Ask about this productRelated genes to: C5AR1 Blocking Peptide
- Gene:
- C5AR1 NIH gene
- Name:
- complement C5a receptor 1
- Previous symbol:
- C5R1
- Synonyms:
- C5A, C5AR, CD88
- Chromosome:
- 19q13.32
- Locus Type:
- gene with protein product
- Date approved:
- 1991-12-04
- Date modifiied:
- 2016-08-10
Related products to: C5AR1 Blocking Peptide
Related articles to: C5AR1 Blocking Peptide
- Glioma represents the most common primary malignant tumor of the central nervous system. The complement system, as a key component of the tumor microenvironment (TME), participates in tumor progression by mediating inflammatory responses and immune regulation. However, the specific mechanisms whereby complement system-related genes drive glioma recurrence remain unclear, and robust molecular biomarkers for recurrence prediction are absent. Therefore, this study aims to explore how these genes facilitate glioma progression and recurrence, and to construct a gene signature for recurrence risk prediction. - Source: PubMed
Publication date: 2026/06/25
Sun YanqiBao XiaozhangYang YuhengZhang PeinanTian Nan - C1q is a multifunctional protein, including its role as the initiating protein of the classical complement cascade. While classical pathway activation is involved in synaptic pruning during nervous system development, it also contributes to inflammation and cognitive decline in Alzheimer's disease (AD). Constitutive genetic C1q deficiency has been shown to reduce glial activation and attenuate neuronal loss in AD mouse models, but the specific contributions of microglial C1q to AD pathology while avoiding deficits during post-natal development remain unaddressed. To dissect specific role(s) of microglial C1q in AD progression, we crossed the Cx3cr1 mouse model that deletes C1q from microglia in young adulthood (8 weeks of age) to the aggressive Arctic48 (Arc) amyloidosis mouse model. At 10 months, young adult microglial C1q deletion (Arc C1q) was associated with improved spatial memory performance, despite unchanged amyloid plaque burden. Furthermore, Arc C1q mice exhibited reduced hippocampal C3 protein levels without altering C3 mRNA. No changes were observed in C5aR1, astrocyte GFAP, or microglial Iba1 protein expression. However, Arc C1q mice demonstrated region specific reductions in microglial synaptic engulfment, alongside decreased phagolysosome-associated amyloid in both microglia and astrocytes, and reduced hippocampal amyloid compaction. These findings support a role for C1q in astrocytic C3 induction and the engulfment of both synapses and amyloid. Importantly, young adult microglial C1q inhibition confers cognitive benefits without exacerbating amyloid pathology, suggesting a therapeutic window in which targeting microglial C1q may help preserve synaptic integrity and modulate the neuroinflammatory processes during the later stages of AD. - Source: PubMed
Petrisko Tiffany JChu Shu-HuiGomez-Arboledas AngelaZhang BlossomTenner Andrea J - - Source: PubMed
Publication date: 2026/07/13
Zhang ShuaiZhao XincanTian QiLiu ChengliJiang ShengmingWang GuijunXiang XiLiao JianmingLi Mingchang - Excessive production of complement C5a detected in acute kidney injury (AKI) and during the development of chronic kidney disease (CKD) suggests its possible role in CKD progression, but the underlying mechanism remains unclear. - Source: PubMed
Publication date: 2026/07/10
Ma JingyuanYiu Wai HanLok Sarah W YZou YixinLam Derek KFeng YuchenLai Kar NengZhou WudingKöhl JörgChen MinTang Sydney C W - Activation of the complement cascade is a primary innate immune response mechanism to combat pathogenic infections. Complement anaphylatoxins (i.e., C3a and C5a) exert a robust inflammatory response via prototypical GPCRs (i.e., C3aR and C5aR1). Several peptides derived from anaphylatoxins have shown promise as immunostimulants from therapeutic standpoint by eliciting immune response without excessive inflammation. EP67, a C5a-derived decapeptide, is the most advanced candidate with preclinical indications in antiviral and antibacterial context. Still, the molecular mechanism and the precise receptor target of EP67 remain unclear. Here, we perform a comprehensive pharmacological profiling of EP67 on the human and mouse C3aR and C5aR1 and find that it preferentially activates human C3aR in transducer-coupling assays. Subsequently, we determined four cryo-EM structures of C3aR and C5aR1 in complex with EP67, which elucidate the molecular details of its interaction with, and activation of, these receptors. Interestingly, we observe that EP67 adopts a hook-like structure and binds in the orthosteric pocket of the receptors, analogous to that of the carboxyl terminus of C3a and C5a. We employ site-directed mutagenesis studies to validate the key interactions of EP67 with these receptors and corroborate the structural observations including the engagement of a critical activation switch. Finally, we observe that EP67 induces distinct conformations of the TM7-Helix8 interface for C3aR and C5aR1, which provides a plausible explanation for its ability to preferentially activate C3aR. In summary, our study elucidates molecular insights into the interaction of EP67 with the complement anaphylatoxin receptors, and it should facilitate further optimization for therapeutic applications. - Source: PubMed
Publication date: 2026/07/08
Dalal AnnuYadav Manish KGanguly ManisankarMishra SudhaYadav RaviSinha ShachieRoy NabarunTiwari DivyanshuMukherjee DebdattaReyaz AshnaDsouza Calvin ANigam AmeeshaBanerjee NilanjanaLi Xaria XClark Richard JWoodruff Trent MBanerjee RamanujGati CorneliusShukla Arun K