression. 6 Similarly, DDR1 overexpression has been shown to enhance lymphocyte migration. 10,11 However, the mechanism underlying the enhanced leukocyte migration remains unknown.We show that circulating human primary neutrophils solely express DDR2 and establish that DDR2 regulates the ability of neutrophils to migrate directionally toward chemoattractants in a collagen I matrix. DDR2 activation induces increased MMP secretion, leading to the generation of collagen-derived chemotactic peptides that are poised to form local gradients and enhance neutrophil persistence. Methods Isolation of human blood neutrophilsBlood was collected from anonymous healthy donors enrolled in the National Institutes of Health Blood Bank research prog...

show abstract

CD167 Acts as a Novel Costimulatory Receptor in T-Cell Activation

Cited by 9 publications

References 51 publications

Discoidin domain receptor 1 expression in activated T cells is regulated by the ERK MAP kinase signaling pathway

Discoidin domain receptor 1 expression in activated T cells is regulated by the ERK MAP kinase signaling pathway

Discoidin domain receptor 1 promotes Th17 cell migration by activating the RhoA/ROCK/MAPK/ERK signaling pathway

Discoidin domain receptor 2 regulates neutrophil chemotaxis in 3D collagen matrices

Contact Info

Product

Resources

About