cathepsin C

WordNet

1. the 3rd letter of the Roman alphabet (同)c
2. (music) the keynote of the scale of C major
3. a general-purpose programing language closely associated with the UNIX operating system

PrepTutorEJDIC

1. carbonの化学記号
2. cesiumの化学記号
3. cadmiumの化学記号

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/07/04 18:36:00」(JST)

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Cathepsin C
PDB rendering based on 1k3b.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1K3B, 2DJF, 2DJG, 3PDF, 4CDC, 4CDD, 4CDE, 4CDF
Identifiers
Symbols	CTSC ; CPPI; DPP-I; DPP1; DPPI; HMS; JP; JPD; PALS; PDON1; PLS
External IDs	OMIM: 602365 MGI: 109553 HomoloGene: 1373 IUPHAR: 2344 ChEMBL: 2252 GeneCards: CTSC Gene
EC number	3.4.14.1
Gene ontology Molecular function • serine-type endopeptidase activity • protein binding • cysteine-type peptidase activity • peptidase activator activity involved in apoptotic process • phosphatase binding • chloride ion binding • identical protein binding • protein self-association • chaperone binding Cellular component • extracellular space • lysosome • endoplasmic reticulum • Golgi apparatus • membrane • extracellular vesicular exosome Biological process • T cell mediated cytotoxicity • proteolysis • apoptotic process • immune response • aging • response to organic substance • positive regulation of proteolysis involved in cellular protein catabolic process • positive regulation of apoptotic signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1075	13032
Ensembl	ENSG00000109861	ENSMUSG00000030560
UniProt	P53634	P97821
RefSeq (mRNA)	NM_001114173	NM_009982
RefSeq (protein)	NP_001107645	NP_034112
Location (UCSC)	Chr 11: 88.03 – 88.07 Mb	Chr 7: 88.28 – 88.31 Mb
PubMed search	[1]	[2]

Cathepsin C exclusion domain
re-determination of the native structure of human dipeptidyl peptidase i (cathepsin c)
Identifiers
Symbol	CathepsinC_exc
Pfam	PF08773
InterPro	IPR014882
SCOP	1k3b
SUPERFAMILY	1k3b
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase C1 family. 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 C) comprising signal peptides of 24 residues, pro-regions of 205 (rat cathepsin C) or 206 (human cathepsin C) residues and catalytic domains of 233 residues which contain the catalytic residues and are 30-40% identical to the mature amino acid sequences of papain and a number of other cathepsins including cathepsins, B, H, K, L, and S.

The translated prepro-cathepsin C is processed into the mature form by at least four cleavages of the polypeptide chain. The signal peptide is removed during translocation or secretion of the pro-enzyme (pro-cathepsin C) and a large N-terminal proregion fragment (also known as the exclusion domain), which is retained in the mature enzyme, is separated from the catalytic domain by excision of a minor C-terminal part of the pro-region, called the activation peptide. A heavy chain of about 164 residues and a light chain of about 69 residues are generated by cleavage of the catalytic domain.

Unlike the other members of the papain family, mature cathepsin C consists of four subunits, each composed of the N-terminal proregion fragment, the heavy chain and the light chain. Both the pro-region fragment and the heavy chain are glycosylated.

Clinical significance

Defects in the encoded protein have been shown to be a cause of Papillon-Lefevre disease, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis.

Cathepsin C functions as a key enzyme in the activation of granule serine peptidases in inflammatory cells, such as elastase and cathepsin G in neutrophils cells and chymase and tryptase in mast cells. In many inflammatory diseases, such as Rheumatoid Arthritis, Chronic Obstructive Pulmonary Disease (COPD), Inflammatory Bowel Disease, Asthma, Sepsis and Cystic Fibrosis, a significant part of the pathogenesis is caused by increased activity of some of these inflammatory proteases. Once activated by cathepsin C, the proteases are capable of degrading various extracellular matrix components, which can lead to tissue damage and chronic inflammation.

References

Further reading

• McGuire MJ, Lipsky PE, Thiele DL (1992). "Purification and characterization of dipeptidyl peptidase I from human spleen". Arch. Biochem. Biophys. 295 (2): 280–8. doi:10.1016/0003-9861(92)90519-3. PMID 1586157. 
• Paris A, Strukelj B, Pungercar J et al. (1995). "Molecular cloning and sequence analysis of human preprocathepsin C". FEBS Lett. 369 (2–3): 326–30. doi:10.1016/0014-5793(95)00777-7. PMID 7649281. 
• Dolenc I, Turk B, Pungercic G et al. (1995). "Oligomeric structure and substrate induced inhibition of human cathepsin C". J. Biol. Chem. 270 (37): 21626–31. doi:10.1074/jbc.270.37.21626. PMID 7665576. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Rao NV, Rao GV, Hoidal JR (1997). "Human dipeptidyl-peptidase I. Gene characterization, localization, and expression". J. Biol. Chem. 272 (15): 10260–5. doi:10.1074/jbc.272.15.10260. PMID 9092576. 
• Fischer J, Blanchet-Bardon C, Prud'homme JF et al. (1997). "Mapping of Papillon-Lefevre syndrome to the chromosome 11q14 region". Eur. J. Hum. Genet. 5 (3): 156–60. PMID 9272739. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Cigić B, Krizaj I, Kralj B et al. (1998). "Stoichiometry and heterogeneity of the pro-region chain in tetrameric human cathepsin C". Biochim. Biophys. Acta 1382 (1): 143–50. doi:10.1016/S0167-4838(97)00173-8. PMID 9507095. 
• Toomes C, James J, Wood AJ et al. (1999). "Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis". Nat. Genet. 23 (4): 421–4. doi:10.1038/70525. PMID 10581027. 
• Hart TC, Hart PS, Bowden DW et al. (2000). "Mutations of the cathepsin C gene are responsible for Papillon-Lefèvre syndrome". J. Med. Genet. 36 (12): 881–7. doi:10.1136/jmg.36.12.881. PMC 1734286. PMID 10593994. 
• Hart TC, Hart PS, Michalec MD et al. (2000). "Haim-Munk syndrome and Papillon-Lefèvre syndrome are allelic mutations in cathepsin C". J. Med. Genet. 37 (2): 88–94. doi:10.1136/jmg.37.2.88. PMC 1734521. PMID 10662807. 
• Hart TC, Hart PS, Michalec MD et al. (2000). "Localisation of a gene for prepubertal periodontitis to chromosome 11q14 and identification of a cathepsin C gene mutation". J. Med. Genet. 37 (2): 95–101. doi:10.1136/jmg.37.2.95. PMC 1734516. PMID 10662808. 
• Suzuki Y, Ishihara D, Sasaki M et al. (2000). "Statistical analysis of the 5' untranslated region of human mRNA using "Oligo-Capped" cDNA libraries". Genomics 64 (3): 286–97. doi:10.1006/geno.2000.6076. PMID 10756096. 
• Cigić B, Dahl SW, Pain RH (2000). "The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme". Biochemistry 39 (40): 12382–90. doi:10.1021/bi0008837. PMID 11015218. 
• Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–1795. doi:10.1101/gr.143000. PMC 310948. PMID 11076863. 
• Hart PS, Zhang Y, Firatli E et al. (2001). "Identification of cathepsin C mutations in ethnically diverse papillon-Lefèvre syndrome patients". J. Med. Genet. 37 (12): 927–32. doi:10.1136/jmg.37.12.927. PMC 1734492. PMID 11106356. 
• Zhang Y, Lundgren T, Renvert S et al. (2001). "Evidence of a founder effect for four cathepsin C gene mutations in Papillon-Lefèvre syndrome patients". J. Med. Genet. 38 (2): 96–101. doi:10.1136/jmg.38.2.96. PMC 1734811. PMID 11158173. 
• Nakano A, Nomura K, Nakano H et al. (2001). "Papillon-Lefèvre syndrome: mutations and polymorphisms in the cathepsin C gene". J. Invest. Dermatol. 116 (2): 339–43. doi:10.1046/j.1523-1747.2001.01244.x. PMID 11180012. 
• Allende LM, García-Pérez MA, Moreno A et al. (2001). "Cathepsin C gene: First compound heterozygous patient with Papillon-Lefèvre syndrome and a novel symptomless mutation". Hum. Mutat. 17 (2): 152–3. doi:10.1002/1098-1004(200102)17:2<152::AID-HUMU10>3.0.CO;2-#. PMID 11180601. 
• Wiemann S, Weil B, Wellenreuther R et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166. 

External links

• The MEROPS online database for peptidases and their inhibitors: C01.070
• Cathepsin C at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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English Journal

• The Synthesis of α,α-Disubstituted α-Amino Acids via Ichikawa Rearrangement.

• Szcześniak P1, Pieczykolan M1, Stecko S1.
• The Journal of organic chemistry.J Org Chem.2016 Feb 5;81(3):1057-74. doi: 10.1021/acs.joc.5b02628. Epub 2016 Jan 12.
• An approach to α,α-disubstituted α-amino acids is reported. The key step is allyl cyanate-to-isocyanate rearrangement. As demonstrated, the resultant allyl isocyanates can be directly trapped with various nucleophiles, for instance, alcohols, amines, and organometallic reagents, to provide a broa
• PMID 26726732

• Analysis of urinary cathepsin C for diagnosing Papillon-Lefèvre syndrome.

• Hamon Y1,2,3,4, Legowska M5, Fergelot P6,7,8, Dallet-Choisy S1,2, Newell L9, Vanderlynden L1,2, Kord Valeshabad A10, Acrich K11, Kord H12, Charalampos T9, Morice-Picard F13, Surplice I9, Zoidakis J14, David K11, Vlahou A14, Ragunatha S15, Nagy N16,17,18, Farkas K16,17,18, Széll M16,17,18, Goizet C6,8, Schacher B19, Battino M20,21, Al Farraj Aldosari A22, Wang X23, Liu Y24, Marchand-Adam S1,2, Lesner A5, Kara E25, Korkmaz-Icöz S26, Moss C9,27, Eickholz P19, Taieb A13, Kavukcu S28, Jenne DE3,4, Gauthier F1,2, Korkmaz B1,2.
• The FEBS journal.FEBS J.2016 Feb;283(3):498-509. doi: 10.1111/febs.13605. Epub 2016 Jan 4.
• Papillon-Lefèvre syndrome (PLS) (OMIM: 245000) is a rare disease characterized by severe periodontitis and palmoplantar keratoderma. It is caused by mutations in both alleles of the cathepsin C (CatC) gene CTSC that completely abrogate the proteolytic activity of this cysteine proteinase. Most ofte
• PMID 26607765

• Regulation of split anergy in natural killer cells by inhibition of cathepsins C and H and cystatin F.

• Magister Š1, Tseng HC2, Bui VT2, Kos J1,3, Jewett A2,4.
• Oncotarget.Oncotarget.2015 Sep 8;6(26):22310-27.
• Freshly isolated human primary NK cells induce preferential lysis of Oral Squamous Carcinoma Stem Cells (OSCSCs) when compared to differentiated Oral Squamous Carcinoma Cells (OSCCs), while anti-CD16 antibody and monocytes induce functional split anergy in primary NK cells by decreasing the cytotoxi
• PMID 26247631

Japanese Journal

• Cobalt protoporphyrin represses osteoclastogenesis through blocking multiple signaling pathways

• Yashima Yuka,Okamoto Kuniaki,Sakai Eiko,Iwatake Mayumi,Fukuma Yutaka,Nishishita Kazuhisa,Tsukuba Takayuki
• BioMetals 28(4), 725-732, 2015-08
• … CoPP suppressed the protein levels of nuclear factor of activated T cells cytoplasmic-1 (NFATc1) as well as those of OCLs markers such as Src and cathepsin K, which are transcriptionally regulated by NFATc1 in mature OCLs. …
• NAID 120005624091

• Status of autophagy, lysosome activity and apoptosis during corpus luteum regression in cattle

• ABOELENAIN Mansour,KAWAHARA Manabu,BALBOULA Ahmed Zaky [他]
• The journal of reproduction and development 61(3), 229-236, 2015-06
• NAID 40020494171

Related Links

• cathepsin C Antibody (D-6) | Santa Cruz Biotech

cathepsin C Antibody (D-6) is a mouse monoclonal IgG 1 provided at 200 µg/ml raised against amino acids 251-394 mapping mapping to the heavy chain of cathepsin C of human origin recommended for detection of cathepsin C of ...

• cathepsin C Antibody (L-14) | Santa Cruz Biotech

cathepsin C Antibody (L-14) is a goat polyclonal IgG provided at 200 µg/ml epitope mapping within an internal region of cathepsin C of human origin recommended for detection of cathepsin C of mouse, rat and human origin by WB, IF ...

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★リンクテーブル★

リンク元	「カテプシンC」「dipeptidyl peptidase I」
関連記事	「C」「Cs」「Cd」「c」

「カテプシンC」

　　[★]

英

cathepsin C

関

ジペプチジルペプチダーゼI

「dipeptidyl peptidase I」

　　[★]

ジペプチジルペプチダーゼI

関

cathepsin C

「C」

　　[★]

• 炭素 carbon
• シトシン cytosine
• システイン cysteine
• シチジン
• セルシウス度 摂氏 degrees Celsius degree C
• 産婦人科領域で「子宮外頚 子宮外頚部 exocervix」を表現するための略語

　 　 　 　

「Cs」

　　[★] セシウム, caesium, cesium 　

「Cd」

　　[★] カドミウム

関

cadmium

　

「c」

　　[★]

• 光速, speed of light