CTSD

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Cathepsin D
PDB rendering based on 1lya.
Available structures: 1lya, 1lyb, 1lyw
Identifiers
Symbol(s) CTSD; CLN10; CPSD; MGC2311
External IDs OMIM: 116840 MGI: 88562 HomoloGene: 55616
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 1509 13033
Ensembl ENSG00000117984 ENSMUSG00000007891
Uniprot P07339 Q05BF3
Refseq NM_001909 (mRNA)
NP_001900 (protein)		 NM_009983 (mRNA)
NP_034113 (protein)
Location Chr 11: 1.73 - 1.74 Mb Chr 7: 142.19 - 142.2 Mb
Pubmed search [1] [2]

Cathepsin D, also known as CTSD, is a human gene.[1]

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.[1]

[edit] References

  1. ^ a b Entrez Gene: CTSD cathepsin D.

[edit] 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
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v • d • e
Hydrolase: proteases (EC 3.4)
Exopeptidase 3.4.11-19
Endopeptidase 3.4.21-24
Cathepsin 3.4.18,21,22,23
A - B - C - D - E - F - G - H - K - L1/L2 - S - W - Z