Cathepsin G

Cathepsin G

Cathepsin G
PDB rendering based on 1au8.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; CATG; CG
External IDs ChEMBL: GeneCards:
EC number
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Cathepsin G (EC, 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, but it is most closely related to other immune serine proteases, such as neutrophil elastase and the granzymes.[1] Cathepsin G may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation. It also localizes to Neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases.[1] Transcript variants utilizing alternative polyadenylation signals exist for this gene.[2]


  • Clinical significance 1
  • See also 2
  • References 3
  • Further reading 4
  • External links 5

Clinical significance

An upregulation of cathepsin G was reported in studies of keratoconus.[3]

See also


  1. ^ a b Thomas MP, Whangbo J, McCrossan G, Deutsch AJ, Martinod K, Walch M, Lieberman J (June 2014). "Leukocyte protease binding to nucleic acids promotes nuclear localization and cleavage of nucleic acid binding proteins". J. Immunol. 192 (11): 5390–7.  
  2. ^ "Entrez Gene: CTSG cathepsin G". 
  3. ^ 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.  

Further reading

  • Shafer WM, Katzif S, Bowers S, Fallon M, Hubalek M, Reed MS, Veprek P, Pohl J (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.  
  • Cohen AB, Stevens MD, Miller EJ, Atkinson MA, Mullenbach G (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.  
  • Sasaki T, Ueno-Matsuda E (1992). "Immunocytochemical localization of cathepsins B and G in odontoclasts of human deciduous teeth". J. Dent. Res. 71 (12): 1881–4.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • Gabay JE, Scott RW, Campanelli D, Griffith J, Wilde C, Marra MN, Seeger M, Nathan CF (1989). "Antibiotic proteins of human polymorphonuclear leukocytes". Proc. Natl. Acad. Sci. U.S.A. 86 (14): 5610–4.  
  • Hohn PA, Popescu NC, Hanson RD, Salvesen G, Ley TJ (1989). "Genomic organization and chromosomal localization of the human cathepsin G gene". J. Biol. Chem. 264 (23): 13412–9.  
  • Livesey SA, Buescher ES, Krannig GL, Harrison DS, Linner JG, Chiovetti R (1989). "Human neutrophil granule heterogeneity: immunolocalization studies using cryofixed, dried and embedded specimens". Scanning Microsc. Suppl. 3: 231–9; discussion 239–40.  
  • 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.  
  • Salvesen G, Farley D, Shuman J, Przybyla A, Reilly C, Travis J (1987). "Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases". Biochemistry 26 (8): 2289–93.  
  • Heck LW, Rostand KS, Hunter FA, Bhown A (1986). "Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors". Anal. Biochem. 158 (1): 217–27.  
  • Crocker J, Jenkins R, Burnett D (1985). "Immunohistochemical localization of cathepsin G in human tissues". Am. J. Surg. Pathol. 9 (5): 338–43.  
  • Klickstein LB, Kaempfer CE, Wintroub BU (1982). "The granulocyte-angiotensin system. Angiotensin I-converting activity of cathepsin G". J. Biol. Chem. 257 (24): 15042–6.  
  • LaRosa CA, Rohrer MJ, Benoit SE, Barnard MR, Michelson AD (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.  
  • Owen CA, Campbell MA, Sannes PL, Boukedes SS, Campbell EJ (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.  
  • Savage MJ, Iqbal M, Loh T, Trusko SP, Scott R, Siman R (1994). "Cathepsin G: localization in human cerebral cortex and generation of amyloidogenic fragments from the beta-amyloid precursor protein". Neuroscience 60 (3): 607–19.  
  • 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.  
  • 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.  

External links

  • 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.