Regulation of integrin function by T cell activation

Zell, Traci; Kivens, Wendy J.; Kellermann, Sirid Aimée; Shimizu, Yoji

doi:10.1007/bf02786469

Cited by 25 publications

(20 citation statements)

References 146 publications

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“…The functionality of the cultured salivary acinar cells in vitro is confirmed by their secretion and organization of their own basement membrane including the critical component perlecan that can support further growth and differentiation by virtue of its ability to interact with cell adhesion molecules that can influence integrin-mediated events. 11,15 Uniquely, no non-human-derived material was needed for isolation or culture of the acinar cells.…”

Section: Discussionmentioning

confidence: 99%

Perlecan Domain IV Peptide Stimulates Salivary Gland Cell AssemblyIn Vitro

Pradhan

Zhang

Jia

et al. 2009

Tissue Engineering Part A

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Section: Discussionmentioning

confidence: 99%

Perlecan Domain IV Peptide Stimulates Salivary Gland Cell AssemblyIn Vitro

Pradhan

Zhang

Jia

et al. 2009

Tissue Engineering Part A

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“…For example, the absence of ADAP also profoundly affects TCR-stimulated, integrin-mediated adhesion (70,71). Integrin receptors provide costimulatory signals to naive T cells by stabilizing contacts between the TCR and immobilized anti-CD3 Ab and decreasing the threshold for activation (73)(74)(75). Because PTP␣ positively regulates integrin signaling in fibroblasts (8,9), it might play a role in Ag-mediated interactions between the TCR and T cell integrins as well.…”

Section: Studies Of Fynmentioning

confidence: 99%

Protein Tyrosine Phosphatase α Regulates Fyn Activity and Cbp/PAG Phosphorylation in Thymocyte Lipid Rafts

Maksumova

Muratkhodjaev

et al. 2005

The Journal of Immunology

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A role for the receptor protein tyrosine phosphatase α (PTPα) in immune cell function and regulation of Src family kinases was investigated using thymocytes from PTPα-deficient mice. PTPα-null thymocytes develop normally, but unstimulated PTPα−/− cells exhibit increased tyrosine phosphorylation of specific proteins, increased Fyn activity, and hyperphosphorylation of Cbp/PAG that promotes its association with C-terminal Src kinase. Elevated Fyn activity in the absence of PTPα is due to enhanced phosphorylation of Fyn tyrosines 528 and 417. Some PTPα is localized in lipid rafts of thymocytes, and raft-associated Fyn is specifically activated in PTPα−/− cells. PTPα is not a Cbp/PAG phosphatase, because it is not required for Cbp/PAG dephosphorylation in unstimulated or anti-CD3-stimulated thymocytes. Together, our results indicate that PTPα, likely located in lipid rafts, regulates the activity of raft Fyn. In the absence of PTPα this population of Fyn is activated and phosphorylates Cbp/PAG to enhance association with C-terminal Src kinase. Although TCR-mediated tyrosine phosphorylation was apparently unaffected by the absence of PTPα, the long-term proliferative response of PTPα−/− thymocytes was reduced. These findings indicate that PTPα is a component of the complex Src family tyrosine kinase regulatory network in thymocytes and is required to suppress Fyn activity in unstimulated cells in a manner that is not compensated for by the major T cell PTP and SFK regulator, CD45.

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“…Efficient TCR signaling following T cell activation requires conjugate formation with an APC (38). The hyporesponsive state of orally tolerized T cells may be due to inefficient conjugate formation.…”

Section: Orally Tolerized T Cells Can Form Stable Conjugates With Apcsmentioning

confidence: 99%

Orally Tolerized T Cells Can Form Conjugates with APCs but Are Defective in Immunological Synapse Formation

Ise

Nakamura

Shimizu

et al. 2005

The Journal of Immunology

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Oral tolerance is systemic immune hyporesponsiveness induced by the oral administration of soluble Ags. Hyporesponsiveness of Ag-specific CD4 T cells is responsible for this phenomenon. However, the molecular mechanisms underlying the hyporesponsive state of these T cells are not fully understood. In the present study, we investigated the ability of orally tolerized T cells to form conjugates with Ag-bearing APCs and to translocate TCR, protein kinase C-θ (PKC-θ), and lipid rafts into the interface between T cells and APCs. Orally tolerized T cells were prepared from the spleens of OVA-fed DO11.10 mice. Interestingly, the orally tolerized T cells did not show any impairment in the formation of conjugates with APCs. The conjugates were formed in a LFA-1-dependent manner. Upon antigenic stimulation, the tolerized T cells could indeed activate Rap1, which is critical for LFA-1 activation and thus cell adhesion. However, orally tolerized T cells showed defects in the translocation of TCR, PKC-θ, and lipid rafts into the interface between T cells and APCs. Translocation of TCR and PKC-θ to lipid raft fractions upon antigenic stimulation was also impaired in the tolerized T cells. Ag-induced activation of Vav, Rac1, and cdc42, which are essential for immunological synapse and raft aggregation, were down-regulated in orally tolerized T cells. These results demonstrate that orally tolerized T cells can respond to specific Ags in terms of conjugate formation but not with appropriate immunological synapse formation. This may account for the hyporesponsive state of orally tolerized T cells.

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Regulation of integrin function by T cell activation

Cited by 25 publications

References 146 publications

Perlecan Domain IV Peptide Stimulates Salivary Gland Cell AssemblyIn Vitro

Perlecan Domain IV Peptide Stimulates Salivary Gland Cell AssemblyIn Vitro

Protein Tyrosine Phosphatase α Regulates Fyn Activity and Cbp/PAG Phosphorylation in Thymocyte Lipid Rafts

Orally Tolerized T Cells Can Form Conjugates with APCs but Are Defective in Immunological Synapse Formation

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