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C1q is the target recognition protein of the classical complement pathway and a major connecting link between innate and acquired immunity. As a charge pattern recognition molecule of innate immunity, C1q can engage a broad range of ligands derived from self, non-self and altered self via its heterotrimeric globular (gC1q) domain and thus trigger the classical complement pathway. The trimeric gC1q signature domain has been identified in a variety of non-complement proteins that can be grouped together as a C1q family. C1q circulates in serum as part of the C1 complex, in association with a catalytic tetrameric assembly of two homologous yet distinct serine proteases, C1r and C1s. Binding of C1q to appropriate targets leads to sequential activation of C1r and C1s, the latter being able to cleave complement components C4 and C2 thereby triggering the complement cascade. Activation of the classical pathway plays an important role in innate immune protection against pathogens and damaged elements from self. However, its involvement has been shown in various pathologies including ischemia-reperfusion injury and hereditary angioedema. Unexpected roles for the classical pathway have also been discovered recently, linked to both physiological and pathological aspects of development, including brain and cancer cells. These new perspectives should arouse renewed interest in a search for specific inhibitors of the classical pathway. In addition, C1q has recently been shown to have a number of functions that are independent of the activation of the classical pathway. This research topic is aimed at providing a state-of-the-art overview of the classical pathway, including, but not restricted to emerging functions of C1q and of the C1 complex, as well as pathological consequences of C1 activation or of the presence of anti-C1q autoantibodies . Contributions are included in the areas such as structural basis of C1q ligand recognition, C1q family proteins, inhibitors of the classical pathway identified in pathogens and improved derived inhibitors, structural determinants of the substrate specificities of C1r and C1s, elucidation of the architecture of C1, structural and functional homology of C1 with the initiating complexes of the lectin complement pathway, and novel involvement of C1q in processes such as ageing, cancer, synaptic pruning, and pregnancy.

C1 complex --- classical pathway activation --- Autoimmunity --- c1q --- C1s --- emerging functions --- gC1q structure --- complement --- C1 complex --- classical pathway activation --- Autoimmunity --- c1q --- C1s --- emerging functions --- gC1q structure --- complement

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C1q is the target recognition protein of the classical complement pathway and a major connecting link between innate and acquired immunity. As a charge pattern recognition molecule of innate immunity, C1q can engage a broad range of ligands derived from self, non-self and altered self via its heterotrimeric globular (gC1q) domain and thus trigger the classical complement pathway. The trimeric gC1q signature domain has been identified in a variety of non-complement proteins that can be grouped together as a C1q family. C1q circulates in serum as part of the C1 complex, in association with a catalytic tetrameric assembly of two homologous yet distinct serine proteases, C1r and C1s. Binding of C1q to appropriate targets leads to sequential activation of C1r and C1s, the latter being able to cleave complement components C4 and C2 thereby triggering the complement cascade. Activation of the classical pathway plays an important role in innate immune protection against pathogens and damaged elements from self. However, its involvement has been shown in various pathologies including ischemia-reperfusion injury and hereditary angioedema. Unexpected roles for the classical pathway have also been discovered recently, linked to both physiological and pathological aspects of development, including brain and cancer cells. These new perspectives should arouse renewed interest in a search for specific inhibitors of the classical pathway. In addition, C1q has recently been shown to have a number of functions that are independent of the activation of the classical pathway. This research topic is aimed at providing a state-of-the-art overview of the classical pathway, including, but not restricted to emerging functions of C1q and of the C1 complex, as well as pathological consequences of C1 activation or of the presence of anti-C1q autoantibodies . Contributions are included in the areas such as structural basis of C1q ligand recognition, C1q family proteins, inhibitors of the classical pathway identified in pathogens and improved derived inhibitors, structural determinants of the substrate specificities of C1r and C1s, elucidation of the architecture of C1, structural and functional homology of C1 with the initiating complexes of the lectin complement pathway, and novel involvement of C1q in processes such as ageing, cancer, synaptic pruning, and pregnancy.

C1 complex --- classical pathway activation --- Autoimmunity --- c1q --- C1s --- emerging functions --- gC1q structure --- complement

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Complement C1q --- Immunoglobulin A --- Immunoglobulin G --- Autoantibodies --- Arthritis, Rheumatoid --- immunology --- analysis --- classification --- blood --- immunology

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Complement C1q --- Receptors, Complement --- Autoantibodies --- Complement C1 Inactivator Proteins --- immunology --- immunology --- blood --- physiology

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Marine creatures are rich sources of glycoconjugate-containing glycans and have diversified structures. The advance of genomics has provided a valuable clue for their production and developments. This information will encourage breeding and engineering functional polysaccharides with slime ingredients in algae. These glycans will have the potential for applications to antioxidant, anticancer, and antimicrobial drugs in addition to health supplements and cosmetics. The combination of both biochemical and transcriptome approaches of marine creatures will lead to the opportunity to discover new activities of proteins such as glycan-relating enzymes and lectins. These proteins will also be used for experimental and medical purposes, such as diagnostics and trial studies. The topic of marine glycomics is also focusing on understanding the physiological properties of marine creatures, such as body defense against pathogens and cancers. In the competitions for natural selection, living creatures have evolved both their glycans and their recognition. They have primitive systems of immunity, and few of their mechanisms are closely related to glycans. If we are able to describe the accumulation of data of glycans of creatures living in the seashore and the oceans, we may be able to anticipate a time when we can talk about the ecosystem with glycans. That knowledge will be useful for the development of drugs that cure our diseases and for an understanding of living systems in addition to the preservation of living environments.

Research & information: general --- Biology, life sciences --- Acropora tenuis --- coral --- chemoattraction --- lectin --- white-spotted charr lectin --- oncolytic vaccinia virus --- interferon --- antiviral response --- Chlorella vulgaris --- Dunaliella salina --- Arthrospira platensis --- growth rate --- accumulation of carbohydrates --- biohydrogen --- antibacterial activity --- anticancer activity --- antifungal activity --- Aplysia kurodai --- apoptosis --- Ehrlich ascites carcinoma --- sulfated fucose-rich polysaccharides --- sulfated fucan --- fucosylated chondroitin sulfate --- fucoidan --- oral administration --- anticoagulant activity --- fucosylated glycosaminoglycan --- anticoagulant --- platelet aggregation --- contact activation --- hypotension --- pulmonary embolism --- sulfated polysaccharides --- marine hydrobionts --- antiparasitic activity --- protozoa --- malaria --- leishmaniasis --- trypanosomiasis --- schistosomiasis --- cryptosporidiosis --- trichomoniasis --- bivalve mollusk --- C1q domain-containing --- lectin-like --- pattern recognition receptor --- polysaccharides --- interstitial compartment --- marine worms --- sipunculids --- bioactive properties --- peptides --- rotifera --- pattern recognition receptors --- microbe-associated molecular patterns --- innate immunity --- C-type lectins --- C1q domain-containing proteins --- galectins --- bacterial exopolysaccharides --- bioflocculanting activity --- microalgae growth-promoting bacterium --- harmful algal bloom-forming dinoflagellate --- Alexandrium catenella --- Mameliella alba --- n/a