CTSD

Cathepsin D
PDB rendering based on 1lya.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1lya​, 1lyb​, 1lyw​
Identifiers
Symbols	CTSD ; CLN10; CPSD; MGC2311
External IDs	Template:OMIM5 Template:MGI HomoloGene: 55616
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO 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 D, also known as CTSD, is a human gene.

This gene encodes a lysosomal aspartyl protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. This proteinase, which is a member of the peptidase C1 family, has a specificity similar to but narrower than that of pepsin A. Transcription of this gene is initiated from several sites, including one which 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.

Further reading

• Chao J, Miao RQ, Chen V; et al. (2001). "Novel roles of kallistatin, a specific tissue kallikrein inhibitor, in vascular remodeling". Biol. Chem. 382 (1): 15–21. PMID 11258665.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Leto G, Tumminello FM, Crescimanno M; et al. (2004). "Cathepsin D expression levels in nongynecological solid tumors: clinical and therapeutic implications". Clin. Exp. Metastasis. 21 (2): 91–106. PMID 15168727.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Liaudet-Coopman E, Beaujouin M, Derocq D; et al. (2006). "Cathepsin D: newly discovered functions of a long-standing aspartic protease in cancer and apoptosis". Cancer Lett. 237 (2): 167–79. doi:10.1016/j.canlet.2005.06.007. PMID 16046058.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Knight CG, Barrett AJ (1976). "Interaction of human cathepsin D with the inhibitor pepstatin". Biochem. J. 155 (1): 117–25. PMID 938470.
• Gulnik S, Baldwin ET, Tarasova N, Erickson J (1992). "Human liver cathepsin D. Purification, crystallization and preliminary X-ray diffraction analysis of a lysosomal enzyme". J. Mol. Biol. 227 (1): 265–70. PMID 1522590.CS1 maint: Multiple names: authors list (link)
• Conner GE, Richo G (1992). "Isolation and characterization of a stable activation intermediate of the lysosomal aspartyl protease cathepsin D.". Biochemistry. 31 (4): 1142–7. PMID 1734961.
• Fujita H, Tanaka Y, Noguchi Y; et al. (1991). "Isolation and sequencing of a cDNA clone encoding rat liver lysosomal cathepsin D and the structure of three forms of mature enzymes". Biochem. Biophys. Res. Commun. 179 (1): 190–6. PMID 1883350.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Dunn AD, Crutchfield HE, Dunn JT (1991). "Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by cathepsins B, D, and L.". J. Biol. Chem. 266 (30): 20198–204. PMID 1939080.CS1 maint: Multiple names: authors list (link)
• Lenarcic B, Krasovec M, Ritonja A; et al. (1991). "Inactivation of human cystatin C and kininogen by human cathepsin D.". FEBS Lett. 280 (2): 211–5. PMID 2013314.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Redecker B, Heckendorf B, Grosch HW; et al. (1991). "Molecular organization of the human cathepsin D gene". DNA Cell Biol. 10 (6): 423–31. PMID 2069717.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Conner GE, Udey JA (1990). "Expression and refolding of recombinant human fibroblast procathepsin D.". DNA Cell Biol. 9 (1): 1–9. PMID 2180427.
• Capony F, Rougeot C, Montcourrier P; et al. (1989). "Increased secretion, altered processing, and glycosylation of pro-cathepsin D in human mammary cancer cells". Cancer Res. 49 (14): 3904–9. PMID 2736531.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lenarcic B, Kos J, Dolenc I; et al. (1988). "Cathepsin D inactivates cysteine proteinase inhibitors, cystatins". Biochem. Biophys. Res. Commun. 154 (2): 765–72. PMID 3261170.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Westley BR, May FE (1987). "Oestrogen regulates cathepsin D mRNA levels in oestrogen responsive human breast cancer cells". Nucleic Acids Res. 15 (9): 3773–86. PMID 3588310.
• Terayama H, Fukuzumi R (1987). "Ubiquitous presence of calciferin-like and cathepsin D-like activities in the sera (vertebrates) and humoral fluids (invertebrates)". Comp. Biochem. Physiol., B. 87 (4): 675–9. PMID 3665421.
• Faust PL, Kornfeld S, Chirgwin JM (1985). "Cloning and sequence analysis of cDNA for human cathepsin D.". Proc. Natl. Acad. Sci. U.S.A. 82 (15): 4910–4. PMID 3927292.CS1 maint: Multiple names: authors list (link)
• Sekiguchi K, Siri A, Zardi L, Hakomori S (1985). "Differences in domain structure between human fibronectins isolated from plasma and from culture supernatants of normal and transformed fibroblasts. Studies with domain-specific antibodies". J. Biol. Chem. 260 (8): 5105–14. PMID 3988746.CS1 maint: Multiple names: authors list (link)
• Lemansky P, Gieselmann V, Hasilik A, von Figura K (1984). "Cathepsin D and beta-hexosaminidase synthesized in the presence of 1-deoxynojirimycin accumulate in the endoplasmic reticulum". J. Biol. Chem. 259 (16): 10129–35. PMID 6236213.CS1 maint: Multiple names: authors list (link)
• Dreyer RN, Bausch KM, Fracasso P; et al. (1994). "Processing of the pre-beta-amyloid protein by cathepsin D is enhanced by a familial Alzheimer's disease mutation". Eur. J. Biochem. 224 (2): 265–71. PMID 7523115.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Atkins KB, Troen BR (1995). "Regulation of cathepsin D gene expression in HL-60 cells by retinoic acid and calcitriol". Cell Growth Differ. 6 (7): 871–7. PMID 7547509.