描述：
B72, also known as CD86, B70, and ETC-1, is a 60-100 kDa variably glycosylated protein in
the B7 family. B7 family members are transmembrane cell surface molecules that play
important roles in immune activation and the maintenance of immune tolerance. Mature rat
B72 consists of a 222 amino acid (aa) extracellular domain (ECD) with two Ig-like domains,
a 19 aa transmembrane segment, and a 46 aa cytoplasmic tail. Within the ECD, rat B7-2
shares 59% and 81% aa sequence identity with human and mouse B7-2, respectively. B7-2 is
highly expressed on activated antigen presenting cells (APC), e.g. B cells, dendritic cells, and
monocytes, as well as on vascular endothelial cells. B7-2 and the closely related B7-1/CD80
exhibit overlapping but distinct functional properties. Their binding to CD28, which is
constitutively expressed on T cells, enhances T cell receptor signaling and also provides TCR
independent co-stimulation. B7-1 and B7-2 additionally bind the CD28related protein, CTLA-4,
which is up-regulated and recruited to the immunological synapse (IS) at the onset
of T cell activation. CTLA-4 ligation inhibits the T cell response and supports regulatory T
cell function. B7-2 is expressed earlier than B7-1 following APC activation, and both proteins
bind with higher affinity to CTLA-4 than to CD28. B7-2 promotes the stabilization of CD28 in the
IS, while B7-1 is primarily responsible for promoting CTLA-4 recruitment and accumulation in
the IS. The relative participation of B7-1 and B7-2 in T cell costimulation can also alter the
Th1/Th2 bias of the immune response. Both B7-1 and B7-2 serve as cellular receptors for B
species adenoviruses.
原厂资料：
B72, also known as CD86, B70, and ETC-1, is a 60-100 kDa variably glycosylated protein in
the B7 family. B7 family members are transmembrane cell surface molecules that play
important roles in immune activation and the maintenance of immune tolerance. Mature rat
B72 consists of a 222 amino acid (aa) extracellular domain (ECD) with two Ig-like domains,
a 19 aa transmembrane segment, and a 46 aa cytoplasmic tail. Within the ECD, rat B7-2
shares 59% and 81% aa sequence identity with human and mouse B7-2, respectively. B7-2 is
highly expressed on activated antigen presenting cells (APC), e.g. B cells, dendritic cells, and
monocytes, as well as on vascular endothelial cells. B7-2 and the closely related B7-1/CD80
exhibit overlapping but distinct functional properties. Their binding to CD28, which is
constitutively expressed on T cells, enhances T cell receptor signaling and also provides TCR
independent co-stimulation. B7-1 and B7-2 additionally bind the CD28related protein, CTLA-4,
which is up-regulated and recruited to the immunological synapse (IS) at the onset
of T cell activation. CTLA-4 ligation inhibits the T cell response and supports regulatory T
cell function. B7-2 is expressed earlier than B7-1 following APC activation, and both proteins
bind with higher affinity to CTLA-4 than to CD28. B7-2 promotes the stabilization of CD28 in the
IS, while B7-1 is primarily responsible for promoting CTLA-4 recruitment and accumulation in
the IS. The relative participation of B7-1 and B7-2 in T cell costimulation can also alter the
Th1/Th2 bias of the immune response. Both B7-1 and B7-2 serve as cellular receptors for B
species adenoviruses.
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