User:JonSDSUGrad/Sandbox/Demo 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

Gene ontology
Molecular Function:	• cathepsin D activity • pepsin A activity • peptidase activity
Cellular Component:	• extracellular region • mitochondrion • lysosome
Biological Process:	• proteolysis

RNA expression pattern

Image:PBB GE CTSD 239 at tn.png

More reference expression data

Orthologs

Human

Mouse

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

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

[edit] Further reading

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.
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.
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.
Whiteman HJ, Weeks ME, Dowen SE, et al. (2007). "The role of S100P in the invasion of pancreatic cancer cells is mediated through cytoskeletal changes and regulation of cathepsin D.". Cancer Res. 67 (18): 8633-42. doi:10.1158/0008-5472.CAN-07-0545. PMID 17875703.
Vashishta A, Saraswat Ohri S, Vetvickova J, et al. (2007). "Procathepsin D secreted by HaCaT keratinocyte cells - A novel regulator of keratinocyte growth.". Eur. J. Cell Biol. 86 (6): 303-13. doi:10.1016/j.ejcb.2007.03.008. PMID 17532541.
Castino R, Bellio N, Nicotra G, et al. (2007). "Cathepsin D-Bax death pathway in oxidative stressed neuroblastoma cells.". Free Radic. Biol. Med. 42 (9): 1305-16. doi:10.1016/j.freeradbiomed.2006.12.030. PMID 17395004.
Hilfiker-Kleiner D, Kaminski K, Podewski E, et al. (2007). "A cathepsin D-cleaved 16 kDa form of prolactin mediates postpartum cardiomyopathy.". Cell 128 (3): 589-600. doi:10.1016/j.cell.2006.12.036. PMID 17289576.
Lou X, Xiao T, Zhao K, et al. (2007). "Cathepsin D is secreted from M-BE cells: its potential role as a biomarker of lung cancer.". J. Proteome Res. 6 (3): 1083-92. doi:10.1021/pr060422t. PMID 17284061.
Follo C, Castino R, Nicotra G, et al. (2007). "Folding, activity and targeting of mutated human cathepsin D that cannot be processed into the double-chain form.". Int. J. Biochem. Cell Biol. 39 (3): 638-49. doi:10.1016/j.biocel.2006.11.010. PMID 17188016.
Mása M, Maresová L, Vondrásek J, et al. (2008). "Cathepsin D propeptide: mechanism and regulation of its interaction with the catalytic core.". Biochemistry 45 (51): 15474-82. doi:10.1021/bi0614986. PMID 17176069.
Sakamoto T, Saito H, Ishii K, et al. (2007). "Aluminum inhibits proteolytic degradation of amyloid beta peptide by cathepsin D: a potential link between aluminum accumulation and neuritic plaque deposition.". FEBS Lett. 580 (28-29): 6543-9. doi:10.1016/j.febslet.2006.10.075. PMID 17112520.
Chi A, Valencia JC, Hu ZZ, et al. (2007). "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.". J. Proteome Res. 5 (11): 3135-44. doi:10.1021/pr060363j. PMID 17081065.
Haidar B, Kiss RS, Sarov-Blat L, et al. (2007). "Cathepsin D, a lysosomal protease, regulates ABCA1-mediated lipid efflux.". J. Biol. Chem. 281 (52): 39971-81. doi:10.1074/jbc.M605095200. PMID 17032648.
Wang Z, Liang R, Huang GS, et al. (2006). "Glucosamine sulfate-induced apoptosis in chronic myelogenous leukemia K562 cells is associated with translocation of cathepsin D and downregulation of Bcl-xL.". Apoptosis 11 (10): 1851-60. doi:10.1007/s10495-006-9529-6. PMID 16850161.
Mariani E, Seripa D, Ingegni T, et al. (2006). "Interaction of CTSD and A2M polymorphisms in the risk for Alzheimer's disease.". J. Neurol. Sci. 247 (2): 187-91. doi:10.1016/j.jns.2006.05.043. PMID 16784755.
Hasan L, Mazzucchelli L, Liebi M, et al. (2006). "Function of liver activation-regulated chemokine/CC chemokine ligand 20 is differently affected by cathepsin B and cathepsin D processing.". J. Immunol. 176 (11): 6512-22. PMID 16709808.
Steinfeld R, Reinhardt K, Schreiber K, et al. (2006). "Cathepsin D deficiency is associated with a human neurodegenerative disorder.". Am. J. Hum. Genet. 78 (6): 988-98. doi:10.1086/504159. PMID 16685649.
Riemenschneider M, Blennow K, Wagenpfeil S, et al. (2006). "The cathepsin D rs17571 polymorphism: effects on CSF tau concentrations in Alzheimer disease.". Hum. Mutat. 27 (6): 532-7. doi:10.1002/humu.20326. PMID 16652347.
Corder EH, Huang R, Cathcart HM, et al. (2006). "Membership in genetic groups predicts Alzheimer disease.". Rejuvenation Res 9 (1): 89-93. doi:10.1089/rej.2006.9.89. PMID 16608402.
Davidson Y, Gibbons L, Pritchard A, et al. (2006). "Genetic associations between cathepsin D exon 2 C-->T polymorphism and Alzheimer's disease, and pathological correlations with genotype.". J. Neurol. Neurosurg. Psychiatr. 77 (4): 515-7. doi:10.1136/jnnp.2005.063917. PMID 16543533.