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CD49b

Introduction

Integrin alpha-2 or CD49b (cluster of differentiation 49b) is a protein which in humans is encoded by the CD49b gene.

The CD49b protein is an integrin alpha subunit. It makes up half of the Ξ±2Ξ²1 integrin duplex. Integrins are heterodimeric integral membrane glycoproteins composed of a distinct alpha chain and a common beta chain. They are found on a wide variety of cell types including, T cells (the NKT cells), NK cells, fibroblasts and platelets. Integrins are involved in cell adhesion and also participate in cell-surface mediated signalling.[1]

Expression of CD49b in conjunction with LAG-3 has been used to identify type 1 regulatory (Tr1) cells.[2]

DX5 is a monoclonal antibody which binds to CD49b.[3]

Interactions

Interactions

CD49b has been shown to interact with MMP1.[4][5]

References

References

  1. ↑ “Entrez Gene: ITGA2 integrin, alpha 2 (CD49B, alpha 2 subunit of VLA-2 receptor)”.
  2. ↑ Gagliani, Nicola; Magnani, Chiara F.; Huber, Samuel; Gianolini, Monica E.; Pala, Mauro; Licona-Limon, Paula; Guo, Binggege; Herbert, De’Broski R.; Bulfone, Alessandro (2013-06-01). “Coexpression of CD49b and LAG-3 identifies human and mouse T regulatory type 1 cells”. Nature Medicine. 19 (6): 739–746. doi:10.1038/nm.3179. ISSNΒ 1546-170X. PMIDΒ 23624599.
  3. ↑ Arase H, Saito T, Phillips JH, Lanier LL (August 2001). “Cutting edge: the mouse NK cell-associated antigen recognized by DX5 monoclonal antibody is CD49b (alpha 2 integrin, very late antigen-2)”. Journal of Immunology. 167 (3): 1141–4. doi:10.4049/jimmunol.167.3.1141. PMIDΒ 11466327.
  4. ↑ Stricker TP, Dumin JA, Dickeson SK, Chung L, Nagase H, Parks WC, Santoro SA (Aug 2001). “Structural analysis of the alpha(2) integrin I domain/procollagenase-1 (matrix metalloproteinase-1) interaction”. J. Biol. Chem. 276 (31): 29375–81. doi:10.1074/jbc.M102217200. PMIDΒ 11359774.
  5. ↑ Dumin JA, Dickeson SK, Stricker TP, Bhattacharyya-Pakrasi M, Roby JD, Santoro SA, Parks WC (Aug 2001). “Pro-collagenase-1 (matrix metalloproteinase-1) binds the alpha(2)beta(1) integrin upon release from keratinocytes migrating on type I collagen”. J. Biol. Chem. 276 (31): 29368–74. doi:10.1074/jbc.M104179200. PMIDΒ 11359786.
External links
Further reading

Further reading

  • Moroi M, Jung SM (1997). “Platelet receptors for collagen”. Thromb. Haemost. 78 (1): 439–44. PMIDΒ 9198193.
  • Takada Y, Kamata T, Irie A, Puzon-McLaughlin W, Zhang XP (1998). “Structural basis of integrin-mediated signal transduction”. Matrix Biol. 16 (4): 143–51. doi:10.1016/S0945-053X(97)90002-0. PMIDΒ 9402003.
  • Dickeson SK, Santoro SA (1998). “Ligand recognition by the I domain-containing integrins”. Cell. Mol. Life Sci. 54 (6): 556–66. doi:10.1007/s000180050184. PMIDΒ 9676575.
  • Porter JC, Hogg N (1999). “Integrins take partners: cross-talk between integrins and other membrane receptors”. Trends Cell Biol. 8 (10): 390–6. doi:10.1016/S0962-8924(98)01344-0. PMIDΒ 9789327.
  • Plenz GA, Deng MC, Robenek H, VΓΆlker W (2003). “Vascular collagens: spotlight on the role of type VIII collagen in atherogenesis”. Atherosclerosis. 166 (1): 1–11. doi:10.1016/S0021-9150(01)00766-3. PMIDΒ 12482545.
  • Charakida M, Tousoulis D, Stefanadis C, Toutouzas P (2003). “The impact of platelet glycoprotein IIIa and Ia polymorphisms in cardiovascular thrombotic disease”. Italian Heart Journal. 4 (1): 17–22. PMIDΒ 12690916.
  • Tsantes AE, Nikolopoulos GK, Bagos PG, Vaiopoulos G, Travlou A (2007). “Lack of association between the platelet glycoprotein Ia C807T gene polymorphism and coronary artery disease: a meta-analysis”. Int. J. Cardiol. 118 (2): 189–96. doi:10.1016/j.ijcard.2006.06.047. PMIDΒ 17023078.
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