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Signal-regulatory protein alpha : ウィキペディア英語版 | Signal-regulatory protein alpha
Signal regulatory protein α (SIRP α) is regulatory membrane glycoprotein from SIRP family expressed mainly by myeloid cells and also by stem cells or neurons. SIRP α acts as inhibitory receptor and interacts with a broadly expressed transmembrane protein CD47 also called the "don´t eat me" signal. This interaction negatively controls effector function of innate immune cells such as host cell phagocytosis. This is analogous to the self signals provided by MHC class I molecules to NK cells via Ig-like or Ly49 receptors.〔 〕 〔 〕 ==Structure== The cytoplasmic region of SIRP α is highly conserved between rats, mice and humans. Cytoplasmic region consists of tyrosine residues conform to inhibitory ITIMs that associates with phosphataseSHP2. The extracellular region contains three Immunoglobulin superfamily domains – single V-set and two C1-set IgSF domains. SIRP β and γ have the similar extracellular structure but different cytoplasmic regions giving contrasting types of signals. SIRP α polymorphisms are found in ligand-binding IgSF V-set domain but it does not affect ligand binding. One idea is that the polymorphism is important to protect the receptor of pathogens binding.〔 〕 〔 〕
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