Expression of a synapse-associated membrane protein, P84/SHPS-1, and its ligand, IAP/CD47, in mouse retina

Mi, Zhi Ping; Jiang, Peihua; Weng, Weili; Lindberg, Frederik P.; Narayanan, Vinodh; Lagenaur, Carl F.

doi:10.1002/(sici)1096-9861(20000117)416:3<335::aid-cne5>3.0.co;2-x

Cited by 61 publications

(14 citation statements)

References 23 publications

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“…21,26,27 Expression of SIRPs in cancer cells and neuronal cells has also been reported. 7,14,28,29 Among SIRP proteins, SIRPα was identified to be a counter extracellular receptor for CD47 and growing evidence has demonstrated the vital role of SIRPα-CD47 binding interactions in leukocyte-mediated cell functions. For example, studies showed that macrophages recognize phagocytic targets, such as apoptotic cells or opsonized RBCs in autoimmune anemia, via macrophage surface SIRPα trans interactions with CD47 on the target cells.…”

Section: Discussionmentioning

confidence: 99%

Functional Elements on SIRPα IgV Domain Mediate Cell Surface Binding to CD47

Liu

Qiao

Zhou

et al. 2007

Journal of Molecular Biology

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SIRPalpha and SIRPbeta1, the two major isoforms of the signal regulatory protein (SIRP) family, are co-expressed in human leukocytes but mediate distinct extracellular binding interactions and divergent cell signaling responses. Previous studies have demonstrated that binding of SIRPalpha with CD47, another important cell surface molecule, through the extracellular IgV domain regulates important leukocyte functions including macrophage recognition, leukocyte adhesion and transmigration. Although SIRPbeta1 shares highly homologous extracellular IgV structure with SIRPalpha, it does not bind to CD47. Here, we defined key amino acid residues exclusively expressing in the IgV domain of SIRPalpha, but not SIRPbeta1, which determine the extracellular binding interaction of SIRPalpha to CD47. These key residues include Gln67, a small hydrophobic amino acid (Ala or Val) at the 57th position and Met102. We found that Gln67 and Ala/Val57 are critical. Mutation of either of these residues abates SIRPalpha directly binding to CD47. Functional cell adhesion and leukocyte transmigration assays further demonstrated central roles of Gln67 and Ala/Val57 in SIRPalpha extracellular binding mediated cell interactions and cell migration. Another SIRPalpha-specific residue, Met102, appears to assist SIRPalpha IgV binding through Gln67 and Ala/Val57. An essential role of these amino acid residues in SIRPalpha binding to CD47 was further confirmed by introducing these residues into the SIRPbeta1 IgV domain, which dramatically converts SIRPbeta1 into a CD47-binding molecule. Our results thus revealed the molecular basis by which SIRPalpha binds to CD47 and shed new light into the structural mechanisms of SIRP isoform mediated distinctive extracellular interactions and cellular responses.

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Section: Discussionmentioning

confidence: 99%

Functional Elements on SIRPα IgV Domain Mediate Cell Surface Binding to CD47

Liu

Qiao

Zhou

et al. 2007

Journal of Molecular Biology

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“…Microglia can stimulate synaptogenesis through secretion of thrombospondins (TSP) (Chamak et al, 1995;Moller et al, 1996). CD47, thrombospondin-1 receptor and its other ligand SIRPa are co-localized at synaptic level in retinas for example (Mi et al, 2000). Genetic ablation of CD47 results in a loss of SIRPa localization suggesting that CD47 is necessary for the recruitment and localization of SIRPa.…”

Section: Molecular Mechanisms Involved In Microglial Modulation Of Symentioning

confidence: 99%

Microglia in neuronal plasticity: Influence of stress

et al. 2015

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“…CD47 is expressed throughout the brain, with the regions in which it is abundant overlapping extensively with those enriched in SIRPα [5]–[7]. CD47 and SIRPα are both highly expressed in synapse-rich regions [2], [4], [6], and are considered to form a heterophilic complex to mediate bi-directional signaling between cells [2], [8], [9]. Binding of CD47 to SIRPα is required for the tyrosine phosphorylation of SIRPα [10], which is regulated by various receptor-type tyrosine kinases, including tropomyosin-related kinase B (TrkB), as well as the Src family kinases (SFKs) [4].…”

Section: Introductionmentioning

confidence: 99%

Comprehensive Behavioral Analysis of Cluster of Differentiation 47 Knockout Mice

et al. 2014

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Cluster of differentiation 47 (CD47) is a member of the immunoglobulin superfamily which functions as a ligand for the extracellular region of signal regulatory protein α (SIRPα), a protein which is abundantly expressed in the brain. Previous studies, including ours, have demonstrated that both CD47 and SIRPα fulfill various functions in the central nervous system (CNS), such as the modulation of synaptic transmission and neuronal cell survival. We previously reported that CD47 is involved in the regulation of depression-like behavior of mice in the forced swim test through its modulation of tyrosine phosphorylation of SIRPα. However, other potential behavioral functions of CD47 remain largely unknown. In this study, in an effort to further investigate functional roles of CD47 in the CNS, CD47 knockout (KO) mice and their wild-type littermates were subjected to a battery of behavioral tests. CD47 KO mice displayed decreased prepulse inhibition, while the startle response did not differ between genotypes. The mutants exhibited slightly but significantly decreased sociability and social novelty preference in Crawley’s three-chamber social approach test, whereas in social interaction tests in which experimental and stimulus mice have direct contact with each other in a freely moving setting in a novel environment or home cage, there were no significant differences between the genotypes. While previous studies suggested that CD47 regulates fear memory in the inhibitory avoidance test in rodents, our CD47 KO mice exhibited normal fear and spatial memory in the fear conditioning and the Barnes maze tests, respectively. These findings suggest that CD47 is potentially involved in the regulation of sensorimotor gating and social behavior in mice.

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Expression of a synapse-associated membrane protein, P84/SHPS-1, and its ligand, IAP/CD47, in mouse retina

Cited by 61 publications

References 23 publications

Functional Elements on SIRPα IgV Domain Mediate Cell Surface Binding to CD47

Functional Elements on SIRPα IgV Domain Mediate Cell Surface Binding to CD47

Microglia in neuronal plasticity: Influence of stress

Comprehensive Behavioral Analysis of Cluster of Differentiation 47 Knockout Mice

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