CTSD

Cathepsin D, also known as CTSD, is a human gene.cite web | title = Entrez Gene: CTSD cathepsin D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1509| accessdate = ]

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: CTSD cathepsin D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1509| accessdate = ]

References

Further reading

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

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