Siming GAO, Honglin ZHU, Xiaoxia ZUO, Hui LUO

Department of Rheumatology, Xiangya Hospital, Hunan, China

Keywords: Autoimmune disease; cathepsin G; immune reaction; inflammation

Abstract

Cathepsin G belongs to the neutrophil serine proteases family, known for its function in killing pathogens. Studies over the past several years indicate that cathepsin G has important effects on inflammation and immune reaction, and may be a key factor in the pathogenesis of some autoimmune diseases. In this article, we discuss the roles of cathepsin G in inflammation, immune reaction, and autoimmune diseases. To our knowledge, this is the first study providing important information about cathepsin G in the pathogenesis of autoimmune diseases and suggesting that cathepsin G may be a new biomarker or treatment target.

Cathepsin G (CTSG) is a member of the serine proteases family, which was first found in the azurophilic granules of neutrophil leukocytes and named in 1976.(1,2) Then, CTSG was detected in other myeloid cells, such as B cells, primary human monocytes, myeloid dendritic cells, plasmacytoid dendritic cells, and murine microglia.(3) Recently, studies proved that CTSG also existed in neutrophil traps and human urine exosomes.(4,5) The gene for CTSG was located on chromosome 14q11.2, spans 2.7kb, and consists five exons and four introns,(6) prepro-CTSG was a 255-amino-acid residue protein. After cleavage of the signal peptide, two amino acids and 11 amino acids remain at the N-terminal and C-terminal side of pro-CTSG, respectively. Both of these may be released by proteases.(7) CTSG was stored in primary granules in the aforementioned cells, and when the cells were stimulated by immune complexes, some pharmacological agents or phagocytosis, CTSG was released to the extracellular space or bound on the surface of those cells(1,8) which were the two active forms of CTSG.(9) Released CTSG can evade its inhibitors, which exist in the extracellular space, by binding to cell membranes, forming sequestered microenvironments, binding to its substrates tightly, and inactivating its inhibitors.(10)

Cathepsin G has many functions. It can clear pathogens, regulate inflammation by modifying the chemokines, cytokines, cell surface receptors,(11-14) and C components,(1) control the blood pressure, and induce thrombogenesis.(15,16) Purified CTSG also has important effects on increasing the permeability of endothelial cells(17) and epithelial cells.(18) Furthermore, studies have shown that mice with loss-of-function mutations in CTSG were resistant to experimental arthritis,(19) and had marked decrease in tubular cells apoptosis and collagen deposition after renal ischemia/ reperfusion injury.(20) Inhibition of CTSG with its inhibitor reduced tumor growth factor-beta signaling, which subsequently reduced tumor vascularity by decreasing in both monocyte chemotactic protein-1 and vascular endothelial growth factor.(21) The CTSG family members may become new biomarkers or treatment targets for autoimmune diseases and other diseases in the following years. In this article, we reviewed the effects of CTSG in inflammation and immune reaction, and discussed the important roles of CTSG in autoimmune diseases.

Roles of cathepsin G in inflammation and immune Reaction

Cathepsin G has important roles in the development of inflammation. It promotes the migration of neutrophils, monocytes and antigen presenting cells (APCs) by changing chemokine (C-X-C motif) ligand 5 and chemokine (C-C motif) ligand 15 into more potent chemotactic factors by proteolytic processing of CTSG,(22,23) and converting prochemerin into chemerin, which is a novel chemoattractant factor that specifically attracts APCs through its receptor ChemR.(23,24) CTSG is able to cleave chemokine (C-C motif) ligand 23 at its N-terminal or C-terminal, resulting in potent CC-type chemokine receptor 1 and formyl peptide receptor-like 1 activity, which is an attractant of monocytes and neutrophils in vitro, and recruit leukocytes in vivo.(25) CTSG can also promote inflammation by activating the cell surface receptors. For example, CTSG directly activates protease-activated receptors 4 (PAR4) at the surface of platelets, which may lead to platelet secretion and aggregation, and the interaction between neutrophils and platelets at the sites of inflammation or vascular injury.(26) CTSG is able to activate protease-activated receptors 2 (PAR2) on the surface of human gingival fibroblasts by cleaving the peptide corresponding to the N terminus of PAR2, which leads to the production and secretion of interleukin-8 and monocyte chemoattractant protein 1 and may play roles in a number of inflammatory processes such as periodontitis.(27) CTSG stimulates monocytes to produce oxidative burst and pro-inflammatory cytokines by releasing soluble CD23 fragments, which is independent of any co-stimulatory signals.(28)

The roles of CTSG in immune reaction are mediated by regulating the autoantigen processing, and activating lymphocytes, and so on. It has been proven that CTSG degraded the immunodominant myelin basic protein (MBP) epitope (MBP85-99), generated another T cell epitope (MBP115-123), and eliminated its binding to major histocompatibility complex (MHC) class II and a MBP-specific T cell response, thus participating in the immunopathogenesis of multiple sclerosis.(29) CTSG also plays a critical role in processing proinsulin into several intermediates, which can polarize T cell activation in type 1 diabetes.(30) Selective inhibition of CTSG result in reduced tetanus toxin C-fragment and hemagglutinin processing and presentation to CD4+ T cells,(31) and CTSG augments antigen specific antibody via activation of T cells by involving both T helper 1 (Th1) and Th2 pathways in BALB/c mice.(32) Some scientists show that CTSG on the U937 cell surface is able to cleave complement 3 (C3) into C3a-, C3b-, C3c- and C3d-like fragments, and these active fragments are likely to be involved in cell-protein interactions, and cell-cell interactions, and in mediating immune reaction and inflammatory response.(33)

Cathepsin G augments the production of antigen-specific antibody by activating T cells in BALB/C mice.(32) CTSG binds to lymphocytes, including CD4+, CD8+, natural killer, and B cells with a thrombin-like receptor,(34) increases the cytotoxicity of natural killer cells, activates reactive T cells, and increases cytokines and antigen- specific antibody production. All the above functions are CTSG dose dependent.(35)

Roles of cathepsin G in vasculaR peRmeability

Cathepsin G affects the cell shapes and causes the formation of intercellular gap in the endothelial cells and epithelial cells, which can increase their permeability. The exact mechanism may relate to breaking the balance of calcium homeostasis, which may lead to increased inositol phosphate and the activation of protein kinase C, and increase albumin flux across the endothelial monolayer;(36) or relate to cleaving the extracellular part of vascular endothelial cadherin, an essential protein to maintain vascular integrity.(37) Scientists have found that neutrophil surface- bound proteases could cleave vascular endothelial cadherin of human umbilical vein endothelial cells inducing the formation of gaps and increasing the transmigration of neutrophils, and these could be reduced by specific inhibition of CTSG.(37,38) CTSG can also increase the permeability of human microvascular endothelial cell monolayers by degrading the tight junction protein occludin and vascular endothelial-cadherin, which may mediate the vasogenic edema during diabetic ketoacidosis.(39) The mechanisms of CTSG increasing the vascular permeability may also have some relationship with its role in cleaving extracellular matrix components.

Cathepsin G increases the permeability of type II epithelial monolayers in some types of acute and chronic lung disease, which is accompanied by structural changes in the monolayers with enlarged intercellular gaps visible by scanning electron microscopy.(40) CTSG increases the paracellular permeability of intestinal epithelial barriers through PAR4, and increases the phosphorylation of myosin light chain, leading to the disruption of epithelial tight junction in ulcerative colitis.(41,42)

Cathepsin G affects tissue remodeling directly by degrading components of the matrix and indirectly by cleaving and activating matrix-degrading metalloproteinases. It has been proven that CTSG induces the activation of promatrix metalloproteinase-2 in a dose- and time-dependent way, and injuries the microvasculature, thus playing roles in tumor invasion and angiogenesis.(43) CTSG has been found in the physiologic and pathologic vascular regression, and to be capable of activating matrix metalloproteinase-1 and matrix metalloproteinase-10, participating in capillary tube regression and collagen gel contraction.(44)

Increased vascular permeability is found in numerous diseases, such as sepsis, acute lung injury, encephaledema, and so on. Thus, CTSG may involve in the development and progression of these diseases, but the specific molecular mechanism needs further studies.

Cathepsin G and autoimmune diseases

As mentioned above, the role of CTSG in immune reaction and inflammation is complicated and various, and CTSG participate in the pathogenesis of some autoimmune diseases. The concentration and activity of CTSG are increased in the synovial fluids of rheumatoid arthritis (RA) patients when compared with healthy controls or patients with osteoarthritis. However, the CTSG messenger ribonucleic acid (mRNA) levels are not higher in CD14+ cells of RA, because CTSG mainly play roles in peripheral joints.(45) As a monocyte chemoattractant, CTSG affected the involvement of monocytes in synovial lesions of RA patients, and CTSG concentration in the synovial fluid of RA patients was significantly correlated with the count of lymphocytes.(46) Studies have shown that CTSG in the adjacent cartilage-pannus junction can degrade articular cartilage in RA.(47) CTSG is one of the antigens of anti-neutrophil cytoplasmic antibodies in Japanese patients with RA, but the difference between the positive and negative groups in terms of clinical manifestations and laboratory parameters is not significant.(48) Further studies are necessary to elucidate how CTSG increases monocyte chemotaxis and its exact role in the pathogenesis of RA.

Cathepsin G was the major antigen for anti- neutrophil cytoplasmic antibodies in systemic lupus erythematosus (SLE), and the CTSG antibodies in the sera of active SLE patients were significantly increased than inactive patients and healthy controls, and rapidly decreased after the corticosteroid therapy.(49) Other studies also proved that CTSG in the sera of SLE patients may correlate with disease activity and vasculitis, but has no relationship with organic involvement.(50,51) Anti-CTSG anti- neutrophil cytoplasmic antibodies were the major antigenic targets of antineutrophil cytoplasmic autoantibodies in systemic sclerosis, but were not significantly associated with any clinical or serological features. However, the exact role in scleroderma needs to be clarified.(52,53)

The mRNA levels of CTSG increase in peripheral blood mononuclear cells and muscles of dermatomyositis patients. The activity of serum CTSG also increase in dermatomyositis and correlate with creatine kinase and lactate dehydrogenase levels; moreover, patients with Jo-1 auto-antibody have higher activity of CTSG. Besides, CTSG increases the lymphocytes infiltration through inducing the expression of protease activated receptor 2 and altering the cytoskeleton of human dermal microvascular endothelial cells.(54)

As for multiple sclerosis, CTSG participated in the disease development as a rate-limiting protease for the degradation of intact myelin basic protein. CTSG can directly destroy the major immunodominant myelin basic protein epitope, which may enable myelin basic protein-specific autoreactive T cells to escape negative selection, therefore involving in the pathogenesis of multiple sclerosis.(29,55)

Both the transcript level and activity of CTSG were increased in type 1 diabetes mellitus patients compared with healthy control donors. CTSG degraded proinsulin after internalization into endocytic compartments, and activated proinsulin reactive T cells. This process can be significantly reduced by a CTSG inhibitor.(30) In non-obese diabetic mice, the expression of CTSG was increased. Treating the mice with CTSG-specific inhibitor reduced the blood glucose level, improved the function of islet beta cells, and reduced the activation of CD4+ T cells. Using CTSG small interfering RNA in the pre-diabetic mellitus stage improved the function of islet beta cells, reduced islet inflammation and beta cell apoptosis, and lowered the activation level of CD4+ T cells, thus slowing down the progression of diabetes.(56)

In conclusion, CTSG has important roles in the development and progression of some autoimmune diseases. Although the specific role needs further clarification, it may involve the activation of immune cells and the mobilization of immune reaction by inducing the production of lymphokines, which in turn promote T cell- dependent cellular immunity and antigen-specific antibody production.

Other cathepsins and autoimmune diseases

Except for CTSG, other cathepsins also play important roles in autoimmune diseases and serve as useful biomarkers. The concentration and activity of cathepsin B,(57-59) cathepsin D,(60) cathepsin K,(61,62) cathepsin L,(63,64) and cathepsin S(65) were increased in synovial cells, synovial fluid and even in the sera of RA patients. When inhibited by specific inhibitor, they could suppress autoimmune inflammation of the joints, and osteoclastic bone resorption, leading to less cartilage damage. The upregulation of cathepsin K in the sera of RA patients correlated with the degree of radiological damage, and erythrocyte sedimentation rate.(62) The level of cathepsin L and cathepsin S in the synovial fluid was higher in patients with anti-cyslic citrullinated peptides, immunoglobulin M-rheumatoid factor and immunoglobulin A-rheumatoid factor.(64)

In SLE patients, the activity of serum cathepsin D correlated with renal involvement.(65) In MRL-Fas(lpr) mice, cathepsin S could promote SLE by driving MHC II mediated T and B cell priming, germinal center formation and B cell maturation towards the plasma cells, which could be reversed by its antagonists.(66)

In Sjögren’s syndrome; cathepsin B, cathepsin D, and cathepsin S were present and had greater immunoreactivity in the acini and tears of patients.(67,68) and cathepsin S inhibitor was effective in preventing the autoimmune lesions of the salivary and lacrimal glands in the Sjögren’s syndrome model.(69) Cathepsin K was also strongly expressed in ankylosing spondylitis patients at the sites of bone destruction.(70) The expression and activity of cathepsin B,(71,72) cathepsin D, and cathepsin S(73) were elevated in multiple sclerosis patients, and were associated with the physiologic degradation of myelin basic protein. It has been proven that single nucleotide polymorphisms within cathepsin S gene were closely associated with the immunotherapies for multiple sclerosis.(74) Cathepsin B(75) and cathepsin S(76) also had a potential role in the pathology of Graves’ disease and myasthenia gravis.

In conclusion, cathepsin G is an important regulator of immune reaction and inflammation. Studies over the past years demonstrate that, besides clearing pathogens, CTSG can regulate immune reaction and inflammatory response by modifying chemokines, cytokines, and cell surface receptors, and activate some lymphocytes. It can also increase the permeability of endothelial cells and epithelial cells. Recently, more and more reports show that CTSG family members play pivotal roles in the development and progression of autoimmune diseases, and their concentrations or activities correlate with the clinical or serological features of diseases. Nonetheless, the exact mechanism needs further studies. Studies indicate that inhibition of CTSG may be an effective approach for the treatment of atopic dermatitis, psoriasis, psoriatic arthritis, RA, and other clinical conditions.(77) Along with other studies on the pathogenesis of CTSG in inflammation and autoimmune disease, CTSG may become a new biomarker or therapeutic targets in some diseases.

Citation: Gao S, Zhu H, Zuo X, Luo H. Cathepsin G and its role in inflammation and autoimmune diseases. Arch Rheumatol 2018;33(4):498-504.

Conflict of Interest

The authors declared no conflicts of interest with respect to the authorship and/or publication of this article.

Financial Disclosure

This work was supported by grants from National Natural Science Foundation of China (81373206, 81401357), National High Technology Research and Development Program of China (2012AA02A513), Hunan Natural Science Foundation (13JJ5010), Hunan Special Fund for Science and Technology Development Program (2013WK3022), and Independent Innovation Projects of Central South University (2016zzts131).

References

  1. Starkey PM, Barrett AJ. Human cathepsin G. Catalytic and immunological properties. Biochem J 1976;155:273-8.
  2. Delgado MB, Clark-Lewis I, Loetscher P, Langen H, Thelen M, Baggiolini M, et al. Rapid inactivation of stromal cell-derived factor-1 by cathepsin G associated with lymphocytes. Eur J Immunol 2001;31:699-707.
  3. Burster T, Macmillan H, Hou T, Boehm BO, Mellins ED. Cathepsin G: roles in antigen presentation and beyond. Mol Immunol 2010;47:658-65.
  4. Brinkmann V, Reichard U, Goosmann C, Fauler B, Uhlemann Y, Weiss DS, et al. Neutrophil extracellular traps kill bacteria. Science 2004;303:1532-5.
  5. Prunotto M, Farina A, Lane L, Pernin A, Schifferli J, Hochstrasser DF, et al. Proteomic analysis of podocyte exosome-enriched fraction from normal human urine. J Proteomics 2013;82:193-229.
  6. Caughey GH, Schaumberg TH, Zerweck EH, Butterfield JH, Hanson RD, Silverman GA, et al. The human mast cell chymase gene (CMA1): mapping to the cathepsin G/granzyme gene cluster and lineage- restricted expression. Genomics 1993;15:614-20.
  7. Adkison AM, Raptis SZ, Kelley DG, Pham CT. Dipeptidyl peptidase I activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis. J Clin Invest 2002;109:363-71.
  8. Bank U, Ansorge S. More than destructive: neutrophil- derived serine proteases in cytokine bioactivity control. J Leukoc Biol 2001;69:197-206.
  9. Owen CA, Campbell MA, Sannes PL, Boukedes SS, Campbell EJ. 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 1995;131:775-89.
  10. Owen CA, Campbell EJ. Extracellular proteolysis: new paradigms for an old paradox. J Lab Clin Med 1999;134:341-51.
  11. Meyer-Hoffert U. Neutrophil-derived serine proteases modulate innate immune responses. Front Biosci (Landmark Ed) 2009;14:3409-18.
  12. Nathan C. Neutrophils and immunity: challenges and opportunities. Nat Rev Immunol 2006;6:173-82.
  13. Pham CT. Neutrophil serine proteases: specific regulators of inflammation. Nat Rev Immunol 2006;6:541-50.
  14. Pham CT. Neutrophil serine proteases fine-tune the inflammatory response. Int J Biochem Cell Biol 2008;40:1317-33.
  15. Tonnesen MG, Klempner MS, Austen KF, Wintroub BU. Identification of a human neutrophil angiotension II-generating protease as cathepsin G. J Clin Invest 1982;69:25-30.
  16. Selak MA, Chignard M, Smith JB. Cathepsin G is a strong platelet agonist released by neutrophils. Biochem J 1988;251:293-9.
  17. Pintucci G, Iacoviello L, Castelli MP, Amore C, Evangelista V, Cerletti C, et al. Cathepsin G--induced release of PAI-1 in the culture medium of endothelial cells: a new thrombogenic role for polymorphonuclear leukocytes? J Lab Clin Med 1993;122:69-79.
  18. Peterson MW. Neutrophil cathepsin G increases transendothelial albumin flux. J Lab Clin Med 1989;113:297-308.
  19. Hu Y, Pham CT. Dipeptidyl peptidase I regulates the development of collagen-induced arthritis. Arthritis Rheum 2005;52:2553-8.
  20. Shimoda N, Fukazawa N, Nonomura K, Fairchild RL. Cathepsin g is required for sustained inflammation and tissue injury after reperfusion of ischemic kidneys. Am J Pathol 2007;170:930-40.
  21. Wilson TJ, Nannuru KC, Futakuchi M, Singh RK. Cathepsin G-mediated enhanced TGF-beta signaling promotes angiogenesis via upregulation of VEGF and MCP-1. Cancer Lett 2010;288:162-9.
  22. Richter R, Bistrian R, Escher S, Forssmann WG, Vakili J, Henschler R, et al. Quantum proteolytic activation of chemokine CCL15 by neutrophil granulocytes modulates mononuclear cell adhesiveness. J Immunol 2005;175:1599-608.
  23. Nufer O, Corbett M, Walz A. Amino-terminal processing of chemokine ENA-78 regulates biological activity. Biochemistry 1999;38:636-42.
  24. Wittamer V, Bondue B, Guillabert A, Vassart G, Parmentier M, Communi D. Neutrophil-mediated maturation of chemerin: a link between innate and adaptive immunity. J Immunol 2005;175:487-93.
  25. Miao Z, Premack BA, Wei Z, Wang Y, Gerard C, Showell H, et al. Proinflammatory proteases liberate a discrete high-affinity functional FPRL1 (CCR12) ligand from CCL23. J Immunol. 2007;178:7395-404.
  26. Sambrano GR, Huang W, Faruqi T, Mahrus S, Craik C, Coughlin SR. Cathepsin G activates protease- activated receptor-4 in human platelets. J Biol Chem 2000;275:6819-23.
  27. Uehara A, Muramoto K, Takada H, Sugawara S. Neutrophil serine proteinases activate human nonepithelial cells to produce inflammatory cytokines through protease-activated receptor 2. J Immunol 2003;170:5690-6.
  28. Brignone C, Munoz O, Batoz M, Rouquette-Jazdanian A, Cousin JL. Proteases produced by activated neutrophils are able to release soluble CD23 fragments endowed with proinflammatory effects. FASEB J 2001;15:2027-9.
  29. Burster T, Beck A, Tolosa E, Marin-Esteban V, Rötzschke O, Falk K, et al. Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes. J Immunol 2004;172:5495- 503.
  30. Zou F, Schäfer N, Palesch D, Brücken R, Beck A, Sienczyk M, et al. Regulation of cathepsin G reduces the activation of proinsulin-reactive T cells from type 1 diabetes patients. PLoS One 2011;6:e22815.
  31. Reich M, Lesner A, Legowska A, Sieńczyk M, Oleksyszyn J, Boehm BO, et al. Application of specific cell permeable cathepsin G inhibitors resulted in reduced antigen processing in primary dendritic cells. Mol Immunol2009;46:2994-9.
  32. Tani K, Murphy WJ, Chertov O, Oppenheim JJ, Wang JM. The neutrophil granule protein cathepsin G activates murine T lymphocytes and upregulates antigen-specific IG production in mice. Biochem Biophys Res Commun 2001;282:971-6.
  33. Maison CM, Villiers CL, Colomb MG. Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G. J Immunol 1991;147:921-6.
  34. Yamazaki T, Aoki Y. Cathepsin G binds to human lymphocytes. J Leukoc Biol 1997;61:73-9.
  35. Yamazaki T, Aoki Y. Cathepsin G enhances human natural killer cytotoxicity. Immunology 1998;93:115-21.
  36. Peterson MW, Gruenhaupt D, Shasby DM. Neutrophil cathepsin G increases calcium flux and inositol polyphosphate production in cultured endothelial cells. J Immunol 1989;143:609-16.
  37. Cohen-Mazor M, Mazor R, Kristal B, Sela S. Elastase and cathepsin G from primed leukocytes cleave vascular endothelial cadherin in hemodialysis patients. Biomed Res Int 2014;2014:459640.
  38. Hermant B, Bibert S, Concord E, Dublet B, Weidenhaupt M, Vernet T, et al. Identification of proteases involved in the proteolysis of vascular endothelium cadherin during neutrophil transmigration. J Biol Chem 2003;278:14002-12.
  39. Woo MM, Patterson EK, Clarson C, Cepinskas G, Bani-Yaghoub M, Stanimirovic DB, et al. Elevated Leukocyte Azurophilic Enzymes in Human Diabetic Ketoacidosis Plasma Degrade Cerebrovascular Endothelial Junctional Proteins. Crit Care Med 2016;44:846-53.
  40. Rochat T, Casale J, Hunninghake GW, Peterson MW. Neutrophil cathepsin G increases permeability of cultured type II pneumocytes. Am J Physiol 1988;255:603-11.
  41. Dabek M, Ferrier L, Roka R, Gecse K, Annahazi A, Moreau J, et al. Luminal cathepsin g and protease- activated receptor 4: a duet involved in alterations of the colonic epithelial barrier in ulcerative colitis. Am J Pathol 2009;175:207-14.
  42. Dabek M, Ferrier L, Annahazi A, Bézirard V, Polizzi A, Cartier C, et al. Intracolonic infusion of fecal supernatants from ulcerative colitis patients triggers altered permeability and inflammation in mice: role of cathepsin G and protease-activated receptor-4. Inflamm Bowel Dis 2011;17:1409-14.
  43. Shamamian P, Schwartz JD, Pocock BJ, Monea S, Whiting D, Marcus SG, et al. Activation of progelatinase A (MMP-2) by neutrophil elastase, cathepsin G, and proteinase-3: a role for inflammatory cells in tumor invasion and angiogenesis. J Cell Physiol 2001;189:197-206.
  44. Saunders WB, Bayless KJ, Davis GE. MMP-1 activation by serine proteases and MMP-10 induces human capillary tubular network collapse and regression in 3D collagen matrices. J Cell Sci 2005;11:2325-40.
  45. Trzybulska D, Olewicz-Gawlik A, Graniczna K, Kisiel K, Moskal M, Cieslak D, et al. Quantitative analysis of elastase and cathepsin G mRNA levels in peripheral blood CD14(+) cells from patients with rheumatoid arthritis. Cell Immuno2014;292:40-4.
  46. Miyata J, Tani K, Sato K, Otsuka S, Urata T, Lkhagvaa B, et al. Cathepsin G: the significance in rheumatoid arthritis as a monocyte chemoattractant. Rheumatol Int 2007;27:375-82.
  47. Velvart M, Fehr K. Degradation in vivo of articular cartilage in rheumatoid arthritis and juvenile chronic arthritis by cathepsin G and elastase from polymorphonuclear leukocytes. Rheumatol Int 1987;7:195-202.
  48. Tamiya H, Tani K, Miyata J, Sato K, Urata T, Lkhagvaa B, et al. Defensins- and cathepsin G-ANCA in systemic lupus erythematosus. Rheumatol Int 2006;27:147-52.
  49. Kida I, Kobayashi S, Takeuchi K, Tsuda H, Hashimoto H, Takasaki Y. Antineutrophil cytoplasmic antibodies against myeloperoxidase, proteinase 3, elastase, cathepsin G and lactoferrin in Japanese patients with rheumatoid arthritis. Mod Rheumatol 2011;21:43-50.
  50. Zhao MH, Liu N, Zhang YK, Wang HY. Antineutrophil cytoplasmic autoantibodies (ANCA) and their target antigens in Chinese patients with lupus nephritis. Nephrol Dial Transplant 1998;13:2821-4.
  51. Nishiya K, Chikazawa H, Nishimura S, Hisakawa N, Hashimoto K. Anti-neutrophil cytoplasmic antibody in patients with systemic lupus erythematosus is unrelated to clinical features. Clin Rheumatol 1997;16:70-5.
  52. Grypiotis P, Ruffatti A, Cozzi F, Sinico RA, Tonello M, Radice A, et al. Prevalence and clinical significance of cathepsin G antibodies in systemic sclerosis. Reumatismo 2003;55:256-62. [Abstract]
  53. Khanna D, Aggarwal A, Bhakuni DS, Dayal R, Misra R. Bactericidal/permeability-increasing protein and cathepsin G are the major antigenic targets of antineutrophil cytoplasmic autoantibodies in systemic sclerosis. J Rheumatol 2003;30:1248-52.
  54. Gao S, Zhu H, Yang H, Zhang H, Li Q, Luo H. The role and mechanism of cathepsin G in dermatomyositis. Biomed Pharmacother 2017;94:697-704.
  55. Burster T, Beck A, Poeschel S, Øren A, Baechle D, Reich M, et al. Interferon-gamma regulates cathepsin G activity in microglia-derived lysosomes and controls the proteolytic processing of myelin basic protein in vitro. Immunology 2007;121:82-93.
  56. Zou F, Lai X, Li J, Lei S, Hu L. Downregulation of cathepsin G reduces the activation of CD4+ T cells in murine autoimmune diabetes. Am J Transl Res 2017;9:5127-37.
  57. Trabandt A, Gay RE, Fassbender HG, Gay S. Cathepsin B in synovial cells at the site of joint destruction in rheumatoid arthritis. Arthritis Rheum 1991;34:1444-51.
  58. Ikeda Y, Ikata T, Mishiro T, Nakano S, Ikebe M, Yasuoka S. Cathepsins B and L in synovial fluids from patients with rheumatoid arthritis and the effect of cathepsin B on the activation of pro-urokinase. J Med Invest 2000;47:61-75.
  59. Van Noorden CJ, Smith RE, Rasnick D. Cysteine proteinase activity in arthritic rat knee joints and the effects of a selective systemic inhibitor, Z-Phe- AlaCH2F. J Rheumatol 1988;15:1525-35.
  60. Peltonen L, Puranen J, Lehtinen K, Korhonen LK. Proteolytic enzymes in joint destruction. Scand J Rheumatol 1981;10:107-14.
  61. Hou WS, Li W, Keyszer G, Weber E, Levy R, Klein MJ, et al. Comparison of cathepsins K and S expression within the rheumatoid and osteoarthritic synovium. Arthritis Rheum 2002;46:663-74.
  62. Skoumal M, Haberhauer G, Kolarz G, Hawa G, Woloszczuk W, Klingler A. Serum cathepsin K levels of patients with longstanding rheumatoid arthritis: correlation with radiological destruction. Arthritis Res Ther 2005;7:R65-70.
  63. Cunnane G, FitzGerald O, Hummel KM, Youssef PP, Gay RE, Gay S, et al. Synovial tissue protease gene expression and joint erosions in early rheumatoid arthritis. Arthritis Rheum 2001;44:1744-53.
  64. Weitoft T, Larsson A, Manivel VA, Lysholm J, Knight A, Rönnelid J. Cathepsin S and cathepsin L in serum and synovial fluid in rheumatoid arthritis with and without autoantibodies. Rheumatology (Oxford) 2015;54:1923-8.
  65. Phi NC, Chien DK, Binh VV, Gergely P. Cathepsin D-like activity in serum of patients with systemic lupus erythematosus. J Clin Lab Immunol 1989;29:185-8.
  66. Rupanagudi KV, Kulkarni OP, Lichtnekert J, Darisipudi MN, Mulay SR, Schott B, et al. Cathepsin S inhibition suppresses systemic lupus erythematosus and lupus nephritis because cathepsin S is essential for MHC class II-mediated CD4 T cell and B cell priming. Ann Rheum Dis 2015;74:452-63.
  67. Steinfeld S, Maho A, Chaboteaux C, Daelemans P, Pochet R, Appelboom T, et al. Prolactin up-regulates cathepsin B and D expression in minor salivary glands of patients with Sjögren’s syndrome. Lab Invest 2000;80:1711-20.
  68. Hamm-Alvarez SF, Janga SR, Edman MC, Madrigal S, Shah M, Frousiakis SE, et al. Tear cathepsin S as a candidate biomarker for Sjögren’s syndrome. Arthritis Rheumatol 2014;66:1872-81.
  69. Saegusa K, Ishimaru N, Yanagi K, Arakaki R, Ogawa K, Saito I, et al. Cathepsin S inhibitor prevents autoantigen presentation and autoimmunity. J Clin Invest 2002;110:361-9.
  70. Neidhart M, Baraliakos X, Seemayer C, Zelder C, Gay RE, Michel BA, et al. Expression of cathepsin K and matrix metalloproteinase 1 indicate persistent osteodestructive activity in long-standing ankylosing spondylitis. Ann Rheum Dis 2009;68:1334-9.
  71. Bever CT Jr, Panitch HS, Johnson KP. Increased cathepsin B activity in peripheral blood mononuclear cells of multiple sclerosis patients. Neurology 1994;44:745-8.
  72. Bever CT Jr, Garver DW. Increased cathepsin B activity in multiple sclerosis brain. J Neurol Sci 1995;131:71-3.
  73. Martino S, Montesano S, di Girolamo I, Tiribuzi R, Di Gregorio M, Orlacchio A, et al. Expression of cathepsins S and D signals a distinctive biochemical trait in CD34+ hematopoietic stem cells of relapsing- remitting multiple sclerosis patients. Mult Scler 2013;19:1443-53.
  74. Haves-Zburof D, Paperna T, Gour-Lavie A, Mandel I, Glass-Marmor L, Miller A. Cathepsins and their endogenous inhibitors cystatins: expression and modulation in multiple sclerosis. J Cell Mol Med 2011;15:2421-9.
  75. Shuja S, Cai J, Iacobuzio-Donahue C, Zacks J, Beazley RM, Kasznica JM, et al. Cathepsin B activity and protein levels in thyroid carcinoma, Graves’ disease, and multinodular goiters. Thyroid 1999;9:569-77.
  76. Yang H, Kala M, Scott BG, Goluszko E, Chapman HA, Christadoss P. Cathepsin S is required for murine autoimmune myasthenia gravis pathogenesis. J Immunol 2005;174:1729-37.
  77. Kosikowska P, Lesner A. Inhibitors of cathepsin G: a patent review (2005 to present). Expert Opin Ther Pat 2013;23:1611-24.