CTSH (gene)

Cathepsin H

PDB rendering based on 1nb3.

| Available structures

PDB |  Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
| List of PDB id codes

1nb3​, 1nb5​, 8pch​

Identifiers
Symbols|  CTSH ; CPSB; ACC-4; ACC-5; DKFZp686B24257; MGC1519; minichain
External IDs|  Template:OMIM5 Template:MGI HomoloGene: 36159
| Gene ontology

Molecular function | Template:GNF GO Template:GNF GO
Cellular component | Template:GNF GO
Biological process | Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species|  Human|  Mouse
Entrez|  n/a|  n/a
Ensembl|  n/a|  n/a
UniProt|  n/a|  n/a
RefSeq (mRNA)|  n/a|  n/a
RefSeq (protein)|  n/a|  n/a
Location (UCSC)|  n/a|  n/a
PubMed search|  n/a|  n/a

Cathepsin H, also known as CTSH, is a human gene.[1]

The protein encoded by this gene is a lysosomal cysteine proteinase 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.[1]

## References[edit | edit source]

1. ↑ 1.0 1.1 "Entrez Gene: CTSH cathepsin H".

## Further reading[edit | edit source]

* Sawicki G, Warwas M (1990). "Cathepsin H from human placenta". Acta Biochim. Pol. 36 (3–4): 343–51. PMID 2486008.
* Fuchs R, Gassen HG (1990). "Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase". Nucleic Acids Res. 17 (22): 9471. PMID 2587265.
* Chernaia VI, Reva AD (1990). "[Cathepsin H activity in the human brain and human brain neoplasms]". Ukr. Biokhim. Zh. 61 (5): 47–50. PMID 2588347.
* Fuchs R, Machleidt W, Gassen HG (1989). "Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H.". Biol. Chem. Hoppe-Seyler. 369 (6): 469–75. PMID 2849458.CS1 maint: Multiple names: authors list (link)
* Ritonja A, Popović T, Kotnik M; et al. (1988). "Amino acid sequences of the human kidney cathepsins H and L.". FEBS Lett. 228 (2): 341–5. PMID 3342889.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Järvinen M, Rinne A (1983). "Human spleen cysteineproteinase inhibitor. Purification, fractionation into isoelectric variants and some properties of the variants". Biochim. Biophys. Acta. 708 (2): 210–7. PMID 6184075.
* Kato S, Sekine S, Oh SW; et al. (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. PMID 7821789.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Baumgrass R, Williamson MK, Price PA (1997). "Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S.". J. Bone Miner. Res. 12 (3): 447–55. PMID 9076588.CS1 maint: Multiple names: authors list (link)
* Söderström M, Salminen H, Glumoff V; et al. (1999). "Cathepsin expression during skeletal development". Biochim. Biophys. Acta. 1446 (1–2): 35–46. PMID 10395917.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Jokimaa V, Oksjoki S, Kujari H; et al. (2001). "Expression patterns of cathepsins B, H, K, L and S in the human endometrium". Mol. Hum. Reprod. 7 (1): 73–8. PMID 11134363.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Uusitalo H, Hiltunen A, Söderström M; et al. (2001). "Expression of cathepsins B, H, K, L, and S and matrix metalloproteinases 9 and 13 during chondrocyte hypertrophy and endochondral ossification in mouse fracture callus". Calcif. Tissue Int. 67 (5): 382–90. PMID 11136537.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Pol E, Björk I (2001). "Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases". Protein Sci. 10 (9): 1729–38. PMID 11514663.
* Waghray A, Keppler D, Sloane BF; et al. (2002). "Analysis of a truncated form of cathepsin H in human prostate tumor cells". J. Biol. Chem. 277 (13): 11533–8. doi:10.1074/jbc.M109557200. PMID 11796715.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Brasch F, Ten Brinke A, Johnen G; et al. (2002). "Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes". Am. J. Respir. Cell Mol. Biol. 26 (6): 659–70. PMID 12034564.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Bühling F, Waldburg N, Krüger S; et al. (2003). "Expression of cathepsins B, H, K, L, and S during human fetal lung development". Dev. Dyn. 225 (1): 14–21. doi:10.1002/dvdy.10134. PMID 12203716.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Jenko S, Dolenc I, Guncar G; et al. (2003). "Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases". J. Mol. Biol. 326 (3): 875–85. PMID 12581647.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Nagai A, Terashima M, Harada T; et al. (2003). "Cathepsin B and H activities and cystatin C concentrations in cerebrospinal fluid from patients with leptomeningeal metastasis". Clin. Chim. Acta. 329 (1–2): 53–60. PMID 12589965.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Han SR, Momeni A, Strach K; et al. (2004). "Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis". Arterioscler. Thromb. Vasc. Biol. 23 (4): 661–7. doi:10.1161/01.ATV.0000063614.21233.BF. PMID 12615673.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
* Dodt J, Reichwein J (2004). "Human cathepsin H: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase". Biol. Chem. 384 (9): 1327–32. PMID 14515996.

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