ArticleFrontiers in immunology2018
Is the A-Chain the Engine That Drives the Diversity of C1q Functions? Revisiting Its Unique Structure.
Article in Frontiers in immunology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- New insights into the role of complement system in colorectal cancer (Review).Molecular medicine reports · 2025Review
- Complement in Human Brain Health: Potential of Dietary Food in Relation to Neurodegenerative Diseases.Foods (Basel, Switzerland) · 2023Review
- Understanding the contextual functions of C1q and LAIR-1 and their applications.Experimental & molecular medicine · 2022Review
- Discoidin Domain Receptor 1, a Potential Biomarker and Therapeutic Target in Hepatocellular Carcinoma.International journal of general medicine · 2022Review
- Autoantibodies against complement component C1q in systemic lupus erythematosus.Clinical & translational immunology · 2021Review
- C1q A08 Is a Half-Cryptic Epitope of Anti-C1q A08 Antibodies in Lupus Nephritis and Important for the Activation of Complement Classical Pathway.Frontiers in immunology · 2020Article
- Is the Complement Protein C1q a Pro- or Anti-tumorigenic Factor? Bioinformatics Analysis Involving Human Carcinomas.Frontiers in immunology · 2019Article
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Authors and funding
4 authors.
Funding
Abstract
The immunopathological functions associated with human C1q are still growing in terms of novelty, diversity, and pathologic relevance. It is, therefore, not surprising that C1q is being recognized as an important molecular bridge between innate and adaptive immunity. The secret of this functional diversity, in turn, resides in the elegant but complex structure of the C1q molecule, which is assembled from three distinct gene products: A, B, and C, each of which has evolved from a separate and unique ancestral gene template. The C1q molecule is made up of 6A, 6B, and 6C polypeptide chains, which are held together through strong covalent and non-covalent bonds to form the 18-chain, bouquet-of-flower-like protein that we know today. The assembled C1q protein displays at least two distinct structural and functional regions: the collagen-like region (cC1q) and the globular head region (gC1q), each being capable of driving a diverse range of ligand- or receptor-mediated biological functions. What is most intriguing, however, is the observation that most of the functions appear to be predominantly driven by the A-chain of the molecule, which begs the question: what are the evolutionary modifications or rearrangements that singularly shaped the primordial A-chain gene to become a pluripotent and versatile component of the intact C1q molecule? Here, we revisit and discuss some of the known unique structural and functional features of the A-chain, which may have contributed to its versatility.
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