Academic literature on the topic 'GP90 lymphocyte homing/adhesion receptor'

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Journal articles on the topic "GP90 lymphocyte homing/adhesion receptor"

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Mobley, J. L., and M. O. Dailey. "Regulation of adhesion molecule expression by CD8 T cells in vivo. I. Differential regulation of gp90MEL-14 (LECAM-1), Pgp-1, LFA-1, and VLA-4 alpha during the differentiation of cytotoxic T lymphocytes induced by allografts." Journal of Immunology 148, no. 8 (1992): 2348–56. http://dx.doi.org/10.4049/jimmunol.148.8.2348.

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Abstract A variety of adhesion molecules regulate the traffic and tissue localization of lymphocytes in vivo by mediating their binding to vascular endothelial cells. The homing receptor gp90MEL-14 (gp90), also known as LECAM-1 or L-selectin, mediates the adhesion of lymphocytes to specialized high endothelial venules in lymph nodes (LN) and is the primary molecule regulating lymphocyte recirculation and homing to LN, whereas other adhesion molecules have a major role in the localization of lymphocytes in inflammatory sites. We used four-color flow cytometric analysis to examine the regulation
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Pals, S. T., F. Hogervorst, G. D. Keizer, T. Thepen, E. Horst, and C. C. Figdor. "Identification of a widely distributed 90-kDa glycoprotein that is homologous to the Hermes-1 human lymphocyte homing receptor." Journal of Immunology 143, no. 3 (1989): 851–57. http://dx.doi.org/10.4049/jimmunol.143.3.851.

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Abstract Homing of recirculating lymphocytes from the blood into the lymphoid tissues is mediated by 90-kDa homing receptors on the lymphocyte cell surface, allowing selective binding to specialized endothelium lining high endothelial venules. This study describes two novel mAb, NKI-P1 and NKI-P2, directed against functional epitopes of a human lymphocyte homing receptor, gp90. Biochemical studies demonstrated that these antibodies recognize a 90-kDa glycoprotein which is similar to the Ag recognized by the mAb Hermes-1. This notion was confirmed by immunohistochemical studies showing identica
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Jung, T. M., and M. O. Dailey. "Rapid modulation of homing receptors (gp90MEL-14) induced by activators of protein kinase C. Receptor shedding due to accelerated proteolytic cleavage at the cell surface." Journal of Immunology 144, no. 8 (1990): 3130–36. http://dx.doi.org/10.4049/jimmunol.144.8.3130.

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Abstract Lymphocyte entry into lymph nodes and Peyer's patches is initiated by the adhesion of the lymphocytes to specialized postcapillary high endothelial venules (HEV). The binding of lymphocytes to lymph node HEV is mediated by the cell surface receptor gp90MEL-14 (gp90). Previous work has shown that gp90 is down-regulated over a period of days after mitogenic or mixed lymphocyte reaction stimulation of T lymphocytes. In our study, it is shown that stimulation of lymphocytes with activators of protein kinase C (PKC), such as PMA or 1-oleoyl 2-acetyl-glycerol, results in the nearly complete
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Hamann, A., D. Jablonski-Westrich, A. Duijvestijn, et al. "Evidence for an accessory role of LFA-1 in lymphocyte-high endothelium interaction during homing." Journal of Immunology 140, no. 3 (1988): 693–99. http://dx.doi.org/10.4049/jimmunol.140.3.693.

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Abstract In a variety of lymphocyte interactions, lymphocyte function-associated antigen-1 (LFA-1) plays an important role as an accessory mechanism mediating cell adhesion. We tested the possibility that LFA-1 could also be involved in the specific binding of lymphocytes to high endothelial venules (HEV) during homing. Antibodies against LFA-1 but not against various other cell surface molecules (except the putative gp90 homing receptor defined by the MEL-14 antibody) were found to inhibit in vitro adherence of lymphocytes to HEV in frozen sections of lymph nodes. Binding of T cell lines to H
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Bowen, B. R., T. Nguyen, and L. A. Lasky. "Characterization of a human homologue of the murine peripheral lymph node homing receptor." Journal of Cell Biology 109, no. 1 (1989): 421–27. http://dx.doi.org/10.1083/jcb.109.1.421.

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Lymphocyte trafficking is a fundamental aspect of the immune system that allows B and T lymphocytes with diverse antigen recognition specificities to be exposed to various antigenic stimuli in spatially distinct regions of an organism. A lymphocyte adhesion molecule that is involved with this trafficking phenomenon has been termed the homing receptor. Previous work (Lasky, L., T. Yednock, M. Singer, D. Dowbenko, C. Fennie, H. Rodriguez, T. Nguyen, S. Stachel, and S. Rosen. 1989. Cell. 56:1045-1055) has characterized a cDNA clone encoding a murine homing receptor that is involved in trafficking
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Imai, Y., M. S. Singer, C. Fennie, L. A. Lasky, and S. D. Rosen. "Identification of a carbohydrate-based endothelial ligand for a lymphocyte homing receptor." Journal of Cell Biology 113, no. 5 (1991): 1213–21. http://dx.doi.org/10.1083/jcb.113.5.1213.

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Lymphocyte attachment to high endothelial venules within lymph nodes is mediated by the peripheral lymph node homing receptor (pnHR), originally defined on mouse lymphocytes by the MEL-14 mAb. The pnHR is a calcium-dependent lectin-like receptor, a member of the LEC-CAM family of adhesion proteins. Here, using a soluble recombinant form of the homing receptor, we have identified an endothelial ligand for the pnHR as an approximately 50-kD sulfated, fucosylated, and sialylated glycoprotein, which we designate Sgp50 (sulfated glycoprotein of 50 kD). Recombinant receptor binding to this lymph nod
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Geoffroy, J. S., and S. D. Rosen. "Demonstration that a lectin-like receptor (gp90MEL) directly mediates adhesion of lymphocytes to high endothelial venules of lymph nodes." Journal of Cell Biology 109, no. 5 (1989): 2463–69. http://dx.doi.org/10.1083/jcb.109.5.2463.

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Lymphocyte migration from the blood into most secondary lymphoid organs is initiated by a highly selective adhesive interaction with the endothelium of specialized blood vessels known as high endothelial venules (HEV). The propensity of lymphocytes to migrate to particular lymphoid organs is known as lymphocyte homing, and the receptors on lymphocytes that dictate interactions with HEV at particular anatomical sites are designated "homing receptors". Based upon antibody blockade experiments and cell-type distribution studies, a prominent candidate for the peripheral lymph node homing receptor
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Zhou, D. F., J. F. Ding, L. J. Picker, R. F. Bargatze, E. C. Butcher, and D. V. Goeddel. "Molecular cloning and expression of Pgp-1. The mouse homolog of the human H-CAM (Hermes) lymphocyte homing receptor." Journal of Immunology 143, no. 10 (1989): 3390–95. http://dx.doi.org/10.4049/jimmunol.143.10.3390.

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Abstract Mouse phagocytic glycoprotein-1 (Pgp-1; Ly-24) is a 95-kDa glycoprotein of unknown function that has served as an important T cell/leukocyte differentiation marker. Recent work has suggested that it may be related to a human 85- to 95-kDa glycoprotein (termed variously the Hermes Ag/lymphocyte homing receptor, ECMRIII, P80, and CD44) that is involved in lymphocyte binding to high endothelial venules in the process of lymphocyte homing, and has been implicated in other cell adhesion events. The widespread expression of this molecular class in diverse organ systems suggests a broad role
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Brown, T. A., T. Bouchard, T. St John, E. Wayner, and W. G. Carter. "Human keratinocytes express a new CD44 core protein (CD44E) as a heparan-sulfate intrinsic membrane proteoglycan with additional exons." Journal of Cell Biology 113, no. 1 (1991): 207–21. http://dx.doi.org/10.1083/jcb.113.1.207.

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We previously identified a 90-kD (GP90), collagen-binding, membrane glycoprotein, termed extracellular matrix receptor III (ECMR III), that is homologous to the lymphocyte homing receptor and CD44 antigen (Gallatin, W. M., E. A. Wayner, P. A. Hoffman, T. St. John, E. C. Butcher, and W. G. Carter. 1989. Proc. Natl. Acad. Sci. USA. 86:4654-4658). CD44 is abundantly expressed in many epithelial tissues, and is localized predominantly to filopodia in cultured keratinocytes. Here we establish CD44 as a polymorphic family of related membrane proteoglycans and glycoproteins possessing extensive diver
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Berlin-Rufenach, Cornelia, Florian Otto, Meg Mathies, et al. "Lymphocyte Migration in Lymphocyte Function-associated Antigen (LFA)-1–deficient Mice." Journal of Experimental Medicine 189, no. 9 (1999): 1467–78. http://dx.doi.org/10.1084/jem.189.9.1467.

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Using lymphocyte function-associated antigen (LFA)-1−/− mice, we have examined the role of LFA-1 and other integrins in the recirculation of lymphocytes. LFA-1 has a key role in migration to peripheral lymph nodes (pLNs), and influences migration into other LNs. Second, the α4 integrins, α4β7 and α4β1, have a hitherto unrecognized ability to compensate for the lack of LFA-1 in migration to pLNs. These findings are confirmed using normal mice and blocking LFA-1 and α4 monoclonal antibodies. Unexpectedly, vascular cell adhesion molecule (VCAM)-1, which is essential in inflammatory responses, ser
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Book chapters on the topic "GP90 lymphocyte homing/adhesion receptor"

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Rosen, S. D. "A Lymphocyte Homing Receptor: A Member of an Emerging Class of Cell Adhesion Molecules." In Progress in Immunology. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-83755-5_21.

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