CD5 (protein)
From Wikipedia, the free encyclopedia
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CD5 molecule
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| PDB rendering based on 2ja4. | ||||||||||||||
| Available structures: 2ja4, 2ott | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | CD5; T1; LEU1 | |||||||||||||
| External IDs | OMIM: 153340 MGI: 88340 HomoloGene: 7260 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
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| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 921 | 12507 | ||||||||||||
| Ensembl | ENSG00000110448 | ENSMUSG00000024669 | ||||||||||||
| Uniprot | P06127 | Q3UP78 | ||||||||||||
| Refseq | NM_014207 (mRNA) NP_055022 (protein) |
NM_007650 (mRNA) NP_031676 (protein) |
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| Location | Chr 11: 60.63 - 60.65 Mb | Chr 19: 10.79 - 10.81 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
CD5 is a cluster of differentiation found on a subset of IgM secreting B cells called B-1 cells, and also on T cells.[1] B1 B cells have limited diversity of their B Cell Receptor (BCR) due to their lack of the enzyme terminal deoxynucleotidyl transferase (TdT) and are potentially self-reactive. CD5 serves to mitigate activating signals from the BCR so that the B1 cells can only be activated by a very strong stimuli (such as bacterial proteins) and not by normal tissue proteins. CD5 was used as a T cell marker until mABs against CD3 were developed. In humans, the gene is located on the q arm of chromosome 11[3]. CD72 serves as a ligand.
T cells express higher levels of CD5 than B cells. CD5 is up-regulated on T cells upon strong activation. In the thymus, there is a correlation with CD5 expression and strength of the interaction of the T cell towards self-peptides.
[edit] References
[edit] Further reading
- Berland R, Wortis HH (2002). "Origins and functions of B-1 cells with notes on the role of CD5.". Annu. Rev. Immunol. 20: 253–300. doi:. PMID 11861604.
- Osman N, Ley SC, Crumpton MJ (1992). "Evidence for an association between the T cell receptor/CD3 antigen complex and the CD5 antigen in human T lymphocytes.". Eur. J. Immunol. 22 (11): 2995–3000. PMID 1385158.
- Van de Velde H, von Hoegen I, Luo W, et al. (1991). "The B-cell surface protein CD72/Lyb-2 is the ligand for CD5.". Nature 351 (6328): 662–5. doi:. PMID 1711157.
- Jones NH, Clabby ML, Dialynas DP, et al. (1986). "Isolation of complementary DNA clones encoding the human lymphocyte glycoprotein T1/Leu-1.". Nature 323 (6086): 346–9. doi:. PMID 3093892.
- Lankester AC, van Schijndel GM, Cordell JL, et al. (1994). "CD5 is associated with the human B cell antigen receptor complex.". Eur. J. Immunol. 24 (4): 812–6. PMID 7512031.
- Raab M, Yamamoto M, Rudd CE (1994). "The T-cell antigen CD5 acts as a receptor and substrate for the protein-tyrosine kinase p56lck.". Mol. Cell. Biol. 14 (5): 2862–70. PMID 7513045.
- Dianzani U, Bragardo M, Buonfiglio D, et al. (1995). "Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120.". Eur. J. Immunol. 25 (5): 1306–11. PMID 7539755.
- Van de Velde H, Thielemans K (1996). "Native soluble CD5 delivers a costimulatory signal to resting human B lymphocytes.". Cell. Immunol. 172 (1): 84–91. doi:. PMID 8806810.
- Dennehy KM, Broszeit R, Garnett D, et al. (1997). "Thymocyte activation induces the association of phosphatidylinositol 3-kinase and pp120 with CD5.". Eur. J. Immunol. 27 (3): 679–86. PMID 9079809.
- Gary-Gouy H, Lang V, Sarun S, et al. (1997). "In vivo association of CD5 with tyrosine-phosphorylated ZAP-70 and p21 phospho-zeta molecules in human CD3+ thymocytes.". J. Immunol. 159 (8): 3739–47. PMID 9378960.
- Dennehy KM, Broszeit R, Ferris WF, Beyers AD (1998). "Thymocyte activation induces the association of the proto-oncoprotein c-cbl and ras GTPase-activating protein with CD5.". Eur. J. Immunol. 28 (5): 1617–25. PMID 9603468.
- Bauch A, Campbell KS, Reth M (1998). "Interaction of the CD5 cytoplasmic domain with the Ca2+/calmodulin-dependent kinase IIdelta.". Eur. J. Immunol. 28 (7): 2167–77. PMID 9692886.
- Calvo J, Vildà JM, Places L, et al. (1998). "Human CD5 signaling and constitutive phosphorylation of C-terminal serine residues by casein kinase II.". J. Immunol. 161 (11): 6022–9. PMID 9834084.
- McAlister MS, Davis B, Pfuhl M, Driscoll PC (1999). "NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments.". Protein Eng. 11 (10): 847–53. PMID 9862202.
- Perez-Villar JJ, Whitney GS, Bowen MA, et al. (1999). "CD5 negatively regulates the T-cell antigen receptor signal transduction pathway: involvement of SH2-containing phosphotyrosine phosphatase SHP-1.". Mol. Cell. Biol. 19 (4): 2903–12. PMID 10082557.
- Carmo AM, Castro MA, Arosa FA (1999). "CD2 and CD3 associate independently with CD5 and differentially regulate signaling through CD5 in Jurkat T cells.". J. Immunol. 163 (8): 4238–45. PMID 10510361.
- Vilà JM, Calvo J, Places L, et al. (2001). "Role of two conserved cytoplasmic threonine residues (T410 and T412) in CD5 signaling.". J. Immunol. 166 (1): 396–402. PMID 11123317.
- Vilà JM, Gimferrer I, Padilla O, et al. (2001). "Residues Y429 and Y463 of the human CD5 are targeted by protein tyrosine kinases.". Eur. J. Immunol. 31 (4): 1191–8. PMID 11298344.
- Kirchgessner H, Dietrich J, Scherer J, et al. (2001). "The transmembrane adaptor protein TRIM regulates T cell receptor (TCR) expression and TCR-mediated signaling via an association with the TCR zeta chain.". J. Exp. Med. 193 (11): 1269–84. PMID 11390434.
- Gary-Gouy H, Harriague J, Dalloul A, et al. (2002). "CD5-negative regulation of B cell receptor signaling pathways originates from tyrosine residue Y429 outside an immunoreceptor tyrosine-based inhibitory motif.". J. Immunol. 168 (1): 232–9. PMID 11751967.
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