CTSH (gene)

Cathepsin H, also known as CTSH, is a human gene.cite web | title = Entrez Gene: CTSH cathepsin H| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1512| accessdate = ]

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: CTSH cathepsin H| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1512| accessdate = ]

References

Further reading

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

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