T-Lymphocyte Interactions With Endothelium and Extracellular Matrix

Hunt, S.; Harris, Estelle S.; Kellermann, Sirid Aimée; Shimizu, Yoji

doi:10.1177/10454411960070010501

Cited by 18 publications

(17 citation statements)

References 197 publications

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“…In addition, this study undertook an immunohistochemical analysis of adhesion molecule expression by endothelial cells of the conjunctival vasculature, looking particularly for evidence of adhesion molecules found on HEVs at other sites in the body namely Vascular Adhesion Protein-1 (VAP-1) found in lymph node HEVs (Salmi, Kalimo and Jalkanen, 1993) and Mucosal Addressin Cell Adhesion Molecule-1 (MadCAM-1) found in Peyer's patches and gut lamina propria HEVs (Hunt et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Human Conjunctiva Contains High Endothelial Venules That Express Lymphocyte Homing Receptors

Haynes

Tighe

Scott

et al. 1999

Experimental Eye Research

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Section: Introductionmentioning

confidence: 99%

Human Conjunctiva Contains High Endothelial Venules That Express Lymphocyte Homing Receptors

Haynes

Tighe

Scott

et al. 1999

Experimental Eye Research

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“…1 Overexpression and altered glycosylation of mucins on cancer cells, compared with normal cells, makes them ideal candidates for tumor-based vaccines. 2,3 CD43 is one such member of the mucin family, 4 and is widely expressed on the surface of hematopoietic cells.…”

Section: Introductionmentioning

confidence: 99%

Signaling through CD43 regulates CD4 T-cell trafficking

Mody

Cannon

Bandukwala

et al. 2007

Blood

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The mucin-like protein CD43 is excluded from the immune synapse, and regulates T-cell proliferation as well as T-cell migration. While the CD43 cytoplasmic domain is necessary for regulation of T-cell activation and proliferation, the mechanism via which CD43 regulates trafficking is not well defined. To investigate whether CD43 phosphorylation regulates its function in T cells, we used tandem mass spectrometry and identified Ser76 in murine CD43 as a previously unidentified site of basal phosphorylation. Interestingly, mutation of this single serine to alanine greatly diminishes T-cell trafficking to the lymph node, while CD43 exclusion and CD43-mediated regulation of T-cell proliferation remain intact. Furthermore, the CD43 extracellular domain was also required for T-cell trafficking, providing a hitherto unknown function for the extracellular domain, and suggesting that the extracellu- IntroductionCell-surface mucins, characterized by large, highly glycosylated extracellular domains, are important regulators of tumor progression as well as lymphocyte trafficking. 1 Overexpression and altered glycosylation of mucins on cancer cells, compared with normal cells, makes them ideal candidates for tumor-based vaccines. 2,3 CD43 is one such member of the mucin family, 4 and is widely expressed on the surface of hematopoietic cells. 5 Reduced expression and aberrant glycosylation of CD43 is found on the T cells of patients suffering from Wiskott-Aldrich syndrome, 6-8 as well as HIV infection. 9,10 In contrast, CD43 is overexpressed on lymphomas and leukemias, and while not normally expressed on nonhematopoietic cells, it is present on colon adenomas and carcinomas. 11,12 In spite of its abundance on T cells, the precise function of CD43 remains elusive. T cells from CD43 Ϫ/Ϫ mice exhibit increased proliferation and adhesion in vitro, 13,14 and increased immune responses in vivo. 15 Strikingly, CD43 is excluded from the immune synapse of activated T cells, 16 and often localizes to a protein complex distal to the antigen-presenting cell (APC) contact site, referred to as the distal pole complex (DPC). 17,18 Several groups have reported that failure to exclude CD43 results in inhibition of IL-2 production. 19,20 Based on these data, CD43 has been characterized as a negative regulator of T-cell function.The prevailing hypothesis to explain the mechanism of CD43-mediated negative regulation was that the CD43 extracellular domain acted as a barrier to cell-to-cell interactions. 13,[21][22][23] However, we and others have shown that the cytoplasmic domain is not only necessary, but also sufficient for movement of CD43 away from the immunologic synapse, as well as CD43-mediated attenuation of T-cell proliferation and homotypic adhesion. 14,17,20 These data underscore a critical function for the CD43 cytoplasmic tail in regulating T-cell proliferation and adhesion. Despite significant progress in elucidating the function of the CD43 cytoplasmic tail, there is no well-defined function for its extracellular domain. In the abs...

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“…The composition of extracellular matrix differs between tissues and constitutes an organ-specific microenvironment with the ability to recruit and retain specific cell types (Hunt et al, 1996). Pathological conditions, including inflammation and cancer are associated with changes in the composition of extracellular matrix (Rojkind, 1988), and thus changes in the potential to recruit or retain inflammatory cells.…”

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confidence: 99%

Vitronectin in human hepatic tumours contributes to the recruitment of lymphocytes in an αvβ3-independent manner

et al. 2006

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The degree of lymphocyte infiltration is a prognostic factor in liver cancer, but to date the mechanisms by which lymphocytes infiltrate into and are retained in hepatic tumours are poorly understood. We hypothesised that the extracellular matrix glycoprotein vitronectin, a major component of the stroma of hepatic tumours, might play a role in the recruitment and retention of tumourinfiltrating lymphocytes (TIL). Thus, we investigated the ability of vitronectin to support migration and adhesion of TIL isolated from hepatocellular carcinoma and colorectal hepatic metastases. Soluble vitronectin-induced dose-dependent migration of TIL in in vitro chemotaxis and haptotaxis assays and vitronectin in tissue sections was able to support TIL adhesion to tumour stroma. Neither adhesion nor migration was inhibited by a function blocking mAb against the major vitronectin receptor avb3 and we were unable to detect avb3 on TIL in vitro or in vivo on tumour tissue. However, TIL did express high levels of urokinase-type plasminogen activator receptor (uPAR) and inhibitory antibodies and amiloride both significantly inhibited TIL adhesion to vitronectin and reduced transendothelial migration of lymphocytes across liver endothelium in vitro. Thus, we provide evidence that vitronectin in liver tumours can support the recruitment and retention of effector lymphocytes by an uPAR-dependent mechanism.

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T-Lymphocyte Interactions With Endothelium and Extracellular Matrix

Cited by 18 publications

References 197 publications

Human Conjunctiva Contains High Endothelial Venules That Express Lymphocyte Homing Receptors

Human Conjunctiva Contains High Endothelial Venules That Express Lymphocyte Homing Receptors

Signaling through CD43 regulates CD4 T-cell trafficking

Vitronectin in human hepatic tumours contributes to the recruitment of lymphocytes in an αvβ3-independent manner

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