The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Ctsa  -  cathepsin A

Mus musculus

Synonyms: AU019505, Carboxypeptidase C, Carboxypeptidase L, Cathepsin A, Lysosomal protective protein, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Ctsa


High impact information on Ctsa

  • The lysosomal storage disorder galactosialidosis results from a primary deficiency of the protective protein/cathepsin A (PPCA), which in turn affects the activities of beta-galactosidase and neuraminidase [3].
  • Mice homozygous for a null mutation at the PPCA locus present with signs of the disease shortly after birth and develop a phenotype closely resembling human patients with galactosialidosis [3].
  • To rescue the disease phenotype, GS mice were transplanted with bone marrow from transgenic mice overexpressing human PPCA specifically in monocytes/macrophages under the control of the colony stimulating factor-1 receptor promoter [1].
  • PPCA-expressing perivascular and leptomeningeal macrophages were detected throughout the brain of recipient mice, although some neuronal cells, such as Purkinje cells, continued to show storage and died [1].
  • Here, we established stable donor hematopoiesis in PPCA(-/-) mice that received hematopoietic progenitors transduced with a murine stem cell virus (MSCV)-based, bicistronic retroviral vector overexpressing PPCA and the green fluorescent protein (GFP) marker [4].

Chemical compound and disease context of Ctsa

  • Other proteasome-specific inhibitors, e.g. epoxomicin and N-benzyloxycarbonyl-Ile-Glu(O-tert-Bu)-Ala-leucinal (PSI) at a concentration of 1 microM did not affect cathepsin A activity in melanoma cell line lysates [2].

Biological context of Ctsa

  • Loci mapping between the T2Wa and T28H breakpoints lie in a region that is subject to parental imprinting, and so expression of Ppgb was tested in mice with maternal duplication/paternal deficiency and its reciprocal for the distal region of Chr 2 [5].
  • Protective protein for beta-galactosidase, Ppgb, maps to the distal imprinting region of mouse chromosome 2 but is not imprinted [5].
  • To study the site and level of expression of PPCA mRNA in murine and human tissues, we analyzed the promoter regions of the corresponding genes [6].
  • Molecular cloning and gene expression studies have disclosed that protective protein is cathepsin A [7].

Anatomical context of Ctsa


Associations of Ctsa with chemical compounds

  • Cathepsin A/protective protein [], carboxypeptidase A, is a lysosomal serine protease with structural homology to yeast (Saccharomyces cerevisiae) carboxypeptidase Y [7].
  • These results suggest that spinal 5-HT receptors and alpha2-adrenoceptors are involved in the antinociception induced by MPCA and PPCA, but not in that elicited by dipyrone [11].
  • Intrathecal (i.t.) administration of methysergide (3 and 10 microg) and yohimbine (3 microg), but not of prazosin (0.3 and 1 microg) prevented the antinociceptive action of MPCA and PPCA (500 micromol/kg, s.c.). Dipyrone-induced antinociception (500 micromol/kg, s.c.) was not affected by methysergide or adrenoceptor antagonists [11].
  • Since cathepsin A is also a tumor-associated enzyme, further research is needed to clarify its role and the significance of its inhibition by lactacystin in tumor biology [2].
  • Cathepsin A activity was strongly inhibited by Ag+, Hg2+, diisopropylfluorophosphate and p-chloromercuriphenylsulphonic acid [12].

Physical interactions of Ctsa


Other interactions of Ctsa

  • The pathologic manifestations in patients relate primarily to the severe deficiency of neuraminidase, and the physiological significance of cathepsin A activity remains unclear [6].
  • Several lines of evidence indicate that cathepsin A is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities [7].

Analytical, diagnostic and therapeutic context of Ctsa

  • We have shown by reverse transcription-polymerase chain reaction (RT-PCR) that both parental alleles of Ppgb were expressed in the brain and kidney of 17.5-day-old embryos, 18.5-day-old embryos, and newborn mice [5].


  1. Correction of murine galactosialidosis by bone marrow-derived macrophages overexpressing human protective protein/cathepsin A under control of the colony-stimulating factor-1 receptor promoter. Hahn, C.N., del Pilar Martin, M., Zhou, X.Y., Mann, L.W., d'Azzo, A. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  2. Lactacystin inhibits cathepsin A activity in melanoma cell lines. Kozlowski, L., Stoklosa, T., Omura, S., Wójcik, C., Wojtukiewicz, M.Z., Worowski, K., Ostrowska, H. Tumour Biol. (2001) [Pubmed]
  3. Mouse model for the lysosomal disorder galactosialidosis and correction of the phenotype with overexpressing erythroid precursor cells. Zhou, X.Y., Morreau, H., Rottier, R., Davis, D., Bonten, E., Gillemans, N., Wenger, D., Grosveld, F.G., Doherty, P., Suzuki, K. Genes Dev. (1995) [Pubmed]
  4. Functional amelioration of murine galactosialidosis by genetically modified bone marrow hematopoietic progenitor cells. Leimig, T., Mann, L., Martin, M.d.e.l. .P., Bonten, E., Persons, D., Knowles, J., Allay, J.A., Cunningham, J., Nienhuis, A.W., Smeyne, R., d'Azzo, A. Blood (2002) [Pubmed]
  5. Protective protein for beta-galactosidase, Ppgb, maps to the distal imprinting region of mouse chromosome 2 but is not imprinted. Williamson, C.M., Dutton, E.R., Beechey, C.V., Peters, J. Genomics (1994) [Pubmed]
  6. Identification of the promoters for the human and murine protective protein/cathepsin A genes. Rottier, R.J., D'Azzo, A. DNA Cell Biol. (1997) [Pubmed]
  7. Cathepsin A/protective protein: an unusual lysosomal multifunctional protein. Hiraiwa, M. Cell. Mol. Life Sci. (1999) [Pubmed]
  8. A point mutation in the neu-1 locus causes the neuraminidase defect in the SM/J mouse. Rottier, R.J., Bonten, E., d'Azzo, A. Hum. Mol. Genet. (1998) [Pubmed]
  9. Increase in macrophages in the testis of cathepsin a deficient mice suggests an important role for these cells in the interstitial space of this tissue. Korah, N., Smith, C.E., D'Azzo, A., El-Alfy, M., Hermo, L. Mol. Reprod. Dev. (2003) [Pubmed]
  10. Characterization of cell- and region-specific abnormalities in the epididymis of cathepsin A deficient mice. Korah, N., Smith, C.E., D'Azzo, A., Mui, J., Hermo, L. Mol. Reprod. Dev. (2003) [Pubmed]
  11. Alpha 2-adrenoceptors and 5-HT receptors mediate the antinociceptive effect of new pyrazolines, but not of dipyrone. Godoy, M.C., Fighera, M.R., Souza, F.R., Flores, A.E., Rubin, M.A., Oliveira, M.R., Zanatta, N., Martins, M.A., Bonacorso, H.G., Mello, C.F. Eur. J. Pharmacol. (2004) [Pubmed]
  12. High-performance liquid chromatographic-fluorimetric assay for cathepsin A (lysosomal protective protein) activity. Chikuma, T., Ogura, Y., Kasamatsu, M., Taguchi, K., Mitsui, K., Kato, T., Tanaka, A. J. Chromatogr. B Biomed. Sci. Appl. (1999) [Pubmed]
  13. Lack of PPCA expression only partially coincides with lysosomal storage in galactosialidosis mice: indirect evidence for spatial requirement of the catalytic rather than the protective function of PPCA. Rottier, R.J., Hahn, C.N., Mann, L.W., del Pilar Martin, M., Smeyne, R.J., Suzuki, K., d'Azzo, A. Hum. Mol. Genet. (1998) [Pubmed]
WikiGenes - Universities