The vitronectin receptor serves as an accessory molecule for the activation of a subset of gamma/delta T cells.

Roberts, Kevan; Yokoyama, Wayne M.; Kehn, P J; Shevach, Ethan M.

doi:10.1084/jem.173.1.231

Cited by 84 publications

(48 citation statements)

References 53 publications

(35 reference statements)

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“…The function of VNR on activated T lymphocytes is still unclear; however, it seems likely that VNR functions as a costimulatory molecule (27), as has been recently described for several other integrins (LFA-1, VLA-4, -5, -6) (23)(24)(25) .…”

Section: Rgds Rgesmentioning

confidence: 99%

The mouse vitronectin receptor is a T cell activation antigen.

Moulder

Roberts

Shevach

et al. 1991

The Journal of Experimental Medicine

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ntegrins comprise a complex family of cell adhesion molecules involved in cell-cell and cell-extracellular matrix protein (ECMP)t interactions (1). At least three subfamilies have been defined on the basis of the association ofany of a number of at chains with a common /3 chain (2) . We have previously characterized two mAbs (H9.2B8 and 8.1802) that identified a novel integrin expressed on murine y/S and a//3 T cell lines and hybridomas as well as on T cells activated for prolonged periods of time (7-21 d) by mitogens or alloantigens. This integrin mediated adhesion to fibronectin, vitronectin, and fibrinogen, and the two mAbs in combination, as well as the tetrapeptide RGDS alone, could inhibit the binding of cell lines to these ECMP (3) . In the present report, we make use of a number of antisera to the vitronectin receptor (VNR) and demonstrate that this novel integrin is the murine homologue of the human VNR, thereby demonstrating for the first time that the VNR is present on mouse T lymphocytes and that the expression of this (33 integrin can be upregulated by activation. SummaryIn this report, we demonstrate that the T cell activation antigen, recognized by monoclonal antibody HUN, is the murine homologue of the vitronectin receptor (VNR) and, thereby, we provide initial evidence that VNR is expressed on lymphoid cells . VNR is expressed on a variety of T cell lines, tumors, and Con A-activated splenocytes, but not resting T cells, and is capable of binding to the extracellular matrix proteins fibronectin, fibrinogen, and vitronectin, via the tripeptide sequence RGD. There was no evidence of novel a chains pairing with the VNR ct chain, as has been demonstrated in some human cells . In view of recent studies demonstrating that this molecule functions as an accessory molecule in T cell activation, the VNR may play an important role in mouse T cell functions.Cell Lines. Dendritic epidermal T cell (DETC) line T195 and its corresponding hybridoma (T195/BW) derived from fusion to BW5147 have been previously described (4-6).Antibodies. mAb H9 .2B8 is a hamster mAb obtained after immunizations with mouse DETC lines (3). Rabbit anti-human VNR

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Section: Rgds Rgesmentioning

confidence: 99%

The mouse vitronectin receptor is a T cell activation antigen.

Moulder

Roberts

Shevach

et al. 1991

The Journal of Experimental Medicine

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“…Thus, activation of T lymphocytes via the CD3 component of the antigen receptor is enhanced synergistically by binding of matrix proteins to/32 integrins (Carterra et al, 1988;Wacholz et al 1989;, interaction with collagen (Dang et al, 1990), or binding to fibronectin, laminin or vitronectin via/31 integrins (Nojima et al, 1990;Shimizu et al, 1990a,b;Roberts et al, 1991). In contrast, the matrix protein tenascin seems to inhibit rather than augment the activation of T cells (Ruegg et al, 1989).…”

Section: Adhesion Can Control How Cells Respond To Cytokinesmentioning

confidence: 99%

Cytokines in context.

Nathan

Sporn

1991

The Journal of Cell Biology

771

283

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“…Subsequent studies demonstrated that this receptor has a broad binding specificity and can mediate binding to fibronectin, fibrinogen, von Willebrand factor, and thrombospondin in addition to vitronectin (9)(10)(11)(12). More recently, a mAb specific for the murine ␣v␤3 vitronectin receptor (␣v␤3) was isolated (13,14), and used to identify ␣v␤3 as a costimulatory molecule required for spontaneous activation of ␥␦ T cell hybridomas (15).…”

mentioning

confidence: 99%

Expression of αv and β3 integrin chains on murine lymphocytes

Gerber

Pereira

Huang

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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The vitronectin receptor is a member of the integrin family of adhesion protein receptors and binds a broad spectrum of ligands, including fibronectin and fibrinogen in addition to vitronectin. We have generated four mAbs that recognize the murine ␣v␤3 vitronectin receptor. Biochemical and expression analyses showed that two of the mAbs are specific for the ␣v chain, and two are specific for the ␤3 chain. The mAbs are effective blocking reagents and inhibited cell adhesion to vitronectin, fibrinogen, and fibronectin. Staining analysis revealed expression of ␣v and ␤3 on certain populations of murine thymocytes, splenocytes, and bone marrow cells. The expression of ␣v and ␤3 appeared to be modulated at specific stages of thymocyte development, suggesting a possible function for the ␣v␤3 vitronectin receptor in T cell development.Integrins comprise a large family of heterodimeric cell surface proteins composed of ␣ and ␤ chains that mediate cell-cell interactions and interactions between cells and the extracellular matrix (ECM) (1-3). Integrins are expressed on all cells and are involved in a number of fundamental cell processes including adhesion, migration, activation, and differentiation. The expression and functions of integrins have been particularly well-studied with respect to lymphocytes, which require a variety of cell-cell and cell-ECM interactions to perform their complex programs of immune surveillance and antigen response (4, 5). The functions of integrins depend on binding to specific adhesion proteins, such as fibronectin, often through recognition of the tripeptide, arginine-glycine-aspartic acid (RGD), binding motif (6).The human ␣v␤3 vitronectin receptor was originally identified as a heterodimeric molecule with vitronectin binding activity (7), and later shown to be related to other members of the integrin family (8). Subsequent studies demonstrated that this receptor has a broad binding specificity and can mediate binding to fibronectin, fibrinogen, von Willebrand factor, and thrombospondin in addition to vitronectin (9-12). More recently, a mAb specific for the murine ␣v␤3 vitronectin receptor (␣v␤3) was isolated (13,14), and used to identify ␣v␤3 as a costimulatory molecule required for spontaneous activation of ␥␦ T cell hybridomas (15).In the process of identifying cell surface molecules involved in the constitutive interleukin 2 (IL-2) secretion of murine V␥1, V␦6 T cell hybridomas, we generated a series of monoclonal antibodies (mAbs) that recognize murine ␣v␤3. Here, we present the characterization of four of these mAbs, including the determination of their chain specificities and staining analysis of several lymphoid populations. Contrary to previous reports (13, 16), we observed detectable levels of ␣v and ␤3 expression on certain populations of thymocytes and splenocytes in addition to bone marrow cells. Interestingly, we observed differential expression of the ␣v and ␤3 chains on discrete populations of thymocytes, suggesting a possible role for this receptor in T cell develo...

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The vitronectin receptor serves as an accessory molecule for the activation of a subset of gamma/delta T cells.

Cited by 84 publications

References 53 publications

The mouse vitronectin receptor is a T cell activation antigen.

The mouse vitronectin receptor is a T cell activation antigen.

Cytokines in context.

Expression of αv and β3 integrin chains on murine lymphocytes

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