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CD2 (cluster of differentiation 2) is a cell adhesion molecule found on the surface of T cells and natural killer (NK) cells.
It has also been called T-cell surface antigen T11/Leu-5, LFA-2,[1] LFA-3 receptor, erythrocyte receptor and rosette receptor.[2]
It interacts with other adhesion molecules, such as lymphocyte function-associated antigen-3 (LFA-3/CD58) in humans, or CD48 in rodents, which are expressed on the surfaces of other cells.[3]
In addition to its adhesive properties, CD2 also acts as a co-stimulatory molecule on T and NK cells.[4]
Diagnostic relevance
CD2 is a specific marker for T cells and NK cells, and can therefore be used in immunohistochemistry to identify the presence of such cells in tissue sections. The great majority of T cell lymphomas and leukaemias also express CD2, making it possible to use the presence of the antigen to distinguish these conditions from B cell neoplasms.[5]
↑Wilkins AL, Yang W, Yang JJ (2003). "Structural biology of the cell adhesion protein CD2: from molecular recognition to protein folding and design". Curr Protein Pept Sci. 4 (5): 367–73. doi:10.2174/1389203033487063. PMID14529530.
↑ 4.04.1Yang JJ, Ye Y, Carroll A, Yang W, Lee HW (2001). "Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation". Curr Protein Pept Sci. 2 (1): 1–17. doi:10.2174/1389203013381251. PMID12369898.
↑Leong, Anthony S-Y; Cooper, Kumarason; Leong, F Joel W-M (2003). Manual of Diagnostic Cytology (2 ed.). Greenwich Medical Media, Ltd. p. 61. ISBN978-1-84110-100-2.
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Rouleau M, Mollereau B, Bernard A, Metivier D, Rosenthal-Allieri MA, Charpentier B, Senik A (1997). "CD2 induced apoptosis of peripheral T cells". Transplant. Proc. 29 (5): 2377–8. doi:10.1016/S0041-1345(97)00410-7. PMID9270771.
Yang JJ, Ye Y, Carroll A, Yang W, Lee HW (2002). "Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation". Curr. Protein Pept. Sci. 2 (1): 1–17. doi:10.2174/1389203013381251. PMID12369898.
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Hahn WC, Menu E, Bothwell AL, Sims PJ, Bierer BE (1992). "Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59". Science. 256 (5065): 1805–7. doi:10.1126/science.1377404. PMID1377404.
Luzzati AL, Giacomini E, Giordani L, Pugliese O, Viora M, Chersi A (1992). "The antigen-specific induction of normal human lymphocytes in vitro is down-regulated by a conserved HIV p24 epitope". Immunol. Lett. 33 (3): 307–14. doi:10.1016/0165-2478(92)90078-3. PMID1385321.
Ruegg CL, Strand M (1991). "A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx". Cell. Immunol. 137 (1): 1–13. doi:10.1016/0008-8749(91)90051-C. PMID1832084.
Schraven B, Samstag Y, Altevogt P, Meuer SC (1990). "Association of CD2 and CD45 on human T lymphocytes". Nature. 345 (6270): 71–4. doi:10.1038/345071a0. PMID1970422.
Samelson LE, Fletcher MC, Ledbetter JA, June CH (1990). "Activation of tyrosine phosphorylation in human T cells via the CD2 pathway. Regulation by the CD45 tyrosine phosphatase". J. Immunol. 145 (8): 2448–54. PMID1976695.
Luzzati AL, Pugliese O, Giacomini E, Giordani L, Quintieri F, Hraba T, Mach O, Krchnák V, Vágner J (1990). "Immunoregulatory effect of a synthetic peptide corresponding to a region of protein p24 of HIV". Folia Biol. (Praha). 36 (1): 71–7. PMID2111780.
Peterson A, Seed B (1987). "Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2)". Nature. 329 (6142): 842–6. doi:10.1038/329842a0. PMID2444890.
Leca G, Boumsell L, Fabbi M, Reinherz EL, Kanellopoulos JM (1986). "The sheep erythrocyte receptor and both alpha and beta chains of the human T-lymphocyte antigen receptor bind the mitogenic lectin (phytohaemagglutinin) from Phaseolus vulgaris". Scand. J. Immunol. 23 (5): 535–44. doi:10.1111/j.1365-3083.1986.tb01985.x. PMID3085210.