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Cathepsin G

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Template:PBB 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

References

  1. ^ a b 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.
  • 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.

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