CD2

O CD2 (cluster de diferenciación 2) é unha molécula de adhesión celular proteica atopada na superficie das células T e células asasinas naturais (NK). Tamén recibiu o nome de antíxeno de superficie de células T T11/Leu-5, LFA-2, receptor LFA-3, receptor de eritrocitos e receptor roseta.^[1]

Está codificado nun xene do cromosoma 1 humano.

Función

Interacciona con outras moléculas de adhesión celular, como o antíxeno-3 asociado a función de linfocitos (LFA-3/CD58) en humanos, ou CD48 en roedores, que se expresan nas superficies doutras células.^[2]

Ademais das súas propiedades adhesivas, o CD2 tamén actúa como unha molécula coestimuladora nas células T e NK.^[3]

Importancia diagnóstica

O CD2 é un marcador específico para as células T e NK, e, xa que logo, pode utilizarse en inmunohistoquímica para identificar a presenza de tales células nos cortes histolóxicos. A gran maioría dos linfomas de células T e das leucemias tamén expresan o CD2, facendo posible usar a presenza do antíxeno para distinguir estas doenzas dos neoplasmas de células B.^[4]

Clasificación

Debido ás súas características estruturais, o CD2 é un membro da superfamilia das inmunoglobulinas. Posúe dous dominios de tipo inmunoglobulina na súa porción extracelular.^[3]

Interaccións

O CD2 interacciona co CD2BP2,^[5] Lck^[6] e PSTPIP1.^[7]

Notas

↑ "Uniprot database entry for CD2 (accession number P06729)". Arquivado dende o orixinal o 19 de agosto de 2020. Consultado o 17 de febreiro de 2013.
↑ Wilkins A, Yang W, Yang J (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. PMID 14529530. doi:10.2174/1389203033487063.
↑ ^3,0 ^3,1 Yang J, Ye Y, Carroll A, Yang W, Lee H (2001). "Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation". Curr Protein Pept Sci 2 (1): 1–17. PMID 12369898. doi:10.2174/1389203013381251.
↑ Leong, Anthony S-Y; Cooper, Kumarason; Leong, F Joel W-M (2003). Manual of Diagnostic Cytology (2 ed.). Greenwich Medical Media, Ltd. p. 61. ISBN 1-84110-100-1.
↑ Nishizawa, K; Freund C, Li J, Wagner G, Reinherz E L (1998). "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (25): 14897–902. ISSN 0027-8424. PMC 24547. PMID 9843987. doi:10.1073/pnas.95.25.14897.
↑ Bell, G M; Fargnoli J, Bolen J B, Kish L, Imboden J B (1996). "The SH3 domain of p56lck binds to proline-rich sequences in the cytoplasmic domain of CD2". J. Exp. Med. (UNITED STATES) 183 (1): 169–78. ISSN 0022-1007. PMC 2192399. PMID 8551220. doi:10.1084/jem.183.1.169.
↑ Li, J; Nishizawa K, An W, Hussey R E, Lialios F E, Salgia R, Sunder-Plassmann R, Reinherz E L (1998). "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion". EMBO J. (ENGLAND) 17 (24): 7320–36. ISSN 0261-4189. PMC 1171078. PMID 9857189. doi:10.1093/emboj/17.24.7320.

Bibliografía

Sayre PH, Reinherz EL (1989). "Structure and function of the erythrocyte receptor CD2 on human T lymphocytes: a review.". Scand. J. Rheumatol. Suppl. 76: 131–44. PMID 2471997.
Rouleau M, Mollereau B, Bernard A; et al. (1997). "CD2 induced apoptosis of peripheral T cells.". Transplant. Proc. 29 (5): 2377–8. PMID 9270771. doi:10.1016/S0041-1345(97)00410-7.
Lüscher B (2001). "Function and regulation of the transcription factors of the Myc/Max/Mad network.". Gene 277 (1-2): 1–14. PMID 11602341. doi:10.1016/S0378-1119(01)00697-7.
Yang JJ, Ye Y, Carroll A; et al. (2002). "Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation.". Curr. Protein Pept. Sci. 2 (1): 1–17. PMID 12369898. doi:10.2174/1389203013381251.
Bell GM, Seaman WE, Niemi EC, Imboden JB (1992). "The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line.". J. Exp. Med. 175 (2): 527–36. PMC 2119111. PMID 1346273. doi:10.1084/jem.175.2.527.
Marie-Cardine A, Maridonneau-Parini I, Ferrer M; et al. (1992). "The lymphocyte-specific tyrosine protein kinase p56lck is endocytosed in Jurkat cells stimulated via CD2.". J. Immunol. 148 (12): 3879–84. PMID 1351089.
Hahn WC, Menu E, Bothwell AL; et al. (1992). "Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59.". Science 256 (5065): 1805–7. PMID 1377404. doi:10.1126/science.1377404.
Luzzati AL, Giacomini E, Giordani L; et al. (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. PMID 1385321. doi:10.1016/0165-2478(92)90078-3.
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. PMID 1832084. doi:10.1016/0008-8749(91)90051-C.
Schraven B, Samstag Y, Altevogt P, Meuer SC (1990). "Association of CD2 and CD45 on human T lymphocytes.". Nature 345 (6270): 71–4. PMID 1970422. doi:10.1038/345071a0.
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. PMID 1976695.
Luzzati AL, Pugliese O, Giacomini E; et al. (1990). "Immunoregulatory effect of a synthetic peptide corresponding to a region of protein p24 of HIV.". Folia Biol. (Praha) 36 (1): 71–7. PMID 2111780.
Seed B, Aruffo A (1987). "Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure.". Proc. Natl. Acad. Sci. U.S.A. 84 (10): 3365–9. PMC 304871. PMID 2437578. doi:10.1073/pnas.84.10.3365.
Peterson A, Seed B (1987). "Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2).". Nature 329 (6142): 842–6. PMID 2444890. doi:10.1038/329842a0.
Sayre PH, Chang HC, Hussey RE; et al. (1987). "Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes.". Proc. Natl. Acad. Sci. U.S.A. 84 (9): 2941–5. PMC 304776. PMID 2883656. doi:10.1073/pnas.84.9.2941.
Diamond DJ, Clayton LK, Sayre PH, Reinherz EL (1988). "Exon-intron organization and sequence comparison of human and murine T11 (CD2) genes.". Proc. Natl. Acad. Sci. U.S.A. 85 (5): 1615–9. PMC 279824. PMID 2894031. doi:10.1073/pnas.85.5.1615.
Lang G, Wotton D, Owen MJ; et al. (1988). "The structure of the human CD2 gene and its expression in transgenic mice.". EMBO J. 7 (6): 1675–82. PMC 457152. PMID 2901953.
Leca G, Boumsell L, Fabbi M; et al. (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. PMID 3085210. doi:10.1111/j.1365-3083.1986.tb01985.x.
Sewell WA, Brown MH, Dunne J; et al. (1986). "Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen.". Proc. Natl. Acad. Sci. U.S.A. 83 (22): 8718–22. PMC 387002. PMID 3490670. doi:10.1073/pnas.83.22.8718.

Ligazóns externas

[1] "Uniprot database entry for CD2 (accession number P06729)". Arquivado dende o orixinal o 19 de agosto de 2020. Consultado o 17 de febreiro de 2013.

[2] Wilkins A, Yang W, Yang J (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. PMID 14529530. doi:10.2174/1389203033487063.

[yang-3] 3,0 ^3,1 Yang J, Ye Y, Carroll A, Yang W, Lee H (2001). "Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation". Curr Protein Pept Sci 2 (1): 1–17. PMID 12369898. doi:10.2174/1389203013381251.

[Leong-4] Leong, Anthony S-Y; Cooper, Kumarason; Leong, F Joel W-M (2003). Manual of Diagnostic Cytology (2 ed.). Greenwich Medical Media, Ltd. p. 61. ISBN 1-84110-100-1.

[pmid9843987-5] Nishizawa, K; Freund C, Li J, Wagner G, Reinherz E L (1998). "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (25): 14897–902. ISSN 0027-8424. PMC 24547. PMID 9843987. doi:10.1073/pnas.95.25.14897.

[pmid8551220-6] Bell, G M; Fargnoli J, Bolen J B, Kish L, Imboden J B (1996). "The SH3 domain of p56lck binds to proline-rich sequences in the cytoplasmic domain of CD2". J. Exp. Med. (UNITED STATES) 183 (1): 169–78. ISSN 0022-1007. PMC 2192399. PMID 8551220. doi:10.1084/jem.183.1.169.

[pmid9857189-7] Li, J; Nishizawa K, An W, Hussey R E, Lialios F E, Salgia R, Sunder-Plassmann R, Reinherz E L (1998). "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion". EMBO J. (ENGLAND) 17 (24): 7320–36. ISSN 0261-4189. PMC 1171078. PMID 9857189. doi:10.1093/emboj/17.24.7320.

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