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experimental abdominal aortic aneurysms. Proc Natl Acad Sci U S A 2007;104:2855-60. DOI PubMed PMC
74. John DS, Aschenbach J, Krüger B, et al. Deficiency of cathepsin C ameliorates severity of acute pancreatitis by reduction of
neutrophil elastase activation and cleavage of E-cadherin. J Biol Chem 2019;294:697-707. DOI PubMed PMC
75. Fan K, Wu X, Fan B, et al. Up-regulation of microglial cathepsin C expression and activity in lipopolysaccharide-induced
neuroinflammation. J Neuroinflamm 2012;9:1-13. DOI PubMed
76. Keir HR, Shoemark A, Dicker AJ, et al. Neutrophil extracellular traps, disease severity, and antibiotic response in bronchiectasis: an
international, observational, multicohort study. Lancet Respir Med 2021;9:873-84. DOI
77. Kim S, Nadel JA. Role of neutrophils in mucus hypersecretion in COPD and implications for therapy. Treat Respir Med 2004;3:147-
59. DOI PubMed
78. Guarino C, Hamon Y, Croix C, et al. Prolonged pharmacological inhibition of cathepsin C results in elimination of neutrophil serine
proteases. Biochem Pharmacol 2017;131:52-67. DOI
79. Sanchez Klose FP, Björnsdottir H, Dahlstrand Rudin A, et al. A rare CTSC mutation in Papillon-Lefèvre syndrome results in
abolished serine protease activity and reduced NET formation but otherwise normal neutrophil function. PLoS One
2021;16:e0261724. DOI PubMed PMC
80. Bullón P, Castejón-Vega B, Román-Malo L, et al. Autophagic dysfunction in patients with Papillon-Lefèvre syndrome is restored by
recombinant cathepsin C treatment. J Allergy Clin Immunol 2018;142:1131-1143.e7. DOI
81. Suban D, Zajc T, Renko M, Turk B, Turk V, Dolenc I. Cathepsin C and plasma glutamate carboxypeptidase secreted from Fischer rat
thyroid cells liberate thyroxin from the N-terminus of thyroglobulin. Biochimie 2012;94:719-26. DOI PubMed
82. Bernardini F, Warburton MJ. Lysosomal degradation of cholecystokinin-(29-33)-amide in mouse brain is dependent on tripeptidyl
peptidase-I: implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis. Biochem
J 2002;366:521-9. DOI PubMed PMC
83. Sleat DE, Donnelly RJ, Lackland H, et al. Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid
lipofuscinosis. Science 1997;277:1802-5. DOI
84. Kim KH, Pham CT, Sleat DE, Lobel P. Dipeptidyl-peptidase I does not functionally compensate for the loss of tripeptidyl-peptidase I
in the neurodegenerative disease late-infantile neuronal ceroid lipofuscinosis. Biochem J 2008;415:225-32. DOI PubMed PMC
85. Zhang GP, Yue X, Li SQ. Cathepsin C interacts with TNF-α/p38 MAPK signaling pathway to promote proliferation and metastasis in
hepatocellular carcinoma. Cancer Res Treat 2020;52:10-23. DOI PubMed PMC
86. Kim S, Lee S-I, Kim N, et al. Decursin inhibits cell growth and autophagic flux in gastric cancer via suppression of cathepsin C. Am J
Cancer Res 2021;11:1304. PubMed PMC
87. Khaket TP, Singh MP, Khan I, Bhardwaj M, Kang SC. Targeting of cathepsin C induces autophagic dysregulation that directs ER
stress mediated cellular cytotoxicity in colorectal cancer cells. Cell Signal 2018;46:92-102. DOI PubMed
88. Xiao Y, Cong M, Li J, et al. Cathepsin C promotes breast cancer lung metastasis by modulating neutrophil infiltration and neutrophil
extracellular trap formation. Cancer Cell 2021;39:423-437.e7. DOI
89. Korkmaz B, Lamort AS, Domain R, et al. Cathepsin C inhibition as a potential treatment strategy in cancer. Biochem Pharmacol
2021;194:114803. DOI
90. Kavčič N, Butinar M, Sobotič B, et al. Intracellular cathepsin C levels determine sensitivity of cells to leucyl-leucine methyl ester-
triggered apoptosis. FEBS J 2020;287:5148-66. DOI PubMed
91. Nicklin MJ, Barrett AJ. Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin. Biochem J 1984;223:245-
53. DOI PubMed PMC
92. Tušar L, Usenik A, Turk B, Turk D. Mechanisms applied by protein inhibitors to inhibit cysteine proteases. Int J Mol Sci
2021;22:997. DOI PubMed PMC
93. Hamilton G, Colbert JD, Schuettelkopf AW, Watts C. Cystatin F is a cathepsin C-directed protease inhibitor regulated by proteolysis.
EMBO J 2008;27:499-508. DOI PubMed PMC
94. Halfon S, Ford J, Foster J, et al. Leukocystatin, a new Class II cystatin expressed selectively by hematopoietic cells. J Biol Chem
1998;273:16400-8. DOI
95. Božič J, Dolenc I. Feedback regulation of cathepsin C by the propeptide dipeptides of granzymes A and B. ACSi 2019;66:501-9. DOI
96. Méthot N, Rubin J, Guay D, et al. Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires
sustained exposure to prevent pro-enzyme processing. J Biol Chem 2007;282:20836-46. DOI
97. Mølgaard A, Arnau J, Lauritzen C, Larsen S, Petersen G, Pedersen J. The crystal structure of human dipeptidyl peptidase I (cathepsin
C) in complex with the inhibitor Gly-Phe-CHN2. Biochem J 2007;401:645-50. DOI PubMed PMC
98. Green GD, Shaw E. Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases. J Biol Chem 1981;256:1923-8. DOI
PubMed
99. Laine DI, Busch-Petersen J. Inhibitors of cathepsin C (dipeptidyl peptidase I). Expert Opin Ther Pat 2010;20:497-506. DOI PubMed
100. Furber M, Tiden AK, Gardiner P, et al. Cathepsin C inhibitors: property optimization and identification of a clinical candidate. J Med
Chem 2014;57:2357-67. DOI
101. Gardiner P, Wikell C, Clifton S, Shearer J, Benjamin A, Peters SA. Neutrophil maturation rate determines the effects of dipeptidyl
peptidase 1 inhibition on neutrophil serine protease activity. Br J Pharmacol 2016;173:2390-401. DOI PubMed PMC
102. Bragg RA, Brocklehurst S, Gustafsson F, et al. Aortic binding of AZD5248: mechanistic insight and reactivity assays to support lead
optimzation. Chem Res Toxicol 2015;28:1991-9. DOI