• regulation of protein stability • glycosphingolipid metabolic process • proteolysis • regulation of chaperone-mediated autophagy • proteolysis involved in cellular protein catabolic process • intracellular protein transport • positive regulation of catalytic activity • neutrophil degranulation • negative regulation of chaperone-mediated autophagy
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
5476
19025
Ensembl
ENSG00000064601
ENSMUSG00000017760
UniProt
P10619
P16675
RefSeq (mRNA)
NM_001167594 NM_000308 NM_001127695
NM_001038492 NM_008906
RefSeq (protein)
NP_000299 NP_001121167 NP_001161066
NP_001033581 NP_032932
Location (UCSC)
Chr 20: 45.89 – 45.9 Mb
Chr 2: 164.83 – 164.84 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Cathepsin A is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA gene.[5]
Contents
1Function
2Clinical significance
3Interactions
4References
5Further reading
6External links
Function
This gene encodes a glycoprotein that associates with lysosomal enzymes beta-galactosidase and neuraminidase to form a complex of high-molecular-weight multimers. The formation of this complex provides a protective role for stability and activity. It is protective for β-galactosidase and neuraminidase.[6]
Clinical significance
Deficiencies in this gene are linked to multiple forms of galactosialidosis.[5]
Interactions
Cathepsin A has been shown to interact with NEU1.[7]
References
^ abcGRCh38: Ensembl release 89: ENSG00000064601 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000017760 - Ensembl, May 2017
^"Human PubMed Reference:".
^"Mouse PubMed Reference:".
^ ab"Entrez Gene: CTSA cathepsin A".
^Mitchell, Richard Sheppard; Kumar, Vinay; Robbins, Stanley L.; Abbas, Abul K.; Fausto, Nelson (2007). "Table 7-6". Robbins basic pathology (8th ed.). Saunders/Elsevier. ISBN 1-4160-2973-7.
^van der Spoel, A; Bonten E; d'Azzo A (Mar 1998). "Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A". EMBO J. ENGLAND. 17 (6): 1588–97. doi:10.1093/emboj/17.6.1588. ISSN 0261-4189. PMC 1170506. PMID 9501080.
Further reading
Morreau H, Galjart NJ, Willemsen R, et al. (1992). "Human lysosomal protective protein. Glycosylation, intracellular transport, and association with beta-galactosidase in the endoplasmic reticulum". J. Biol. Chem. 267 (25): 17949–56. PMID 1387645.
Halal F, Chitayat D, Parikh H, et al. (1992). "Ring chromosome 20 and possible assignment of the structural gene encoding human carboxypeptidase-L to the distal segment of the long arm of chromosome 20". Am. J. Med. Genet. 43 (3): 576–9. doi:10.1002/ajmg.1320430314. PMID 1605251.
Jackman HL, Tan FL, Tamei H, et al. (1990). "A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal "protective protein"". J. Biol. Chem. 265 (19): 11265–72. PMID 1694176.
Zhou XY, Galjart NJ, Willemsen R, et al. (1992). "A mutation in a mild form of galactosialidosis impairs dimerization of the protective protein and renders it unstable". EMBO J. 10 (13): 4041–8. PMC 453152. PMID 1756715.
Galjart NJ, Morreau H, Willemsen R, et al. (1991). "Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function". J. Biol. Chem. 266 (22): 14754–62. PMID 1907282.
Yoshida K, Oshima A, Shimmoto M, et al. (1991). "Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common mutation among Japanese adult/chronic cases". Am. J. Hum. Genet. 49 (2): 435–42. PMC 1683306. PMID 1907800.
Wiegant J, Galjart NJ, Raap AK, d'Azzo A (1991). "The gene encoding human protective protein (PPGB) is on chromosome 20". Genomics. 10 (2): 345–9. doi:10.1016/0888-7543(91)90318-9. PMID 2071143.
Strisciuglio P, Sly WS, Dodson WE, et al. (1991). "Combined deficiency of beta-galactosidase and neuraminidase: natural history of the disease in the first 18 years of an American patient with late infantile onset form". Am. J. Med. Genet. 37 (4): 573–7. doi:10.1002/ajmg.1320370431. PMID 2148053.
Kase R, Itoh K, Takiyama N, et al. (1990). "Galactosialidosis: simultaneous deficiency of esterase, carboxy-terminal deamidase and acid carboxypeptidase activities". Biochem. Biophys. Res. Commun. 172 (3): 1175–9. doi:10.1016/0006-291X(90)91572-A. PMID 2244901.
Willemsen R, Hoogeveen AT, Sips HJ, et al. (1986). "Immunoelectron microscopical localization of lysosomal beta-galactosidase and its precursor forms in normal and mutant human fibroblasts". Eur. J. Cell Biol. 40 (1): 9–15. PMID 3084261.
Verheijen FW, Palmeri S, Galjaard H (1987). "Purification and partial characterization of lysosomal neuraminidase from human placenta". Eur. J. Biochem. 162 (1): 63–7. doi:10.1111/j.1432-1033.1987.tb10542.x. PMID 3102233.
Nanba E, Tsuji A, Omura K, Suzuki Y (1987). "Galactosialidosis: a direct evidence that a 46-kilodalton protein restores deficient enzyme activities in fibroblasts". Biochem. Biophys. Res. Commun. 144 (1): 138–42. doi:10.1016/S0006-291X(87)80486-2. PMID 3107551.
Galjart NJ, Gillemans N, Harris A, et al. (1988). "Expression of cDNA encoding the human "protective protein" associated with lysosomal beta-galactosidase and neuraminidase: homology to yeast proteases". Cell. 54 (6): 755–64. doi:10.1016/S0092-8674(88)90999-3. PMID 3136930.
Chitayat D, Applegarth DA, Lewis J, et al. (1989). "Juvenile galactosialidosis in a white male: a new variant". Am. J. Med. Genet. 31 (4): 887–901. doi:10.1002/ajmg.1320310423. PMID 3149149.
Verheijen FW, Palmeri S, Hoogeveen AT, Galjaard H (1985). "Human placental neuraminidase. Activation, stabilization and association with beta-galactosidase and its protective protein". Eur. J. Biochem. 149 (2): 315–21. doi:10.1111/j.1432-1033.1985.tb08928.x. PMID 3922758.
van der Horst GT, Kleijer WJ, Hoogeveen AT, et al. (1984). "Morquio B syndrome: a primary defect in beta-galactosidase". Am. J. Med. Genet. 16 (2): 261–75. doi:10.1002/ajmg.1320160215. PMID 6418007.
Maire I, Nivelon-Chevallier AR (1982). "Combined deficiency of beta-galactosidase and neuraminidase: three affected siblings in a French family". J. Inherit. Metab. Dis. 4 (4): 221–3. doi:10.1007/BF02263656. PMID 6796775.
Pshezhetsky AV, Potier M (1994). "Direct affinity purification and supramolecular organization of human lysosomal cathepsin A.". Arch. Biochem. Biophys. 313 (1): 64–70. doi:10.1006/abbi.1994.1359. PMID 8053688.
Ishii N, Oshima A, Sakuraba H, et al. (1994). "Normal serum beta-galactosidase in juvenile GM1 gangliosidosis". Pediatr. Neurol. 10 (4): 317–9. doi:10.1016/0887-8994(94)90129-5. PMID 8068159.
Chakraborty S, Rafi MA, Wenger DA (1994). "Mutations in the lysosomal beta-galactosidase gene that cause the adult form of GM1 gangliosidosis". Am. J. Hum. Genet. 54 (6): 1004–13. PMC 1918177. PMID 8198123.
External links
Cathepsin+A at the US National Library of Medicine Medical Subject Headings (MeSH)
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PDB gallery
1ivy: PHYSIOLOGICAL DIMER HPP PRECURSOR
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Hydrolase: proteases (EC 3.4)
3.4.11-19: Exopeptidase
3.4.11
Aminopeptidase
Alanine
Arginyl
Aspartyl
Cystinyl
Leucyl
Glutamyl
Methionyl
1
2
O
3.4.13
Dipeptidase
1
2
3
3.4.14
Dipeptidyl peptidase
Cathepsin C
Dipeptidyl peptidase-4
Tripeptidyl peptidase
Tripeptidyl peptidase I
Tripeptidyl peptidase II
3.4.15
Angiotensin-converting enzyme
3.4.16
Serine type carboxypeptidases: Cathepsin A
DD-transpeptidase
3.4.17
Metalloexopeptidases
Carboxypeptidase
A
A2
B
C
E
Glutamate II
Other/ungrouped
Metalloexopeptidase
3.4.21-25: Endopeptidase
Serine protease
Cysteine protease
Aspartic acid protease
Metalloendopeptidase
Threonine endopeptidase
Proteasome endopeptidase complex
HslU—HslV peptidase
Other/ungrouped: Amyloid precursor protein secretase
Alpha secretase
Beta-secretase 1
Beta-secretase 2
Gamma secretase
3.4.99: Unknown
Staphylokinase
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Enzymes
Activity
Active site
Binding site
Catalytic triad
Oxyanion hole
Enzyme promiscuity
Catalytically perfect enzyme
Coenzyme
Cofactor
Enzyme catalysis
Regulation
Allosteric regulation
Cooperativity
Enzyme inhibitor
Enzyme activator
Classification
EC number
Enzyme superfamily
Enzyme family
List of enzymes
Kinetics
Enzyme kinetics
Eadie–Hofstee diagram
Hanes–Woolf plot
Lineweaver–Burk plot
Michaelis–Menten kinetics
Types
EC1 Oxidoreductases (list)
EC2 Transferases (list)
EC3 Hydrolases (list)
EC4 Lyases (list)
EC5 Isomerases (list)
EC6 Ligases (list)
Molecular and Cellular Biology portal
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Neuraminidase 1-mediated desialylation of the mucin 1 ectodomain releases a decoy receptor that protects against Pseudomonas aeruginosa lung infection.