Cd47-flox Mouse

Cd47, also known as cluster of differentiation 47, is a protein expressed on the outer membrane of human cells. It binds to soluble and cell surface receptors, forming a pleiotropic receptor-multiligand interaction network [2]. Cd47 is involved in the CD47/SIRPα axis, where CD47 binds to SIRPα receptor on myeloid cells, delivering a “don't eat me” signal, which is crucial in immune responses, especially in tumor-associated immune regulation [1].

In cancer research, CD47 blockade has been investigated. In syngeneic immunocompetent mouse tumor models, the therapeutic effects of CD47 blockade depend on dendritic cell-mediated cross-priming of T cell responses rather than macrophage phagocytosis as previously thought. The antitumor effects also require the cytosolic DNA sensor STING in CD11c + cells [4]. In glioblastoma, inhibition of fatty acid oxidation (FAO) reduces CD47-mediated immune evasion, as FAO-derived acetyl-CoA upregulates CD47 transcription via NF-κB/RelA acetylation [3].

In conclusion, Cd47 plays a vital role in immune regulation, especially in the context of cancer immune evasion. Studies using mouse models have revealed its complex role in tumor-immune interactions, highlighting its potential as a therapeutic target for cancer immunotherapy. The understanding of how Cd47 functions in these models can help in developing more effective cancer treatment strategies [1,3,4].