Semaphorin-4D (SEMA4D) also known as Cluster of Differentiation 100 (CD100), is a protein of the semaphorin family that in humans is encoded by the SEMA4Dgene.[1]
↑Kumanogoh A, Watanabe C, Lee I, Wang X, Shi W, Araki H, Hirata H, Iwahori K, Uchida J, Yasui T, Matsumoto M, Yoshida K, Yakura H, Pan C, Parnes JR, Kikutani H (November 2000). "Identification of CD72 as a lymphocyte receptor for the class IV semaphorin CD100: a novel mechanism for regulating B cell signaling". Immunity. 13 (5): 621–31. doi:10.1016/S1074-7613(00)00062-5. PMID11114375.
↑Ishida I, Kumanogoh A, Suzuki K, Akahani S, Noda K, Kikutani H (August 2003). "Involvement of CD100, a lymphocyte semaphorin, in the activation of the human immune system via CD72: implications for the regulation of immune and inflammatory responses". Int. Immunol. 15 (8): 1027–34. doi:10.1093/intimm/dxg098. PMID12882840.
↑Deborah A. Witherden; Megumi Watanabe; Olivia Garijo; Stephanie E. Rieder; Gor Sarkisyan; Shane J.F. Cronin; Petra Verdino; Ian A. Wilson; Atsushi Kumanogoh; Hitoshi Kikutani; Luc Teyton; Wolfgang H. Fischer; Wendy L. Havran (August 2012). "The CD100 Receptor Interacts with Its Plexin B2 Ligand to Regulate Epidermal γδ T Cell Function". Immunity. 37 (2): 314–25. doi:10.1016/j.immuni.2012.05.026.
Further reading
Bougeret C, Mansur IG, Dastot H, et al. (1992). "Increased surface expression of a newly identified 150-kDa dimer early after human T lymphocyte activation". J. Immunol. 148 (2): 318–23. PMID1530858.
Herold C, Elhabazi A, Bismuth G, et al. (1997). "CD100 is associated with CD45 at the surface of human T lymphocytes. Role in T cell homotypic adhesion". J. Immunol. 157 (12): 5262–8. PMID8955171.
Furuyama T, Inagaki S, Kosugi A, et al. (1997). "Identification of a novel transmembrane semaphorin expressed on lymphocytes". J. Biol. Chem. 271 (52): 33376–81. doi:10.1074/jbc.271.52.33376. PMID8969198.
Tamagnone L, Artigiani S, Chen H, et al. (1999). "Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates". Cell. 99 (1): 71–80. doi:10.1016/S0092-8674(00)80063-X. PMID10520995.
Elhabazi A, Delaire S, Bensussan A, et al. (2001). "Biological activity of soluble CD100. I. The extracellular region of CD100 is released from the surface of T lymphocytes by regulated proteolysis". J. Immunol. 166 (7): 4341–7. doi:10.4049/jimmunol.166.7.4341. PMID11254687.
Delaire S, Billard C, Tordjman R, et al. (2001). "Biological activity of soluble CD100. II. Soluble CD100, similarly to H-SemaIII, inhibits immune cell migration". J. Immunol. 166 (7): 4348–54. doi:10.4049/jimmunol.166.7.4348. PMID11254688.
Granziero L, Circosta P, Scielzo C, et al. (2003). "CD100/Plexin-B1 interactions sustain proliferation and survival of normal and leukemic CD5+ B lymphocytes". Blood. 101 (5): 1962–9. doi:10.1182/blood-2002-05-1339. PMID12406905.
Izmailova E, Bertley FM, Huang Q, et al. (2003). "HIV-1 Tat reprograms immature dendritic cells to express chemoattractants for activated T cells and macrophages". Nat. Med. 9 (2): 191–7. doi:10.1038/nm822. PMID12539042.
Love CA, Harlos K, Mavaddat N, et al. (2003). "The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D". Nat. Struct. Biol. 10 (10): 843–8. doi:10.1038/nsb977. PMID12958590.
Giraudon P, Vincent P, Vuaillat C, et al. (2004). "Semaphorin CD100 from activated T lymphocytes induces process extension collapse in oligodendrocytes and death of immature neural cells". J. Immunol. 172 (2): 1246–55. doi:10.4049/jimmunol.172.2.1246. PMID14707103.
Deaglio S, Vaisitti T, Bergui L, et al. (2005). "CD38 and CD100 lead a network of surface receptors relaying positive signals for B-CLL growth and survival". Blood. 105 (8): 3042–50. doi:10.1182/blood-2004-10-3873. PMID15613544.
Conrotto P, Valdembri D, Corso S, et al. (2005). "Sema4D induces angiogenesis through Met recruitment by Plexin B1". Blood. 105 (11): 4321–9. doi:10.1182/blood-2004-07-2885. PMID15632204.
Lewandrowski U, Moebius J, Walter U, Sickmann A (2006). "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach". Mol. Cell. Proteomics. 5 (2): 226–33. doi:10.1074/mcp.M500324-MCP200. PMID16263699.