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Cathepsins
Cathepsins (Ancient Greek ''kata-'' "down" and ''hepsein'' "boil"; abbreviated CTS) are proteases ( enzymes that degrade proteins) found in all animals as well as other organisms. There are approximately a dozen members of this family, which are distinguished by their structure, catalytic mechanism, and which proteins they cleave. Most of the members become activated at the low pH found in lysosomes. Thus, the activity of this family lies almost entirely within those organelles. There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption. Cathepsins have a vital role in mammalian cellular turnover. Classification * Cathepsin A (serine protease) * Cathepsin B (cysteine protease) * Cathepsin C (cysteine protease) * Cathepsin D (aspartyl protease) * Cathepsin E (aspartyl protease) * Cathepsin F (cysteine proteinase) * Cathepsin G (serine protease) * Cathepsin H (cysteine protease) * Cathepsin K (cysteine prote ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin B
Cathepsin B belongs to a family of lysosomal cysteine proteases known as the cysteine cathepsins and plays an important role in intracellular proteolysis. In humans, cathepsin B is encoded by the ''CTSB'' gene. Cathepsin B is upregulated in certain cancers, in pre-malignant lesions, and in various other pathological conditions. Structure Gene The ''CTSB'' gene is located at chromosome 8p22, consisting of 13 exons. The promoter of CTSB gene contains a GC-rich region including many SP1 sites, which is similar to housekeeping genes. At least five transcript variants encoding the same protein have been found for this gene. Protein Cathepsin B is synthesized on the rough endoplasmic reticulum as a preproenzyme of 339 amino acids with a signal peptide of 17 amino acids. Procathepsin B of 43/46 kDa is then transported to the Golgi apparatus, where cathepsin B is formed. Mature cathepsin B is composed of a heavy chain of 25-26 kDa and a light chain of 5kDa, which are linked by a di ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cysteine Cathepsin
Papain-like proteases (or papain-like (cysteine) peptidases; abbreviated PLP or PLCP) are a large protein family of cysteine protease enzymes that share structural and enzymatic properties with the group's namesake member, papain. They are found in all domains of life. In animals, the group is often known as cysteine cathepsins or, in older literature, lysosomal peptidases. In the MEROPS protease enzyme classification system, papain-like proteases form Clan CA. Papain-like proteases share a common catalytic dyad active site featuring a cysteine amino acid residue that acts as a nucleophile. The human genome encodes eleven cysteine cathepsins which have a broad range of physiological functions. In some parasites papain-like proteases have roles in host invasion, such as cruzipain from '' Trypanosoma cruzi''. In plants, they are involved in host defense and in development. Studies of papain-like proteases from prokaryotes have lagged their eukaryotic counterparts. In cell ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin L1
Cathepsin L1 is a protein that in humans is encoded by the ''CTSL1'' gene. The protein is a cysteine cathepsin, a lysosomal cysteine protease that plays a major role in intracellular protein catabolism. Function Cathepsin L1 is a member of the Peptidase C1 (cathepsin) MEROPS family, which plays an important role in diverse processes including normal lysosome mediated protein turnover, antigen and proprotein processing, and apoptosis. Its substrates include collagen and elastin, as well as alpha-1 protease inhibitor, a major controlling element of neutrophil elastase activity. The encoded protein has been implicated in several pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. This protein, which is a member of the peptidase C1 family, is a dimer composed of disulfide-linked heavy and light chains, both produced from a single protein precursor. At least two transcript variants encoding ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin H
Cathepsin H is a protein that in humans is encoded by the ''CTSH'' gene. The protein encoded by this gene is a cysteine cathepsin, a lysosomal cysteine protease important in the overall degradation of lysosomal proteins. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. The encoded protein, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of this gene has been correlated with malignant progression of prostate tumors. Two transcript variants encoding different isoforms have been found for this gene. References Further reading * * * * * * * * * * * * * * * * * * * External links * The MEROPS MEROPS is an online database for peptidases (also known as proteases, proteinases and proteolytic enzymes) and their inhibitors. The classification scheme for peptidases was published by Rawlings & Barrett in 1993, and that for protein inh ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin G
Cathepsin G is a protein that in humans is encoded by the ''CTSG'' gene. It is one of the three serine proteases of the chymotrypsin family that are stored in the azurophil granules, and also a member of the peptidase S1 protein family. Cathepsin G plays an important role in eliminating intracellular pathogens and breaking down tissues at inflammatory sites, as well as in anti-inflammatory response. Structure Gene The CTSG gene is located at chromosome 14q11.2, consisting of 5 exons. Each residue of the catalytic triad is located on a separate exon. Five polymorphisms have been identified by scanning the entire coding region. Cathepsin G is one of those homologous protease that evolved from a common ancestor by gene duplication. Protein Cathepsin G is a 255- amino-acid-residue protein including an 18-residue signal peptide, a two-residue activation peptide at the N-terminus and a carboxy terminal extension. The activity of cathepsin G depends on a catalytic triad composed of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin E
Cathepsin E is an enzyme () that in humans is encoded by the ''CTSE'' gene. The enzyme is also known as ''slow-moving proteinase'', ''erythrocyte membrane aspartic proteinase'', ''SMP'', ''EMAP'', ''non-pepsin proteinase'', ''cathepsin D-like acid proteinase'', ''cathepsin E-like acid proteinase'', ''cathepsin D-type proteinase'') is an enzyme. Cathepsin E is a protease found in animals, as well as various other organisms, that belongs to the aspartic protease group. In humans it is encoded by the CTSE gene located at 1q32 on chromosome 1. It is an intracellular non-lysosomal glycoprotein that is mainly found in the skin and in immune cells. The protein is an aspartyl protease that functions as a disulfide-linked homodimer, and has an oligosaccharide chain of the high-mannose type. It is a member of the peptidase A1 family, and therefore observes specificity similar to that of Pepsin A and Cathepsin D. Cathepsin E is an intracellular enzyme and does not appear to be involved in d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin D
Cathepsin D is a protein that in humans is encoded by the ''CTSD'' gene. This gene encodes a lysosomal aspartyl protease composed of a protein dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes. The main function of cathepsin D is to degrade proteins and activate precursors of bioactive proteins in pre-lysosomal compartments. This proteinase, which is a member of the peptidase A1 family, has a specificity similar to but narrower than that of pepsin A. Transcription of the ''CTSD'' gene is initiated from several sites, including one that is a start site for an estrogen-regulated transcript. Mutations in this gene are involved in the pathogenesis of several diseases, including breast cancer and possibly Alzheimer disease. Homozygous deletion of the ''CTSD'' gene leads to early lethality in the postnatal phase. Deficiency of ''CTSD'' gene has ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin C
Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo- cysteine protease belonging to the peptidase C1 protein family, a subgroup of the cysteine cathepsins. In humans, it is encoded by the ''CTSC'' gene. Function Cathepsin C appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. Cathepsin C catalyses excision of dipeptides from the N-terminus of protein and peptide substrates, except if (i) the amino group of the N-terminus is blocked, (ii) the site of cleavage is on either side of a proline residue, (iii) the N-terminal residue is lysine or arginine, or (iv) the structure of the peptide or protein prevents further digestion from the N-terminus. Structure The cDNAs encoding rat, human, murine, bovine, dog and two '' Schistosome'' cathepsin Cs have been cloned and sequenced and show that the enzyme is highly conserved. The human and rat cathepsin C cDNAs encode precursors (prepro-cathepsin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin W
Cathepsin W is a protein that in humans is encoded by the ''CTSW'' gene. The protein encoded by this gene, a member of the peptidase C1 family of cysteine cathepsins, is a cysteine protease cathepsin that may have a specific function in the mechanism or regulation of T-cell cytolytic activity. The encoded protein is found associated with the cell membrane inside the endoplasmic reticulum of natural killer and cytotoxic T-cells. Expression of this gene is up-regulated by interleukin-2. References Further reading * * * * * * * * * * External links * The MEROPS MEROPS is an online database for peptidases (also known as proteases, proteinases and proteolytic enzymes) and their inhibitors. The classification scheme for peptidases was published by Rawlings & Barrett in 1993, and that for protein inhibitor ... online database for peptidases and their inhibitorsC01.037 Proteases EC 3.4.22 Cathepsins {{gene-11-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin F
Cathepsin F is a protein that in humans is encoded by the ''CTSF'' gene. Cysteine cathepsins are a family of cysteine proteases that represent a major component of the lysosomal proteolytic system. In general, cathepsins contain a signal peptide, followed by a propeptide and then a catalytically active mature region. The very long (251-amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of Cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. The cathepsin F proregion is unique within the papain family cysteine proteases in that it contains this additional N-terminal segment predicted to share structural similarities with cysteine protease inhibitors of the cystatin superfamily. This cystatin-like domain contains some of the elements known to be important for inhibitory activity. CTSF encodes a predicted protein of 484 amino acids that contain ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin Z
Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the ''CTSZ'' gene. It is a member of the cysteine cathepsin family of cysteine proteases, which has 11 members. As one of the 11 cathepsins, cathepsin Z contains distinctive features from others. Cathepsin Z has been reported involved in cancer malignancy and inflammation. Structure Gene The ''CTSZ'' gene is located at 20q13.32 on chromosome 20, consisting of 6 exons. At least two transcript variants of this gene have been found, but the full-length nature of only one of them has been determined. Protein Cathepsin Z is characterized by an unusual and unique 3-amino acid insertion in the highly conserved region between the glutamine of the putative oxynion hole and the active site cysteine. The pro-region of cathepsin Z shares no significant similarity with other cathepsin family sequences. It contains only 41 amino acid residues without the conserved motif of ERFNIN or GNFD found in ot ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin A
Cathepsin A is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the ''CTSA'' gene. Function This gene encodes a glycoprotein that associates with lysosomal enzymes beta-galactosidase and neuraminidase to form a complex of high-molecular-weight multimers. The formation of this complex provides a protective role for stability and activity. It is protective for β-galactosidase and neuraminidase. Clinical significance Deficiencies in this gene are linked to multiple forms of galactosialidosis. Interactions Cathepsin A has been shown to interact Advocates for Informed Choice, dba interACT or interACT Advocates for Intersex Youth, is a 501(c)(3) nonprofit organization using innovative strategies to advocate for the legal and human rights of children with intersex traits. The organizat ... with NEU1. References Further reading * * * * * * * * * * * * * * * * * * * * External links * EC 3.4.16 Prot ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
