Complement Subcomponent C1s
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Complement Subcomponent C1s
Complement component 1s (, '' C1 esterase'', ''activated complement C1s'', ''complement C overbar 1r'', ''C1s'') is a protein involved in the complement system. C1s is part of the C1 complex. In humans, it is encoded by the ''C1S'' gene. C1s cleaves C4 and C2, which eventually leads to the production of the classical pathway C3-convertase. See also * C1q - another part of the C1 complex * C1r - another part of the C1 complex * MASP-2 - a protein similar to C1s, part of the lectin pathway The lectin pathway or MBL pathway is a type of cascade reaction in the complement system, similar in structure to the classical complement pathway, in that, after activation, it proceeds through the action of C4 and C2 to produce activated comple ... References Further reading * * * * * * * * * * * * * * * * * * * * External links * * Complement system EC 3.4.21 {{gene-12-stub ...
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C1 Esterase
C1-inhibitor (C1-inh, C1 esterase inhibitor) is a protease inhibitor belonging to the serpin superfamily. Its main function is the inhibition of the complement system (C1r, C1s) to prevent spontaneous activation but also as the major regulator of the contact system (PK, FXIIa, and FXIa). Proteomics C1-inhibitor is the largest member among the ''serpin'' superfamily of proteins. It can be noted that, unlike most family members, C1-inhibitor has a 2-domain structure. The C-terminal serpin domain is similar to other serpins, which is the part of C1-inhibitor that provides the inhibitory activity. The N-terminal domain (also some times referred to as the ''N-terminal tail'') is not essential for C1-inhibitor to inhibit proteases. This domain has no similarity to other proteins. C1-inhibitor is highly glycosylated, bearing both ''N''- and ''O''-glycans. N-terminal domain is especially heavily glycosylated. Role in disease Deficiency of this protein is associated with heredi ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metabolic reactions, DNA replication, Cell signaling, responding to stimuli, providing Cytoskeleton, structure to cells and Fibrous protein, organisms, and Intracellular transport, transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the Nucleic acid sequence, nucleotide sequence of their genes, and which usually results in protein folding into a specific Protein structure, 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called pep ...
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Complement System
The complement system, also known as complement cascade, is a part of the humoral, innate immune system and enhances (complements) the ability of antibodies and phagocytic cells to clear microbes and damaged cells from an organism, promote inflammation, and attack the pathogen's cell membrane. Despite being part of the innate immune system, the complement system can be recruited and brought into action by antibodies generated by the adaptive immune system. The complement system consists of a number of small, inactive, liver synthesized protein precursors circulating in the blood. When stimulated by one of several triggers, proteases in the system cleave specific proteins to release cytokines and initiate an amplifying cascade of further cleavages. The end result of this ''complement activation'' or ''complement fixation'' cascade is stimulation of phagocytes to clear foreign and damaged material, inflammation to attract additional phagocytes, and activation of the cell-killi ...
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C1 Complex
The C1 complex (''complement component 1'', ''C1'') is a protein complex involved in the complement system. It is the first component of the classical complement pathway and is composed of the subcomponents C1q, C1r and C1s. Structure The C1 complex is ~790 kDa and is composed of 1 molecule of C1q, 2 molecules of C1r and 2 molecules of C1s, or ''C1qr2s2''. Function Activation of the C1 complex initiates the classical complement pathway. This occurs when C1q binds to antigen-antibody complexes. The antibodies IgM or certain subclasses of IgG complexed with antigens are able to initiate the complement system: a single pentameric IgM can initiate the pathway, while several monomeric IgG molecules are needed. C1q can also be activated in other ways, for example by binding to pentraxins such as C-reactive protein or directly to the surface of pathogens. Such binding of C1q leads to conformational changes in the C1q molecule, which activates the associated C1r molecules. ...
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Gene
In biology, the word gene has two meanings. The Mendelian gene is a basic unit of heredity. The molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protein-coding genes and non-coding genes. During gene expression (the synthesis of Gene product, RNA or protein from a gene), DNA is first transcription (biology), copied into RNA. RNA can be non-coding RNA, directly functional or be the intermediate protein biosynthesis, template for the synthesis of a protein. The transmission of genes to an organism's offspring, is the basis of the inheritance of phenotypic traits from one generation to the next. These genes make up different DNA sequences, together called a genotype, that is specific to every given individual, within the gene pool of the population (biology), population of a given species. The genotype, along with environmental and developmental factors, ultimately determines the phenotype ...
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Complement Component 4
Complement component 4 (C4), in humans, is a protein involved in the intricate complement system, originating from the human leukocyte antigen (HLA) system. It serves a number of critical functions in immunity, tolerance, and autoimmunity with the other numerous components. Furthermore, it is a crucial factor in connecting the recognition pathways of the overall system instigated by antibody-antigen (Ab-Ag) complexes to the other effector proteins of the innate immune response. For example, the severity of a dysfunctional complement system can lead to fatal diseases and infections. Complex variations of it can also lead to schizophrenia. The C4 protein was thought to derive from a simple two-locus allelic model, which however has been replaced by a much more sophisticated multimodular RCCX gene complex model which contain long and short forms of the C4A or C4B genes usually in tandem RCCX cassettes with copy number variation, that somewhat parallels variation in the levels of the ...
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Complement Component 2
Complement C2 is a protein that in humans is encoded by the ''C2'' gene. The protein encoded by this gene is part of the classical pathway of the complement system, acting as a multi-domain serine protease. Deficiency of C2 has been associated with certain autoimmune diseases. The Complement system is generated to regulate self protection from infection. The overall Complement system is composed of protein groups that collaborate in destroying foreign invaders, which ultimately remove debris from cells and tissues. When the body detects a foreign invader, the body signals the Complement system and the Complement component 2 protein attaches to Complement system 4 resulting in aimmune response.Complement component 2 protein is critical for regulating the body's immune response. Function In the classical and lectin pathways of complement activation, formation of the C3-convertase and C5-convertases requires binding of C2 to an activated surface-bound C4b in the presence of Mg ...
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Classical Complement Pathway
The classical complement pathway is one of three pathways which activate the complement system, which is part of the immune system. The classical complement pathway is initiated by antigen-antibody complexes with the antibody isotypes IgG and IgM. Following activation, a series of proteins are recruited to generate C3 convertase (C4b2b, historically referred C4b2a), which cleaves the C3 protein. The C3b component of the cleaved C3 binds to C3 convertase (C4b2b) to generate C5 convertase (C4b2b3b), which cleaves the C5 protein. The cleaved products attract phagocytes to the site of infection and tags target cells for elimination by phagocytosis. In addition, the C5 convertase initiates the terminal phase of the complement system, leading to the assembly of the membrane attack complex (MAC). The membrane attack complex creates a pore on the target cell's membrane, inducing cell lysis and death. The classical complement pathway can also be activated by apoptotic cells, nec ...
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C3-convertase
C3 convertase (''C4bC2b'', formerly ''C4b2a'') belongs to family of serine proteases and is necessary in innate immunity as a part of the complement system which eventuate in opsonisation of particles, release of inflammatory peptides, C5 convertase formation and cell lysis. C3 convertase can be used to refer to the form produced in the alternative pathway (C3bBb) or the classical and lectin pathways (C4bC2b, formerly C4b2a). Once formed, both C3 convertases will catalyze the proteolytic cleavage of C3 into C3a and C3b (hence the name "C3-convertase"). The smaller fragment called C3a serves to increase vascular permeability and promote extravasation of phagocytes, while the larger C3b fragment can be used as an opsonin or bind to either type of C3 convertase to form the trimolecular C5 convertase to activate C5 for the membrane attack complex. Formation C3 convertase formation can occur in three different pathways: the classical, lectin, and alternative pathways. A ...
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Droga Klasyczna
''Droga'' (, Polish for 'road') was a monthly magazine dedicated to literary and social topics. It was published in Nazi-occupied Warsaw from December 1943 to April 1944. Its founders were Ewa Pohoska and Juliusz Garztecki. See also * List of magazines in Poland The following is a list of notable current and defunct magazines in Poland. In the country, there are also English-language magazines in addition to those published in Polish language, Polish. In terms of frequency, the Polish magazines are mostly ... References 1943 establishments in Poland 1944 disestablishments in Poland Defunct literary magazines published in Poland Poland in World War II Magazines established in 1943 Magazines disestablished in 1944 Magazines published in Warsaw Monthly magazines published in Poland Polish-language magazines Polish underground press in World War II {{WWII-stub ...
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Complement Component 1q
The complement component 1q (or simply C1q) is a protein complex involved in the complement system, which is part of the innate immune system. C1q together with C1r and C1s form the C1 complex. Antibodies of the adaptive immune system can bind antigen, forming an antigen-antibody complex. When C1q binds antigen-antibody complexes, the C1 complex becomes activated. Activation of the C1 complex initiates the classical complement pathway of the complement system. The antibodies IgM and all IgG subclasses except IgG4 are able to initiate the complement system. Structure C1q is a 460 kDa protein formed from 18 peptide chains in 3 subunits of 6. Each 6 peptide subunit consists of a Y-shaped pair of triple peptide helices joined at the stem and ending in a globular non-helical head. The 80-amino acid helical component of each triple peptide contain many Gly-X-Y sequences, where X and Y are proline, isoleucine, or hydroxylysine; they, therefore, strongly resemble collagen fibr ...
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Complement Component 1r
Complement C1r subcomponent (, ''activated complement C1r'', ''C overbar 1r esterase'', ''C1r'') is a protein involved in the complement system of the innate immune system. In humans, C1r is encoded by the ''C1R'' gene. C1r along with C1q and C1s form the C1 complex, which is the first component of the serum complement system. C1r is an enzyme that activates C1s to its active form, by proteolysis, proteolytic cleavage. Clinical significance *Ehlers–Danlos syndromes, Ehlers–Danlos syndrome Periodontal type is associated with mutations in the ''CR1'' gene Function C1r has been shown to Protein-protein interaction, interact with C1s. C1r proteolysis, cleaves C1s to form the active form of C1s. References Further reading * * * * * * * * * * * * * * * * * * * * External links

* * Complement system EC 3.4.21 {{protein-stub ...
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