Cathepsin G

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Cathepsin G

PDB rendering based on 1au8.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CTSG ; CATG; CG
External IDs OMIM116830 MGI88563 HomoloGene105646 ChEMBL: 4071 GeneCards: CTSG Gene
EC number 3.4.21.20
RNA expression pattern
PBB GE CTSG 205653 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1511 13035
Ensembl ENSG00000100448 ENSMUSG00000040314
UniProt P08311 P28293
RefSeq (mRNA) NM_001911 NM_007800
RefSeq (protein) NP_001902 NP_031826
Location (UCSC) Chr 14:
25.04 – 25.05 Mb
Chr 14:
56.1 – 56.1 Mb
PubMed search [1] [2]

Cathepsin G (EC 3.4.21.20, chymotrypsin-like proteinase, neutral proteinase) is an enzymatic protein belonging to the peptidase or protease families. In humans, it is coded by the CTSG gene.

The protein encoded by this gene, a member of the peptidase S1 protein family, is found in azurophil granules of neutrophilic polymorphonuclear leukocytes. The encoded protease has a specificity similar to that of chymotrypsin C, and may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation. Transcript variants utilizing alternative polyadenylation signals exist for this gene.[1]

Clinical significance[edit]

An upregulation of cathepsin G was reported in studies of keratoconus.[2]

See also[edit]

References[edit]

  1. ^ "Entrez Gene: CTSG cathepsin G". 
  2. ^ Whitelock RB, Fukuchi T, Zhou L, Twining SS, Sugar J, Feder RS, Yue BY. (1997). "Cathepsin G, acid phosphatase, and alpha 1-proteinase inhibitor messenger RNA levels in keratoconus corneas". Invest Ophthalmol Vis Sci. 38 (2): 529–34. PMID 9040486. 

Further reading[edit]

  • Shafer WM, Katzif S, Bowers S et al. (2002). "Tailoring an antibacterial peptide of human lysosomal cathepsin G to enhance its broad-spectrum action against antibiotic-resistant bacterial pathogens". Curr. Pharm. Des. 8 (9): 695–702. doi:10.2174/1381612023395376. PMID 11945165. 
  • Cohen AB, Stevens MD, Miller EJ et al. (1992). "Generation of the neutrophil-activating peptide-2 by cathepsin G and cathepsin G-treated human platelets". Am. J. Physiol. 263 (2 Pt 1): L249–56. PMID 1387511. 
  • Sasaki T, Ueno-Matsuda E (1993). "Immunocytochemical localization of cathepsins B and G in odontoclasts of human deciduous teeth". J. Dent. Res. 71 (12): 1881–4. doi:10.1177/00220345920710120501. PMID 1452887. 
  • Maison CM, Villiers CL, Colomb MG (1991). "Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G". J. Immunol. 147 (3): 921–6. PMID 1861080. 
  • Brandt E, Van Damme J, Flad HD (1991). "Neutrophils can generate their activator neutrophil-activating peptide 2 by proteolytic cleavage of platelet-derived connective tissue-activating peptide III". Cytokine 3 (4): 311–21. doi:10.1016/1043-4666(91)90499-4. PMID 1873479. 
  • Kargi HA, Campbell EJ, Kuhn C (1990). "Elastase and cathepsin G of human monocytes: heterogeneity and subcellular localization to peroxidase-positive granules". J. Histochem. Cytochem. 38 (8): 1179–86. doi:10.1177/38.8.2164060. PMID 2164060. 
  • Pratt CW, Tobin RB, Church FC (1990). "Interaction of heparin cofactor II with neutrophil elastase and cathepsin G". J. Biol. Chem. 265 (11): 6092–7. PMID 2318847. 
  • Gabay JE, Scott RW, Campanelli D et al. (1989). "Antibiotic proteins of human polymorphonuclear leukocytes". Proc. Natl. Acad. Sci. U.S.A. 86 (14): 5610–4. doi:10.1073/pnas.86.14.5610. PMC 297672. PMID 2501794. 
  • Hohn PA, Popescu NC, Hanson RD et al. (1989). "Genomic organization and chromosomal localization of the human cathepsin G gene". J. Biol. Chem. 264 (23): 13412–9. PMID 2569462. 
  • Livesey SA, Buescher ES, Krannig GL et al. (1990). "Human neutrophil granule heterogeneity: immunolocalization studies using cryofixed, dried and embedded specimens". Scanning Microsc. Suppl. 3: 231–9; discussion 239–40. PMID 2616953. 
  • Campbell EJ, Silverman EK, Campbell MA (1989). "Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity". J. Immunol. 143 (9): 2961–8. PMID 2681419. 
  • Salvesen G, Farley D, Shuman J et al. (1987). "Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases". Biochemistry 26 (8): 2289–93. doi:10.1021/bi00382a032. PMID 3304423. 
  • Heck LW, Rostand KS, Hunter FA, Bhown A (1987). "Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors". Anal. Biochem. 158 (1): 217–27. doi:10.1016/0003-2697(86)90612-3. PMID 3799965. 
  • Crocker J, Jenkins R, Burnett D (1986). "Immunohistochemical localization of cathepsin G in human tissues". Am. J. Surg. Pathol. 9 (5): 338–43. doi:10.1097/00000478-198505000-00003. PMID 3911778. 
  • Klickstein LB, Kaempfer CE, Wintroub BU (1983). "The granulocyte-angiotensin system. Angiotensin I-converting activity of cathepsin G". J. Biol. Chem. 257 (24): 15042–6. PMID 6294088. 
  • LaRosa CA, Rohrer MJ, Benoit SE et al. (1994). "Neutrophil cathepsin G modulates the platelet surface expression of the glycoprotein (GP) Ib-IX complex by proteolysis of the von Willebrand factor binding site on GPIb alpha and by a cytoskeletal-mediated redistribution of the remainder of the complex". Blood 84 (1): 158–68. PMID 7517206. 
  • Owen CA, Campbell MA, Sannes PL et al. (1995). "Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases". J. Cell Biol. 131 (3): 775–89. doi:10.1083/jcb.131.3.775. PMC 2120617. PMID 7593196. 
  • Savage MJ, Iqbal M, Loh T et al. (1994). "Cathepsin G: localization in human cerebral cortex and generation of amyloidogenic fragments from the beta-amyloid precursor protein". Neuroscience 60 (3): 607–19. doi:10.1016/0306-4522(94)90490-1. PMID 7936190. 
  • Grisolano JL, Sclar GM, Ley TJ (1994). "Early myeloid cell-specific expression of the human cathepsin G gene in transgenic mice". Proc. Natl. Acad. Sci. U.S.A. 91 (19): 8989–93. doi:10.1073/pnas.91.19.8989. PMC 44732. PMID 8090757. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 

External links[edit]

  • The MEROPS online database for peptidases and their inhibitors: S01.133

This article incorporates text from the United States National Library of Medicine, which is in the public domain.