CD11a

Integrin alpha L

Integrin alpha L

Mammalian protein found in Homo sapiens

Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide), also known as ITGAL, is a protein that in humans is encoded by the ITGAL gene.[5] CD11a functions in the immune system. It is involved in cellular adhesion and costimulatory signaling. It is the target of the drug efalizumab.

Quick Facts ITGAL, Available structures ...

Function

ITGAL gene encodes the integrin alpha L chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This I-domain containing alpha integrin combines with the beta 2 chain (ITGB2) to form the integrin lymphocyte function-associated antigen-1 (LFA-1), which is expressed in all leukocytes. LFA-1 plays a central role in leukocyte intercellular adhesion through interactions with its ligands, ICAMs 1-3 (intercellular adhesion molecules 1 through 3), and also functions in lymphocyte costimulatory signaling.[6]

CD11a is one of the two components, along with CD18, which form lymphocyte function-associated antigen-1.

Efalizumab acts as an immunosuppressant by binding to CD11a but was withdrawn in 2009 because it was associated with severe side effects.

Interactions

CD11a has been shown to interact with ICAM-1.[7][8][9]

See also

References

  1. [1]
    GRCh38: Ensembl release 89: ENSG00000005844 – Ensembl, May 2017
  2. [2]
    GRCm38: Ensembl release 89: ENSMUSG00000030830 – Ensembl, May 2017
  3. [3]
    "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. [4]
    "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. [5]
    "NCBI".
  6. [6]
    "Entrez Gene: ITGAL integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)".
  7. [7]
    Lu C, Takagi J, Springer TA (May 2001). "Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state". J. Biol. Chem. 276 (18): 14642–8. doi:10.1074/jbc.M100600200. PMID 11279101.
  8. [8]
    Shimaoka M, Xiao T, Liu JH, Yang Y, Dong Y, Jun CD, McCormack A, Zhang R, Joachimiak A, Takagi J, Wang JH, Springer TA (Jan 2003). "Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation". Cell. 112 (1): 99–111. doi:10.1016/S0092-8674(02)01257-6. PMC 4372089. PMID 12526797.
  9. [9]
    Yusuf-Makagiansar H, Makagiansar IT, Hu Y, Siahaan TJ (Dec 2001). "Synergistic inhibitory activity of alpha- and beta-LFA-1 peptides on LFA-1/ICAM-1 interaction". Peptides. 22 (12): 1955–62. doi:10.1016/S0196-9781(01)00546-0. PMID 11786177. S2CID 54343441.

Further reading


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