CD86

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
CD86
CD86 structure.gif
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCD86, B7-2, B7.2, B70, CD28LG2, LAB72, CD86 molecule
External IDsOMIM: 601020 MGI: 101773 HomoloGene: 10443 GeneCards: CD86
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for CD86
Genomic location for CD86
Band3q13.33Start122,055,362 bp[1]
End122,121,139 bp[1]
RNA expression pattern
PBB GE CD86 210895 s at fs.png

PBB GE CD86 205685 at fs.png

PBB GE CD86 205686 s at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_176892
NM_001206924
NM_001206925
NM_006889
NM_175862

NM_019388

RefSeq (protein)

NP_001193853
NP_001193854
NP_008820
NP_787058
NP_795711

NP_062261

Location (UCSC)Chr 3: 122.06 – 122.12 MbChr 16: 36.6 – 36.67 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cluster of Differentiation 86 (also known as CD86 and B7-2) is a protein expressed on dendritic cells, macrophages, B-cells, and other antigen-presenting cells. Along with CD80, CD86 provides costimulatory signals necessary for T-cell activation and survival. Depending on the ligand bound, CD86 can be used to signal for self-regulation and cell-cell association, or for attenuation of regulation and cell-cell disassociation.[5]

The CD86 gene encodes a type I membrane protein that is a member of the immunoglobulin superfamily.[6] Alternative splicing results in two transcript variants encoding different isoforms. Additional transcript variants have been described, but their full-length sequences have not been determined.[7]

Co-stimulation for T-cell activation[edit]

The binding of CD86 (or the closely related protein CD80) expressed on the surface of an antigen-presenting cell with CD28 on the surface of a mature, naive T-cell, is required for T-cell activation.[8] This protein interaction, along with the primary signal that is the MHC class II with an attached peptide binding to the T-cell receptor (TCR), activates mitogen-activated protein kinase and transcription factor nf-κB in the T-cell. These proteins up-regulate production of CD40L (used in B-cell activation), IL-21 and IL-21R (used for division/proliferation), and IL-2, among other cytokines.[8]

T-reg mediation[edit]

Can't load image
CTLA-4 inhibits CD86 - CD28 binding when active on T-regulatory cells

T-regulatory cells produce CTLA-4, which can dampen an immune response and lead to increased anergy.[5] CTLA-4 binds to CD86 with greater affinity than CD28, which impairs the co-stimulation necessary for proper T-cell activation.[9] When bound to CTLA-4, CD86 can be removed from the surface of an APC and onto the T-reg cell in a process called trogocytosis.[5] Blocking this process with anit-CTLA-4 antibodies is useful for a specific type of cancer immunotherapy called cancer therapy by inhibition of negative immune regulation.[10] Japanese immunologist Tasuku Honjo and American immunologist James P. Allison won the Nobel Prize in Physiology or Medicine in 2018 for their work on this topic.

See also[edit]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000114013 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022901 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c Ohue Y, Nishikawa H (July 2019). "Regulatory T (Treg) cells in cancer: Can Treg cells be a new therapeutic target?". Cancer Science. 110 (7): 2080–2089. doi:10.1111/cas.14069. PMC 6609813. PMID 31102428.
  6. ^ Chen C, Gault A, Shen L, Nabavi N (May 1994). "Molecular cloning and expression of early T cell costimulatory molecule-1 and its characterization as B7-2 molecule". Journal of Immunology. 152 (10): 4929–36. PMID 7513726.
  7. ^ "Entrez Gene: CD86 CD86 molecule".
  8. ^ a b Dyck L, Mills KH (May 2017). "Immune checkpoints and their inhibition in cancer and infectious diseases". European Journal of Immunology. 47 (5): 765–779. doi:10.1002/eji.201646875. PMID 28393361.
  9. ^ Lightman SM, Utley A, Lee KP (2019-05-03). "Survival of Long-Lived Plasma Cells (LLPC): Piecing Together the Puzzle". Frontiers in Immunology. 10: 965. doi:10.3389/fimmu.2019.00965. PMC 6510054. PMID 31130955.
  10. ^ Chen R, Ganesan A, Okoye I, Arutyunova E, Elahi S, Lemieux MJ, Barakat K (March 2020). "Targeting B7-1 in immunotherapy". Medicinal Research Reviews. 40 (2): 654–682. doi:10.1002/med.21632. PMID 31448437. S2CID 201748060.

External links[edit]

Further reading[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.