Cathepsin H is aprotein that in humans is encoded by theCTSHgene.[5][6]
The protein encoded by this gene is acysteine cathepsin, alysosomalcysteine protease important in the overall degradation of lysosomal proteins. It is composed of a dimer ofdisulfide-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 anaminopeptidase and as anendopeptidase. Increased expression of this gene has been correlated with malignant progression ofprostate tumors. Two transcript variants encoding differentisoforms have been found for this gene.[6]
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^Fuchs R, Machleidt W, Gassen HG (Feb 1989). "Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H".Biol Chem Hoppe-Seyler.369 (6):469–75.doi:10.1515/bchm3.1988.369.1.469.PMID2849458.
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.doi:10.1016/0167-4838(82)90222-9.PMID6184075.
Söderström M, Salminen H, Glumoff V, et al. (1999). "Cathepsin expression during skeletal development".Biochim. Biophys. Acta.1446 (1–2):35–46.doi:10.1016/S0167-4781(99)00068-8.PMID10395917.
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.doi:10.1007/s002230001152.PMID11136537.S2CID31004810.
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.doi:10.1165/ajrcmb.26.6.4744.PMID12034564.
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.doi:10.1016/S0022-2836(02)01432-8.PMID12581647.
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.doi:10.1016/S0009-8981(03)00023-8.PMID12589965.
1nb3: 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
1nb5: Crystal structure of stefin A in complex with cathepsin H
8pch: CRYSTAL STRUCTURE OF PORCINE CATHEPSIN H DETERMINED AT 2.1 ANGSTROM RESOLUTION: LOCATION OF THE MINI-CHAIN C-TERMINAL CARBOXYL GROUP DEFINES CATHEPSIN H AMINOPEPTIDASE FUNCTION
