CD2: Difference between revisions

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=== Diagnostic relevance ===
=== 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 [[lymphoma]]s and [[leukaemia]]s also express CD2, making it possible to use the presence of the antigen to distinguish these conditions from B cell [[neoplasm]]s.<ref name=Leong>{{cite book|author=Leong, Anthony S-Y|author2=Cooper, Kumarason|author3=Leong, F Joel W-M|year=2003|title=Manual of Diagnostic Cytology|edition=2|publisher=Greenwich Medical Media, Ltd.|page=61|isbn=1-84110-100-1}}</ref>
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 [[lymphoma]]s and [[leukaemia]]s also express CD2, making it possible to use the presence of the antigen to distinguish these conditions from B cell [[neoplasm]]s.<ref name=Leong>{{cite book|author=Leong, Anthony S-Y|author2=Cooper, Kumarason|author3=Leong, F Joel W-M|year=2003|title=Manual of Diagnostic Cytology|edition=2|publisher=Greenwich Medical Media, Ltd.|page=61|isbn=978-1-84110-100-2}}</ref>


== Classification ==
== Classification ==
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== Interactions ==
== Interactions ==


CD2 has been shown to [[Protein-protein interaction|interact]] with [[CD2BP2]],<ref name=pmid9843987>{{cite journal | vauthors = Nishizawa K, Freund C, Li J, Wagner G, Reinherz EL | title = Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation | journal = [[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] | volume = 95 | issue = 25 | pages = 14897–902 | date = December 1998 | pmid = 9843987 | pmc = 24547 | doi = 10.1073/pnas.95.25.14897 }}</ref> [[Lck]]<ref name=pmid8551220>{{cite journal | vauthors = Bell GM, Fargnoli J, Bolen JB, Kish L, Imboden JB | title = The SH3 domain of p56lck binds to proline-rich sequences in the cytoplasmic domain of CD2 | journal = J. Exp. Med. | volume = 183 | issue = 1 | pages = 169–78 | date = January 1996 | pmid = 8551220 | pmc = 2192399 | doi = 10.1084/jem.183.1.169 }}</ref> and [[PSTPIP1]].<ref name=pmid9857189>{{cite journal | vauthors = Li J, Nishizawa K, An W, Hussey RE, Lialios FE, Salgia R, Sunder-Plassmann R, Reinherz EL | title = A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion | journal = EMBO J. | volume = 17 | issue = 24 | pages = 7320–36 | date = December 1998 | pmid = 9857189 | pmc = 1171078 | doi = 10.1093/emboj/17.24.7320 }}</ref>
CD2 has been shown to [[Protein-protein interaction|interact]] with [[CD2BP2]],<ref name=pmid9843987>{{cite journal | vauthors = Nishizawa K, Freund C, Li J, Wagner G, Reinherz EL | title = Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation | journal = [[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] | volume = 95 | issue = 25 | pages = 14897–902 | date = December 1998 | pmid = 9843987 | pmc = 24547 | doi = 10.1073/pnas.95.25.14897 }}</ref> [[Lck]]<ref name=pmid8551220>{{cite journal | vauthors = Bell GM, Fargnoli J, Bolen JB, Kish L, Imboden JB | title = The SH3 domain of p56lck binds to proline-rich sequences in the cytoplasmic domain of CD2 | journal =[[Journal of Experimental Medicine]] | volume = 183 | issue = 1 | pages = 169–78 | date = January 1996 | pmid = 8551220 | pmc = 2192399 | doi = 10.1084/jem.183.1.169 }}</ref> and [[PSTPIP1]].<ref name=pmid9857189>{{cite journal | vauthors = Li J, Nishizawa K, An W, Hussey RE, Lialios FE, Salgia R, Sunder-Plassmann R, Reinherz EL | title = A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion | journal = EMBO J. | volume = 17 | issue = 24 | pages = 7320–36 | date = December 1998 | pmid = 9857189 | pmc = 1171078 | doi = 10.1093/emboj/17.24.7320 }}</ref>


== References ==
== References ==
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* {{cite journal | vauthors = Sayre PH, Reinherz EL | title = Structure and function of the erythrocyte receptor CD2 on human T lymphocytes: a review. | journal = Scand. J. Rheumatol. Suppl. | volume = 76 | issue =  | pages = 131–44 | year = 1989 | pmid = 2471997 | doi =  }}
* {{cite journal | vauthors = Sayre PH, Reinherz EL | title = Structure and function of the erythrocyte receptor CD2 on human T lymphocytes: a review. | journal = Scand. J. Rheumatol. Suppl. | volume = 76 | issue =  | pages = 131–44 | year = 1989 | pmid = 2471997 | doi =  }}
* {{cite journal | vauthors = Rouleau M, Mollereau B, Bernard A, Metivier D, Rosenthal-Allieri MA, Charpentier B, Senik A | title = CD2 induced apoptosis of peripheral T cells. | journal = Transplant. Proc. | volume = 29 | issue = 5 | pages = 2377–8 | year = 1997 | pmid = 9270771 | doi = 10.1016/S0041-1345(97)00410-7 }}
* {{cite journal | vauthors = Rouleau M, Mollereau B, Bernard A, Metivier D, Rosenthal-Allieri MA, Charpentier B, Senik A | title = CD2 induced apoptosis of peripheral T cells. | journal = Transplant. Proc. | volume = 29 | issue = 5 | pages = 2377–8 | year = 1997 | pmid = 9270771 | doi = 10.1016/S0041-1345(97)00410-7 }}
* {{cite journal | vauthors = Lüscher B | title = Function and regulation of the transcription factors of the Myc/Max/Mad network. | journal = Gene | volume = 277 | issue = 1-2 | pages = 1–14 | year = 2001 | pmid = 11602341 | doi = 10.1016/S0378-1119(01)00697-7 }}
* {{cite journal | vauthors = Lüscher B | title = Function and regulation of the transcription factors of the Myc/Max/Mad network. | journal = Gene | volume = 277 | issue = 1–2 | pages = 1–14 | year = 2001 | pmid = 11602341 | doi = 10.1016/S0378-1119(01)00697-7 }}
* {{cite journal | vauthors = Yang JJ, Ye Y, Carroll A, Yang W, Lee HW | title = Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation. | journal = Curr. Protein Pept. Sci. | volume = 2 | issue = 1 | pages = 1–17 | year = 2002 | pmid = 12369898 | doi = 10.2174/1389203013381251 }}
* {{cite journal | vauthors = Yang JJ, Ye Y, Carroll A, Yang W, Lee HW | title = Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation. | journal = Curr. Protein Pept. Sci. | volume = 2 | issue = 1 | pages = 1–17 | year = 2002 | pmid = 12369898 | doi = 10.2174/1389203013381251 }}
* {{cite journal | vauthors = Bell GM, Seaman WE, Niemi EC, Imboden JB | title = The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line. | journal = J. Exp. Med. | volume = 175 | issue = 2 | pages = 527–36 | year = 1992 | pmid = 1346273 | pmc = 2119111 | doi = 10.1084/jem.175.2.527 }}
* {{cite journal | vauthors = Bell GM, Seaman WE, Niemi EC, Imboden JB | title = The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line. | journal = J. Exp. Med. | volume = 175 | issue = 2 | pages = 527–36 | year = 1992 | pmid = 1346273 | pmc = 2119111 | doi = 10.1084/jem.175.2.527 }}

Latest revision as of 13:07, 7 November 2018

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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]

Function

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]

Classification

Due to its structural characteristics, CD2 is a member of the immunoglobulin superfamily; it possesses two immunoglobulin-like domains in its extracellular portion.[4]

Interactions

CD2 has been shown to interact with CD2BP2,[6] Lck[7] and PSTPIP1.[8]

References

  1. Sanchez-Madrid F, Krensky AM, Ware CF, Robbins E, Strominger JL, Burakoff SJ, Springer TA (1982). "Three distinct antigens associated with human T-lymphocyte-mediated cytolysis: LFA-1, LFA-2, and LFA-3". Proc Natl Acad Sci U S A. 79 (23): 7489–93. doi:10.1073/pnas.79.23.7489. PMC 347365. PMID 6984191.
  2. Uniprot database entry for CD2 (accession number P06729)
  3. 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. PMID 14529530.
  4. 4.0 4.1 Yang 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. PMID 12369898.
  5. 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 978-1-84110-100-2.
  6. Nishizawa K, Freund C, Li J, Wagner G, Reinherz EL (December 1998). "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation". Proc. Natl. Acad. Sci. U.S.A. 95 (25): 14897–902. doi:10.1073/pnas.95.25.14897. PMC 24547. PMID 9843987.
  7. Bell GM, Fargnoli J, Bolen JB, Kish L, Imboden JB (January 1996). "The SH3 domain of p56lck binds to proline-rich sequences in the cytoplasmic domain of CD2". Journal of Experimental Medicine. 183 (1): 169–78. doi:10.1084/jem.183.1.169. PMC 2192399. PMID 8551220.
  8. Li J, Nishizawa K, An W, Hussey RE, Lialios FE, Salgia R, Sunder-Plassmann R, Reinherz EL (December 1998). "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion". EMBO J. 17 (24): 7320–36. doi:10.1093/emboj/17.24.7320. PMC 1171078. PMID 9857189.

Further reading

External links