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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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CTSD

Introduction

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]

References

References

  1. ↑ 1.0 1.1 “Entrez Gene: CTSD cathepsin D”.
Further reading

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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