Cathepsin G

Cathepsin G
PDB rendering based on 1au8.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1AU8​, 1CGH​, 1KYN​, 1T32​
Identifiers
Symbols	CTSG ; CATG; CG
External IDs	OMIM: 116830 MGI: 88563 HomoloGene: 105646 ChEMBL: 4071 GeneCards: CTSG Gene
EC number	3.4.21.20
Gene ontology Molecular function • serine-type endopeptidase activity • protein binding • heparin binding • peptidase activity Cellular component • extracellular region • extracellular space • nucleus • cytoplasm • plasma membrane • cell surface • secretory granule • extracellular matrix • extracellular exosome Biological process • angiotensin maturation • protein phosphorylation • proteolysis • immune response • protein processing • extracellular matrix disassembly • extracellular matrix organization • response to lipopolysaccharide • negative regulation of growth of symbiont in host • cellular protein metabolic process • positive regulation of immune response • defense response to fungus • neutrophil mediated killing of gram-positive bacterium Sources: Amigo / QuickGO
RNA expression pattern
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: 24.57 – 24.58 Mb	Chr 14: 56.1 – 56.1 Mb
PubMed search

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, 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

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

Animal studies

Potential implications of the enzyme in blood-brain barrier breakdown was also found.^[4]

See also

• Cathepsins

References

1. Thomas MP, Whangbo J, McCrossan G, Deutsch AJ, Martinod K, Walch M, Lieberman J (Jun 2014). "Leukocyte protease binding to nucleic acids promotes nuclear localization and cleavage of nucleic acid binding proteins". Journal of Immunology 192 (11): 5390–7. doi:10.4049/jimmunol.1303296. PMC 4041364. PMID 24771851.
2. "Entrez Gene: CTSG cathepsin G".
3. Whitelock RB, Fukuchi T, Zhou L, Twining SS, Sugar J, Feder RS, Yue BY (Feb 1997). "Cathepsin G, acid phosphatase, and alpha 1-proteinase inhibitor messenger RNA levels in keratoconus corneas". Investigative Ophthalmology & Visual Science 38 (2): 529–34. PMID 9040486.
4. Armao D, Kornfeld M, Estrada EY, Grossetete M, Rosenberg GA (Sep 1997). "Neutral proteases and disruption of the blood-brain barrier in rat". Brain Research 767 (2): 259–64. doi:10.1016/S0006-8993(97)00567-2. PMID 9367256.

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". Current Pharmaceutical Design 8 (9): 695–702. doi:10.2174/1381612023395376. PMID 11945165.
• Cohen AB, Stevens MD, Miller EJ, Atkinson MA, Mullenbach G (Aug 1992). "Generation of the neutrophil-activating peptide-2 by cathepsin G and cathepsin G-treated human platelets". The American Journal of Physiology 263 (2 Pt 1): L249–56. PMID 1387511.
• Sasaki T, Ueno-Matsuda E (Dec 1992). "Immunocytochemical localization of cathepsins B and G in odontoclasts of human deciduous teeth". Journal of Dental Research 71 (12): 1881–4. doi:10.1177/00220345920710120501. PMID 1452887.
• Maison CM, Villiers CL, Colomb MG (Aug 1991). "Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G". Journal of Immunology 147 (3): 921–6. PMID 1861080.
• Brandt E, Van Damme J, Flad HD (Jul 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 (Aug 1990). "Elastase and cathepsin G of human monocytes: heterogeneity and subcellular localization to peroxidase-positive granules". The Journal of Histochemistry and Cytochemistry 38 (8): 1179–86. doi:10.1177/38.8.2164060. PMID 2164060.
• Pratt CW, Tobin RB, Church FC (Apr 1990). "Interaction of heparin cofactor II with neutrophil elastase and cathepsin G". The Journal of Biological Chemistry 265 (11): 6092–7. PMID 2318847.
• Gabay JE, Scott RW, Campanelli D, Griffith J, Wilde C, Marra MN, Seeger M, Nathan CF (Jul 1989). "Antibiotic proteins of human polymorphonuclear leukocytes". Proceedings of the National Academy of Sciences of the United States of America 86 (14): 5610–4. doi:10.1073/pnas.86.14.5610. PMC 297672. PMID 2501794.
• Hohn PA, Popescu NC, Hanson RD, Salvesen G, Ley TJ (Aug 1989). "Genomic organization and chromosomal localization of the human cathepsin G gene". The Journal of Biological Chemistry 264 (23): 13412–9. PMID 2569462.
• 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 Microscopy. Supplement 3: 231–9; discussion 239–40. PMID 2616953.
• Campbell EJ, Silverman EK, Campbell MA (Nov 1989). "Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity". Journal of Immunology 143 (9): 2961–8. PMID 2681419.
• Salvesen G, Farley D, Shuman J, Przybyla A, Reilly C, Travis J (Apr 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 (Oct 1986). "Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors". Analytical Biochemistry 158 (1): 217–27. doi:10.1016/0003-2697(86)90612-3. PMID 3799965.
• Crocker J, Jenkins R, Burnett D (May 1985). "Immunohistochemical localization of cathepsin G in human tissues". The American Journal of Surgical Pathology 9 (5): 338–43. doi:10.1097/00000478-198505000-00003. PMID 3911778.
• Klickstein LB, Kaempfer CE, Wintroub BU (Dec 1982). "The granulocyte-angiotensin system. Angiotensin I-converting activity of cathepsin G". The Journal of Biological Chemistry 257 (24): 15042–6. PMID 6294088.
• LaRosa CA, Rohrer MJ, Benoit SE, Barnard MR, Michelson AD (Jul 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, Boukedes SS, Campbell EJ (Nov 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". The Journal of Cell Biology 131 (3): 775–89. doi:10.1083/jcb.131.3.775. PMC 2120617. PMID 7593196.
• Savage MJ, Iqbal M, Loh T, Trusko SP, Scott R, Siman R (Jun 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 (Sep 1994). "Early myeloid cell-specific expression of the human cathepsin G gene in transgenic mice". Proceedings of the National Academy of Sciences of the United States of America 91 (19): 8989–93. doi:10.1073/pnas.91.19.8989. PMC 44732. PMID 8090757.
• Maruyama K, Sugano S (Jan 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

• 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.