Signal Transduction via CD44: Role of Plasma Membrane Microdomains

References

• Borland G., Ross J. A., Guy K. Forms and functions of CD44. Immunology 1998; 93: 139–148
   PubMed Web of Science ®Google Scholar
• Lesley J., Hyman R., English N., Catterall J. B., Turner G. A. CD44 in inflammation and metastasis. Glycoconjugate Journal 1997; 14: 611–622
   PubMed Web of Science ®Google Scholar
• Naor D., Sionov R. V., Ish-Shalom D. CD44: structure, function, and association with the malignant process. Advances in Cancer Research 1997; 71: 241–319
   PubMed Web of Science ®Google Scholar
• Haynes B. F., Telen M. J., Hale L. P., Denning S. M. CD44-a molecule involved in leukocyte adherence and T-cell activation. Immunology Today 1989; 10: 423–428
   PubMedGoogle Scholar
• Aruffo A. CD44: one ligand, two functions. Journal of Clinical Investigation 1996; 98: 2191–2192
   PubMed Web of Science ®Google Scholar
• Huet S., Groux H., Caillou B., Valentin H., Prieur A. M., Bernard A. CD44 contributes to T cell activation. Journal of Immunology 1989; 143: 798–801
   PubMed Web of Science ®Google Scholar
• Shimizu Y., Van Seventer G. A., Siraganian R., Wahl L., Shaw S. Dual role of the CD44 molecule in T cell adhesion and activation. Journal of Immunology 1989; 143: 2457–2463
   PubMed Web of Science ®Google Scholar
• Rothman B. L., Blue M. L., Kelley K. A., Wunderlich D., Mierz D. V., Aune T. M. Human T cell activation by OKT3 is inhibited by a monoclonal antibody to CD44. Journal of Immunology 1991; 147: 2493–2499
   PubMed Web of Science ®Google Scholar
• Denning S. M., Le P. T., Singer K. H., Haynes B. F. Antibodies against the CD44 p80, lymphocyte homing receptor molecule augment human peripheral blood T cell activation. Journal of Immunology 1990; 144: 7–15
   PubMed Web of Science ®Google Scholar
• Conrad P., Rothman B. L., Kelley K. A., Blue M. L. Mechanism of peripheral T cell activation by coengagement of CD44 and CD2. Journal of Immunology 1992; 149: 1833–1839
   PubMed Web of Science ®Google Scholar
• Pierres A., Lipcey C., Mawas C., Olive D. A unique CD44 monoclonal antibody identifies a new T cell activation pathway. European Journal of Immunology 1992; 22: 413–417
   PubMed Web of Science ®Google Scholar
• Guo Y. J., Lin S. C., Wang J. H., Bigby M., Sy M. S. Palmitoylation of CD44 interferes with CD3-mediated signaling in human T lymphocytes. International Immunology 1994; 6: 213–221
   PubMed Web of Science ®Google Scholar
• Galluzzo E., Albi N., Fiorucci S., Merigiola C., Ruggeri L., Tosti A., Grossi C. E., Velardi A. Involvement of CD44 variant isoforms in hyaluronate adhesion by human activated T cells. European Journal of Immunology 1995; 25: 2932–2939
   PubMed Web of Science ®Google Scholar
• Galandrini R., Albi N., Tripodi G., Zarcone D., Terenzi A., Moretta A., Grossi C. E., Velardi A. Antibodies to CD44 trigger effector functions of human T cell clones. Journal of Immunology 1993; 150: 4225–4235
   PubMed Web of Science ®Google Scholar
• Naujokas M. F., Morin M., Anderson M. S., Peterson M., Miller J. The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44. Cell 1993; 74: 257–268
   PubMed Web of Science ®Google Scholar
• Guo Y. J., Ma J., Wong J. H., Lin S. C., Chang H. C., Bigby M., Sy M. S. Monoclonal anti-CD44 antibody acts in synergy with anti-CD2 but inhibits anti-CD3 or T cell receptor-mediated signaling in murine T cell hybridomas. Cellular Immunology 1993; 152: 186–199
   PubMed Web of Science ®Google Scholar
• Sommer F., Huber M., Rollinghoff M., Lohoff M. CD44 plays a co-stimulatory role in murine T cell activation: ligation of CD44 selectively co-stimulates IL-2 production, but not proliferation in TCR-stimulated murine Thl cells. International Immunology 1995; 7: 1779–1786
   PubMed Web of Science ®Google Scholar
• Ayroldi E., Cannarile L., Migliorati G., Bartoli A., Nicoletti I., Riccardi C. CD44 (Pgp-1) inhibits CD3 and dexamethasone-induced apoptosis. Blood 1995; 86: 2672–2678
   PubMed Web of Science ®Google Scholar
• Seth A., Gote L., Nagarkatti M., Nagarkatti P. S. T-cell-receptor-independent activation of cytolytic activity of cytotoxic T lymphocytes mediated through CD44 and gp90MEL-14. Proceedings of the National Academy of Sciences USA 1991; 88: 7877–7881
   PubMed Web of Science ®Google Scholar
• Tan P. H., Santos E. B., Rossbach H. C., Sandmaier B. M. Enhancement of natural killer activity by an antibody to CD44. Journal of Immunology 1993; 150: 812–820
   PubMed Web of Science ®Google Scholar
• Galandrini R., De Maria R., Piccoli M., Frati L., Santoni A. CD44 triggering enhances human NK cell cytotoxic functions. Journal of Immunology 1994; 153: 4399–4407
   PubMed Web of Science ®Google Scholar
• Pericle F., Sconocchia G., Titus J. A., Segal D. M. CD44 is a cytotoxic triggering molecule on human polymorphonuclear cells. Journal of Immunology 1996; 157: 4657–4663
   PubMed Web of Science ®Google Scholar
• Toyama-Sorimachi N., Sorimachi H., Tobita Y., Kitamura F., Yagita H., Suzuki K., Miyasaka M. A novel ligand for CD44 is serglycin, a hematopoietic cell lineage- specific proteoglycan. Possible involvement in lymphoid cell adherence and activation. Journal of Biological Chemistry 1995; 270: 7437–7444
   PubMed Web of Science ®Google Scholar
• Webb D. S., Shimizu Y., Van Seventer G. A., Shaw S., Gerrard T. L. LFA-3, CD44, and CD45: physiologic triggers of human monocyte TNF and IL-1 release. Science 1990; 249: 1295–1297
   PubMed Web of Science ®Google Scholar
• Gruber M. F., Webb D. S., Gerrard T. L. Stimulation of human monocytes via CD45, CD44, and LFA-3 triggers macrophage-colony-stimulating factor production. Synergism with lipopolysaccharide and IL-1 beta. Journal of Immunology 1992; 148: 1113–1118
   PubMed Web of Science ®Google Scholar
• Chong A. S., Boussy I. A., Graf L. H., Scuderi P. Stimulation of IFN-gamma, TNF-alpha, and TNF-beta secretion in IL-2- activated T cells: costimulatory roles for LFA-1, LFA-2, CD44, and CD45 molecules. Cellular Immunology 1992; 144: 69–79
   PubMed Web of Science ®Google Scholar
• Haegel-Kronenberger H., de la Salle H., Bohbot A., Oberling F., Cazenave J. P., Hanau D. Adhesive and/or signaling functions of CD44 isoforms in human dendritic cells. Journal of Immunology 1998; 161: 3902–3911
   PubMed Web of Science ®Google Scholar
• Noble P. W., Lake F. R., Henson P. M., Riches D. W. Hyaluronate activation of CD44 induces insulin-like growth factor- expression by a tumor necrosis factor-alpha-dependent mechanism in murine macrophages. Journal of Clinical Investigation 1993; 91: 2368–2377
   PubMed Web of Science ®Google Scholar
• Rafi A., Nagarkatti M., Nagarkatti P. S. Hyaluronate-CD44 interactions can induce murine B-cell activation. Blood 1997; 89: 2901–2908
   PubMed Web of Science ®Google Scholar
• McKee C. M., Penno M. B., Cowman M., Burdick M. D., Strieter R. M., Bao C., Noble P. W. Hyaluronan (HA) fragments induce chemokine gene expression in alveolar macrophages. The role of HA size and CD44. Journal of Clinical Investigation 1996; 98: 2403–2413
   PubMed Web of Science ®Google Scholar
• McKee C. M., Lowenstein C. J., Horton M. R., Wu J., Bao C., Chin B. Y., Choi A. M., Noble P. W. Hyaluronan fragments induce nitric-oxide synthase in murine macrophages through a nuclear factor kappaB-dependent mechanism. Journal of Biological Chemistry 1997; 272: 8013–8
   PubMed Web of Science ®Google Scholar
• Horton M. R., McKee C. M., Bao C., Liao F., Farber J. M., Hodge-DuFour J., Pure E., Oliver B. L., Wright T. M., Noble P. W. Hyaluronan fragments synergize with interferon-gamma to induce the C-X-C chemokines mig and interferon-inducible protein-10 in mouse macrophages. Journal of Biological Chemistry 1998; 273: 35088–94
   PubMed Web of Science ®Google Scholar
• West D. C., Kumar S. The effect of hyaluronate and its oligosaccharides on endothelial cell proliferation and monolayer integrity. Experimental Cell Research 1989; 183: 179–196
   PubMed Web of Science ®Google Scholar
• Slevin M., Krupinski J., Kumar S., Gaffney J. Angiogenic oligosaccharides of hyaluronan induce protein tyrosine kinase activity in endothelial cells and activate a cytoplasmic signal transduction pathway resulting in proliferation. Laboratory Investigation 1998; 78: 987–1003
   PubMed Web of Science ®Google Scholar
• Fujii K., Tanaka Y., Hubscher S., Saito K., Ota T., Eto S. Cross-Linking of CD44 on Rheumatoid Synovial Cells Up-Regulates VCAM-1. Journal of Immunology 1999; 162: 2391–2398
   PubMed Web of Science ®Google Scholar
• Weber G. F., Ashkar S., Glimcher M. J., Cantor H. Receptor-ligand interaction between CD44 and osteopontin (Eta-1). Science 1996; 271: 509–512
   PubMed Web of Science ®Google Scholar
• Lesley J., Hyman R., Kincade P. W. CD44 and its interaction with extracellular matrix. Advances in Immunology 1993; 54: 271–335
   PubMed Web of Science ®Google Scholar
• Yashiro Y., Tai X. G., Toyo-Oka K., Park C. S., Abe R., Hamaoka T., Kobayashi M., Neben S., Fujiwara H. A fundamental difference in the capacity to induce proliferation of naive T cells between CD28 and other co-stimulatory molecules. European Journal of Immunology 1998; 28: 926–935
   PubMed Web of Science ®Google Scholar
• Sconocchia G., Titus J. A., Segal D. M. CD44 is a cytotoxic triggering molecule in human peripheral blood NK cells. Journal of Immunology 1994; 153: 5473–5481
   PubMed Web of Science ®Google Scholar
• Tan P. H., Liu Y., Santos E. B., Sandmaier B. M. Mechanisms of enhancement of natural killer activity by an antibody to CD44: increase in conjugate formation and release of tumor necrosis factor alpha. Cellular Immunology 1995; 164: 255–264
   PubMed Web of Science ®Google Scholar
• Galandrini R., Piccoli M., Frati L., Santoni A. Tyrosine kinase-dependent activation of human NK cell functions upon triggering through CD44 receptor. European Journal of Immunology 1996; 26: 2807–2811
   PubMed Web of Science ®Google Scholar
• Aruffo A., Stamenkovic I., Melnick M., Underhill C. B., Seed B. CD44 is the principal cell surface receptor for hyaluronate. Cell 1990; 61: 1303–1313
   PubMed Web of Science ®Google Scholar
• Lesley J., Kincade P. W., Hyman R. Antibody-induced activation of the hyaluronan receptor function of CD44 requires multivalent binding by antibody. European Journal of Immunology 1993; 23: 1902–1909
   PubMed Web of Science ®Google Scholar
• Pure E., Camp R. L., Peritt D., Panettieri R. A., Jr., Lazaar A. L., Nayak S. Defective phosphorylation and hyaluronate binding of CD44 with point mutations in the cytoplasmic domain. Journal of Experimental Medicine 1995; 181: 55–62
   PubMed Web of Science ®Google Scholar
• Lokeshwar V. B., Fregien N., Bourguignon L. Y. Ankyrin-binding domain of CD44(GP85) is required for the expression of hyaluronic acid-mediated adhesion function. Journal of Cell Biology 1994; 126: 1099–1109
   PubMed Web of Science ®Google Scholar
• Liu D., Sy M. S. A cysteine residue located in the transmembrane domain of CD44 is important in binding of CD44 to hyaluronic acid. Journal of Experimental Medicine 1996; 183: 1987–1994
   PubMed Web of Science ®Google Scholar
• Liu D., Sy M. S. Phorbol myristate acetate stimulates the dimerization of CD44 involving a cysteine in the transmembrane domain. Journal of Immunology 1997; 159: 2702–2711
   PubMed Web of Science ®Google Scholar
• DeGrendele H. C., Kosfiszer M., Estess P., Siegelman M. H. CD44 activation and associated primary adhesion is inducible via T cell receptor stimulation. Journal of Immunology 1997; 159: 2549–2553
   PubMed Web of Science ®Google Scholar
• Noble P. W., McKee C. M., Cowman M., Shin H. S. Hyaluronan fragments activate an NF-kappa B/I-kappa B alpha autoregulatory loop in murine macrophages. Journal of Experimental Medicine 1996; 183: 2373–8
   PubMed Web of Science ®Google Scholar
• Underhill C. B., Chi-Rosso G., Toole B. P. Effects of detergent solubilization on the hyaluronate-binding protein from membranes of simian virus 40-transformed 3T3 cells. Journal of Biological Chemistry 1983; 258: 8086–8091
   PubMed Web of Science ®Google Scholar
• Galandrini R., Albi N., Vecchiarelli A., Tognellini R., Zarcone D., Grossi C. E., Velardi A. Ligation of the lymphocyte homing receptor CD44 triggers T-helper and cytolytic functions of human T cells. Cytotechnology 1993; 11: S100–S102
   Web of Science ®Google Scholar
• Sconocchia G., Titus J. A., Segal D. M. Signaling pathways regulating CD44-dependent cytolysis in natural killer cells. Blood 1997; 90: 716–725
   PubMed Web of Science ®Google Scholar
• Skubitz K. M., Campbell K. D., Skubitz A. P. Tyrosine kinase activity is associated with CD44 in human neutrophils. FEBS Letters 1998; 439: 97–100
   PubMed Web of Science ®Google Scholar
• Taher T. E., Smit L., Griffioen A. W., Schilder-Tol E. J., Borst J., Pals S. T. Signaling through CD44 is mediated by tyrosine kinases. Association with p561ck in T lymphocytes. Journal of Biological Chemistry 1996; 271: 2863–2867
   PubMed Web of Science ®Google Scholar
• Ilangumaran S., Briol A., Hoessli D. C. CD44 selectively associates with active Src family protein tyrosine kinases Lck and Fyn in glycosphingolipid-rich plasma membrane domains of human peripheral blood lymphocytes. Blood 1998; 91: 3901–3908
   PubMed Web of Science ®Google Scholar
• Bourguignon L. Y., Zhu H., Chu A., Iida N., Zhang L., Hung M. C. Interaction between the adhesion receptor, CD44, and the oncogene product, p185HER2, promotes human ovarian tumor cell activation. Journal of Biological Chemistry 1997; 272: 27913–27918
   PubMed Web of Science ®Google Scholar
• Pawson T. Protein modules and signalling networks. Nature 1995; 373: 573–80
   PubMed Web of Science ®Google Scholar
• Tarone G., Ferracini R., Galetto G., Comoglio P. A cell surface integral membrane glycoprotein of 85,000 mol wt (gp85) associated with triton X-100-insoluble cell skeleton. Journal of Cell Biology 1984; 99: 512–9
   PubMed Web of Science ®Google Scholar
• Lacy B. E., Underhill C. B. The hyaluronate receptor is associated with actin filaments. Journal of Cell Biology 1987; 105: 1395–1404
   PubMed Web of Science ®Google Scholar
• Carter W. G., Wayner E. A. Characterization of the class III collagen receptor, a phosphorylated, transmembrane glycoprotein expressed in nucleated human cells. Journal of Biological Chemistry 1988; 263: 4193–201
   PubMed Web of Science ®Google Scholar
• Kalomiris E. L., Bourguignon L. Y. Mouse T lymphoma cells contain a transmembrane glycoprotein (GP85) that binds ankyrin. Journal of Cell Biology 1988; 106: 319–27
   PubMed Web of Science ®Google Scholar
• Neame S. J., Isacke C. M. The cytoplasmic tail of CD44 is required for basolateral localization in epithelial MDCK cells but does not mediate association with the detergent-insoluble cytoskeleton of fibroblasts. Journal of Cell Biology 1993; 121: 1299–1310
   PubMed Web of Science ®Google Scholar
• Tsukita S., Oishi K., Sato N., Sagara J., Kawai A. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. Journal of Cell Biology 1994; 126: 391–401
   PubMed Web of Science ®Google Scholar
• Perschl A., Lesley J., English N., Hyman R., Trowbridge I. S. Transmembrane domain of CD44 is required for its detergent insolubility in fibroblasts. Journal of Cell Science 1995; 108: 1033–1041
   PubMed Web of Science ®Google Scholar
• Neame S. J., Uff C. R., Sheikh H., Wheatley S. C., Isacke C. M. CD44 exhibits a cell type dependent interaction with triton X-100 insoluble, lipid rich, plasma membrane domains. Journal of Cell Science 1995; 108: 3127–3135
   PubMed Web of Science ®Google Scholar
• Simons K., Ikonen E. Functional rafts in cell membranes. Nature 1997; 387: 569–572
   PubMed Web of Science ®Google Scholar
• Brown D. A., London E. Functions of lipid rafts in biological membranes. Annual Reviews in Cell and Developmental Biology 1998; 14: 111–136
   PubMed Web of Science ®Google Scholar
• Low M. G. The glycosyl-phosphatidylinositol anchor of membrane proteins. Biochimica Biophysica Acta 1989; 988: 427–54
   PubMed Web of Science ®Google Scholar
• Robinson P. J. Phosphatidylinositol membrane anchors and T-cell activation. Immunology Today 1991; 12: 35–41
   PubMedGoogle Scholar
• Hoessli D., Rungger-Brandle E. Association of specific cell-surface glycoproteins with a triton X-100-resistant complex of plasma membrane proteins isolated from T-lymphoma cells (P1798). Experimental Cell Research 1985; 156: 239–50
   PubMed Web of Science ®Google Scholar
• Cinek T., Horejsi V. The nature of large non-covalent complexes containing glycosyl- phosphatidylinositol-anchored membrane glycoproteins and protein tyrosine kinases. Journal of Immunology 1992; 149: 2262–70
   PubMed Web of Science ®Google Scholar
• Brown D. A., Rose J. K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992; 68: 533–44
   PubMed Web of Science ®Google Scholar
• Hoessli D. C., Rungger-Brandle E. Isolation of plasma membrane domains from murine T lymphocytes. Proceedings of the National Academy of Sciences USA 1983; 80: 439–43
   PubMed Web of Science ®Google Scholar
• Brown D. A., London E. Structure of detergent-resistant membrane domains: does phase separation occur in biological membranes?. Biochemical and Biophysical Research Communications 1997; 240: 1–7
   PubMed Web of Science ®Google Scholar
• Brown R. E. Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. Journal of Cell Science 1998; 111: 1–9
   PubMed Web of Science ®Google Scholar
• Varma R., Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 1998; 394: 798–801
   PubMed Web of Science ®Google Scholar
• Friedrichson T., Kurzchalia T. V. Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 1998; 394: 802–805
   PubMed Web of Science ®Google Scholar
• Anderson R. G. The caveolae membrane system. Annual Reviews in Biochemistry 1998; 67: 199–225
   PubMed Web of Science ®Google Scholar
• Schnitzer J. E., McIntosh D. P., Dvorak A. M., Liu J., Oh P. Separation of caveolae from associated microdomains of GPI-anchored proteins. Science 1995; 269: 1435–1439
   PubMed Web of Science ®Google Scholar
• Ilangumaran S., Briol A., Hoessli D. C. Distinct interactions among GPI-anchored, transmembrane and membrane associated intracellular proteins, and sphingolipids in lymphocyte and endothelial cell plasma membranes. Biochimica Biophysica Acta 1997; 1328: 227–236
   PubMed Web of Science ®Google Scholar
• Field K. A., Holowka D., Baird B. Fc epsilon RI-mediated recruitment of p53/56lyn to detergent-resistant membrane domains accompanies cellular signaling. Proceedings of the National Academy of Sciences USA 1995; 92: 9201–9205
   PubMed Web of Science ®Google Scholar
• Montixi C., Langlet C., Bernard A. M., Thimonier J., Dubois C., Wurbel M. A., Chauvin J. P., Pierres M., He H. T. Engagement of T cell receptor triggers its recruitment to low-density detergent-insoluble membrane domains. EMBO Journal 1998; 17: 5334–48
   PubMed Web of Science ®Google Scholar
• Deans J. P., Robbins S. M., Polyak M. J., Savage J. A. Rapid redistribution of CD20 to a low density detergent-insoluble membrane compartment. Journal of Biological Chemistry 1998; 273: 344–348
   PubMed Web of Science ®Google Scholar
• Polyak M. J., Tailor S. H., Deans J. P. Identification of a cytoplasmic region of CD20 required for its redistribution to a detergent-insoluble membrane compartment. Journal of Immunology 1998; 161: 3242–3248
   PubMed Web of Science ®Google Scholar
• Melkonian K. A., Ostermeyer A. G., Chen J. Z., Roth M. G., Brown D. A. Role of Lipid Modifications in Targeting Proteins to Detergent-resistant Membrane Rafts. Many raft proteins are acylated, while few are prenylated. Journal of Biological Chemistry 1999; 274: 3910–3917
   PubMed Web of Science ®Google Scholar
• Shenoy-Scaria A. M., Gauen L. K., Kwong J., Shaw A. S., Lublin D. M. Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosylphosphatidylinositol-anchored proteins. Molecular and Cellular Biology 1993; 13: 6385–6392
   PubMed Web of Science ®Google Scholar
• Kabouridis P. S., Magee A. I., Ley S. C. S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes. EMBO Journal 1997; 16: 4983–4998
   PubMed Web of Science ®Google Scholar
• Stefanova I., Horejsi V., Ansotegui I. J., Knapp W., Stockinger H. GPI-anchored cell-surface molecules complexed to protein tyrosine kinases. Science 1991; 254: 1016–9
   PubMed Web of Science ®Google Scholar
• Minoguchi K., Swaim W. D., Berenstein E. H., Siraganian R. P. Src family tyrosine kinase p53/561yn, a serine kinase and Fc epsilon RI associate with alpha-galactosyl derivatives of ganglioside GD1b in rat basophilic leukemia RBL-2H3 cells. Journal of Biological Chemistry 1994; 269: 5249–54
   PubMed Web of Science ®Google Scholar
• Kasahara K., Watanabe Y., Yamamoto T., Sanai Y. Association of Src family tyrosine kinase Lyn with ganglioside GD3 in rat brain. Possible regulation of Lyn by glycosphingolipid in caveolae- like domains. Journal of Biological Chemistry 1997; 272: 29947–29953
   PubMed Web of Science ®Google Scholar
• Harder T., Scheiffele P., Verkade P., Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. Journal of Cell Biology 1998; 141: 929–942
   PubMed Web of Science ®Google Scholar
• Ilangumaran S., Arni S., van Echten-Deckert G., Borisch B., Hoessli D. C. Microdomain-dependent regulation of Lck and fyn protein tyrosine kinases in T lymphocyte plasma membranes. Molecular Biology of the Cell 1999, In press
   PubMed Web of Science ®Google Scholar
• Xavier R., Brennan T., Li Q., McCormack C., Seed B. Membrane compartmentation is required for efficient T cell activation. Immunity 1998; 8: 723–732
   PubMed Web of Science ®Google Scholar
• Zhang W., Sloan-Lancaster J., Kitchen J., Trible R. P., Samelson L. E. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 1998; 92: 83–92
   PubMed Web of Science ®Google Scholar
• Zhang W., Trible R. P., Samelson L. E. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity 1998; 9: 239–246
   PubMed Web of Science ®Google Scholar
• Viola A., Schroeder S., Sakakibara Y., Lanzavecchia A. T Lymphocyte Costimulation Mediated by Reorganization of Membrane Microdomains. Science 1999; 283: 680–682
   PubMed Web of Science ®Google Scholar
• Sperling A. I., Sedy J. R., Manjunath N., Kupfer A., Ardman B., Burkhardt J. K. TCR signaling induces selective exclusion of CD43 from the T cell- antigen-presenting cell contact site. Journal of Immunology 1998; 161: 6459–62
   PubMed Web of Science ®Google Scholar
• Okkenhaug K., Rottapel R. Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain-proline interaction. Journal of Biological Chemistry 1998; 273: 21194–202
   PubMed Web of Science ®Google Scholar
• Stauffer T. P., Meyer T. Compartmentalized IgE receptor-mediated signal transduction in living cells. Journal of Cell Biology 1997; 139: 1447–1454
   PubMed Web of Science ®Google Scholar
• Clausse B., Fizazi K., Walczak V., Tetaud C., Wiels J., Tursz T., Busson P. High concentration of the EBV latent membrane protein 1 in glycosphingolipid-rich complexes from both epithelial and lymphoid cells. Virology 1997; 228: 285–93
   PubMed Web of Science ®Google Scholar
• Kenney J. L., Guinness M. E., Curiel T., Lacy J. Antisense to the epstein-barr virus (EBV)-encoded latent membrane protein 1 (LMP-1) suppresses LMP-1 and bcl-2 expression and promotes apoptosis in EBV-immortalized B cells. Blood 1998; 92: 1721–7
   PubMed Web of Science ®Google Scholar
• Busch L. K., Bishop G. A. The EBV transforming protein, latent membrane protein I, mimics and cooperates with CD40 signaling in B lymphocytes. Journal of Immunology 1999; 162: 2555–2561
   PubMed Web of Science ®Google Scholar
• Bourguignon L. Y., Kalomiris E. L., Lokeshwar V. B. Acylation of the lymphoma transmembrane glycoprotein, GP85, may be required for GP85-ankyrin interaction. Journal of Biological Chemistry 1991; 266: 11761–5
   PubMed Web of Science ®Google Scholar
• Stulnig T. M., Berger M., Sigmund T., Stockinger H., Horejsi V., Waldhausl W. Signal transduction via glycosyl phosphatidylinositol-anchored proteins in T cells is inhibited by lowering cellular cholesterol. Journal of Biological Chemistry 1997; 272: 19242–7
   PubMed Web of Science ®Google Scholar
• Stulnig T. M., Berger M., Sigmund T., Raederstorff D., Stockinger H., Waldhausl W. Polyunsaturated fatty acids inhibit T cell signal transduction by modification of detergent-insoluble membrane domains. Journal of Cell Biology 1998; 143: 637–644
   PubMed Web of Science ®Google Scholar
• DeGrendele H. C., Estess P., Picker L. J., Siegelman M. H. CD44 and its ligand hyaluronate mediate rolling under physiologic flow: a novel lymphocyte-endothelial cell primary adhesion pathway. Journal of Experimental Medicine 1996; 183: 1119–1130
   PubMed Web of Science ®Google Scholar
• DeGrendele H. C., Estess P., Siegelman M. H. Requirement for CD44 in activated T cell extravasation into an inflammatory site. Science 1997; 278: 672–675
   PubMed Web of Science ®Google Scholar
• Clark R. A., Alon R., Springer T. A. CD44 and hyaluronan-dependent rolling interactions of lymphocytes on tonsillar stroma. Journal of Cell Biology 1996; 134: 1075–1087
   PubMed Web of Science ®Google Scholar
• Balazs E. A., Watson D., Duff I. F., Roseman S. Hyaluronic acid in synovial fluid. I. Molecular parameters of hyaluronic acid in normal and arthritis human fluids. Arthritis and Rheumatology 1967; 10: 357–76
   PubMed Web of Science ®Google Scholar
• Saari H., Konttinen Y. T., Tulamo R. M., Antti-Poika I., Honkanen V. Concentration and degree of polymerization of hyaluronate in equine synovial fluid. American journal of Veterinary Research 1989; 50: 2060–3
   PubMed Web of Science ®Google Scholar
• Mikecz K., Brennan F. R., Kim J. H., Giant T. T. Anti-CD44 treatment abrogates tissue oedema and leukocyte infiltration in murine arthritis. Nature Medicine 1995; 1: 558–563
   PubMed Web of Science ®Google Scholar
• Verdrengh M., Holmdahl R., Tarkowski A. Administration of antibodies to hyaluronanreceptor (CD44) delays the start and ameliorates the severity of collagen 11 arthritis. Scandinavian Journal of Immunology 1995; 42: 353–358
   PubMed Web of Science ®Google Scholar
• Okamoto T., Schlegel A., Scherer P. E., Lisanti M. P. Caveolins, a family of scaffolding proteins for organizing “preassembled signaling complexes” at the plasma membrane. Journal of Biological Chemistry 1998; 273: 5419–5422
   PubMed Web of Science ®Google Scholar
• Hakomori S. Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism. Cancer Research 1996; 56: 5309–5318
   PubMed Web of Science ®Google Scholar