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C5

Official Full Name
complement C5
Organism
Homo sapiens
GeneID
727
Background
This gene encodes a component of the complement system, a part of the innate immune system that plays an important role in inflammation, host homeostasis, and host defense against pathogens. The encoded preproprotein is proteolytically processed to generate multiple protein products, including the C5 alpha chain, C5 beta chain, C5a anaphylatoxin and C5b. The C5 protein is comprised of the C5 alpha and beta chains, which are linked by a disulfide bridge. Cleavage of the alpha chain by a convertase enzyme results in the formation of the C5a anaphylatoxin, which possesses potent spasmogenic and chemotactic activity, and the C5b macromolecular cleavage product, a subunit of the membrane attack complex (MAC). Mutations in this gene cause complement component 5 deficiency, a disease characterized by recurrent bacterial infections. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2015]
Synonyms
C5D; C5a; C5b; ECLZB; CPAMD4;
Bio Chemical Class
Complement system
Protein Sequence
MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETVLTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGEHLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVWLNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGLNNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC
Open
Disease
Amyloidosis, Cardiovascular disease, Chronic obstructive pulmonary disease, Diabetes mellitus, Diffuse large B-cell lymphoma, Haemolytic anemia, Hidradenitis suppurativa, Macular degeneration, Macular degeneration, Myasthenia gravis, Myasthenia gravis, Pemphigoid, Postoperative inflammation, Retinopathy, Rheumatoid arthritis, Thrombotic microangiopathy
Approved Drug
4 +
Clinical Trial Drug
17 +
Discontinued Drug
3 +

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Detailed Information

Essential for the defense against infections and the control of inflammation, the complement system is a component of every natural immunological reaction. The C5 gene is one of the main participants in this system as it codes for a protein necessary for starting and controlling complement activation. Three primary pathways—the classical route, the lectin pathway, and the alternative pathway—allow the complement system to be triggered by a sequence of enzymatic events. Every one of these routes converges to activate C5, producing two important fragments: C5a and C5b.

Comprising two chains—the C5 alpha chain and the C5 beta chain—linked by a disulfide bridge, the C5 protein is itself a complicated structure. A convertase enzyme activates C5, which is cleaved into C5a, anaphylatoxin is required for the inflammatory response, and C5b, which is essential for the construction of the membrane attack complex (MAC). The strong spasmogenic and chemotactic action of C5a is well-known and greatly helps immune cells be recruited to areas of inflammation. Rising an efficient immune response against infections depends on this recruitment.

However deregulation of the complement system—especially about too high C5a activation—has been linked to several diseases, including peripheral neuropathies. These disorders may provide a special difficulty as the balance between a strong immune response and the possibility of autoimmunity has to be carefully maintained. In this regard, C5 becomes especially important as mutations in the C5 gene may cause complement component 5 insufficiency, a disorder marked by repeated bacterial infections resulting from reduced immune response.

Pathways of Complement Activation

The conventional route starts when immune complexes—more especially, antigen-antibody complexes—bind to C1q. This interaction reveals the Fc region of antibodies, thus enabling the activation of the serine proteases C1r and C1s, which cleave C4 and C2, so producing the C3 convertase. The hydrolyment of C3 depends on the synthesis of this convertase, which subsequently generates the C5 convertase complex enabling the cleavage of C5 into its active components.

By contrast, the lectin pathway is triggered when mannose-binding lectin (MBL) binds certain carbohydrates on the surface of pathogens. MBL interacts with related serine proteases to cleave C4 and C2 in a fashion similar to the classical route, therefore producing the same results in terms of C3 and C5 activation.

But another method may start to complement activation apart from antibodies. The alternate route C3 convertase is formed by the spontaneous hydrolysis of C3 bound to factor B and then cleaved by factor D. A range of surfaces may trigger this pathway, including bacterial cell walls and virus particles, therefore highlighting the quick response capacity of the innate immune system to infections.

Figure 1 describes the activation pathways of the C5a complement system, detailing the classical, lectin, and alternative pathways, along with their mechanisms and implications for immune response.Figure 1.C5a Complement Activation Pathways. (Giorgio C, et al., 2021)

The C5a/C5aR1 Axis and Peripheral Neuropathies

Once produced, C5a works mostly via C5aR1, expressed on many immune cells including neutrophils, macrophages, and T cells. The binding of C5a to C5aR1 sets off a series of intracellular processes leading to inflammation, increased vascular permeability, and the recruitment of extra immune cells to the site of tissue injury or infection. In the setting of peripheral neuropathies, where incorrect activation may cause more pain and tissue damage, this route is very important.

The C5a/C5aR1 axis has been implicated in many kinds of peripheral neuropathy, including Guillain-Barré syndrome, chronic inflammatory demyelinating polyradiculoneuropathy, familial amyloid polyneuropathy, and chemotherapy-induced peripheral neuropathy, according to research. Many times, these disorders include neuroinflammation—where the dysregulation of the complement system aggravates symptoms, therefore causing pain and functional disability.

In the framework of neuropathic pain, the activation of C5a and its receptor has attracted interest for their possible therapeutic target. Stopping this signaling route might provide a fresh technique to treat neuropathic pain not responsive to conventional treatments. Aiming to lower inflammation and related pain without impairing the general immune response, current research is on the development of complement-targeting therapies such as monoclonal antibodies and small compounds that selectively block the C5a/C5aR1 interaction.

Therapeutic Strategies Targeting C5

Therapeutic approaches that alter C5's function are under active research as it is so important for both immune defense and inflammation. Using monoclonal antibodies against C5 or C5aR1, for example, would provide a selective way to reduce improper complement activation. Preclinical research has shown great promise for these medicines, which are progressively being used clinically.

Furthermore under investigation are new allosteric modulators of C5aR as they might control the response of this receptor. Selective modulation of receptor activity might help to maximize the positive effects of complement activation while reducing the negative inflammatory effects related to dysregulated C5a signaling.

References:

  1. Kim BJ, Mastellos DC, Li Y, et al. Targeting complement components C3 and C5 for the retina: Key concepts and lingering questions. Prog Retin Eye Res. 2021;83:100936.
  2. Laursen NS, Magnani F, Gottfredsen RH, et al. Structure, function, and control of complement C5 and its proteolytic fragments. Curr Mol Med. 2012;12(8):1083-1097.
  3. Giorgio C, Zippoli M, Cocchiaro P, et al. Emerging Role of C5 Complement Pathway in Peripheral Neuropathies: Current Treatments and Future Perspectives. Biomedicines. 2021;9(4):399.
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