Advances in Clinical and Experimental Medicine
2018, vol. 27, nr 11, November, p. 1529–1534
doi: 10.17219/acem/70811
Publication type: original article
Language: English
Download citation:
Determination of the concentration of cathepsin B by SPRI biosensor in children with appendicitis, and its correlation with proteasomes
1 Department of Pediatric Surgery, Medical University of Bialystok, Poland
2 Department of Biophysics, Medical University of Bialystok, Poland
3 Department of Electrochemistry, Institute of Chemistry, University of Bialystok, Poland
Abstract
Background. Cathepsin B (CatB) belongs to a family of lysosomal cysteine proteases and plays an important role in intracellular proteolysis.
Objectives. The concentration of CatB and 20S proteasome was evaluated in the serum of children with appendicitis, before and after surgery, on a basis of an innovative method for determining biomolecules concentration – surface plasmon resonance imaging (SPRI) biosensor.
Material and Methods. Forty-two children with acute appendicitis, who were treated at the Department of Pediatric Surgery (Medical University of Bialystok, Poland), were randomly included into the study (age: 5–17 years, mean age: 11.5 ±1 year). There were 15 girls and 27 boys in the study group. Eighteen healthy, age-matched subjects, admitted for planned surgeries, served as controls. Exclusion criteria were the following: severe preexisting infections, immunological or cardiovascular diseases that required longterm medication, and complicated cases of appendicitis with perforation of the appendix and/or peritonitis.
Results. The CatB concentrations in the blood plasma of patients with acute appendicitis were elevated before surgery, they were the highest 24 h after surgery, and were above the range of concentrations measured in controls; the difference was statistically significant. The CatB concentration measured 72 h after the operation was decreased, but still did not reach the normal range when compared with the concentration measured in controls (p < 0.05).
Conclusion. Cathepsin B concentration may reflect the metabolic response to acute state of inflammation, surgical intervention in the abdominal cavity and the process of gradual ebbing of the inflammation. The method of operation – classic open appendectomy or laparoscopic appendectomy – does not influence the general trend in the CatB concentration in children with appendicitis. There is a strong positive correlation between the CatB and 20S proteasome concentrations 24 h after surgery. The SPRI method can be successfully used for determining the concentration of active forms of enzymes presented in lysosomes in the diagnosis of inflammatory conditions in the abdominal cavity.
Key words
appendicitis, inflammation, proteasomes, cathepsin B, surface plasmon resonance imaging biosensor
References (43)
- Benchoua A, Braudeau J, Reis A, Couriaud C, Onténiente B. Activation of proinflammatory caspases by cathepsin B in focal cerebral ischemia. J Cereb Blood Flow Metab. 2004;24(11):1272–1279.
- Uchiyama Y. Autophagic cell death and its execution by lysosomal cathepsins. Arch Histol Cytol. 2001;64(3):233–246.
- Boya P, Andreau K, Poncet D, et al. Lysosomal membrane permeabilization induces cell death in a mitochondrion-dependent fashion. J Exp Med. 2003;197(10):1323–1334.
- Li X, Wu Z, Ni J, et al. Cathepsin B regulates collagen expression by fibroblasts via prolonging TLR2/NF-κB activation. Oxid Med Cell Longev. 2016:7894247. doi: 10.1155/2016/7894247
- Foghsgaard L, Wissing D, Mauch D, et al. Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor. J Cell Biol. 2001;153(5):999–1010.
- Terada K, Yamada J, Hayashi Y, et al. Involvement of cathepsin B in the processing and secretion of interleukin-1β in chromogranin a-stimulated microglia. Glia. 2010;58(1):114–124.
- Sun L, Wu Z, Hayashi Y, et al. Microglial cathepsin B contributes to the initiation of peripheral inflammation-induced chronic pain. J Neurosci. 2012;32(33):11330–11342.
- Wu Z, Sun L, Hashioka S, et al. Differential pathways for interleukin-1β production activated by chromogranin A and amyloid β in microglia. Neurobiol Aging. 2013;34(12):2715–2725.
- Dinarello CA. Biologic basis for interleukin-1 in disease. Blood. 1996; 87(6):2095–2147.
- Hornung V, Bauernfeind F, Halle A, Samstad EO, Kono H, Rock KL. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat Immunol. 2008;9(8):847–856.
- Halle A, Hornung V, Petzold GC, Stewart CR, Monks BG, Reinheckel T. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol. 2008;9(8):857–865.
- Geraghty P, Rogan MP, Greene CM, et al. Neutrophil elastase up-regulates cathepsin B and matrix metalloprotease-2 expression. J Immunol. 2007;178(9):5871–5878.
- Ito WD, Lund N, Zhang Z, et al. Activation of cell surface bound 20S proteasome inhibits vascular cell growth and arteriogenesis. Biomed Res Int. 2015:719316. doi: 10.1155/2015/719316
- Dieudé M, Bell C, Turgeon J, et al. The 20S proteasome core, active within apoptotic exosome-like vesicles, induces autoantibody production and accelerates rejection. Sci Transl Med. 2015;7(318):318–200. doi: 10.1126/scitranslmed.aac9816
- Majetschak M, Perez M, Sorell LT, Lam J, Maldonado ME, Hoffman RW. Circulating 20S proteasome levels in patients with mixed connective tissue disease and systemic lupus erythematosus. Clin Vaccine Immunol. 2008;15(9):1489–1493.
- Henry L, Lavabre-Bertrand T, Douche T, et al. Diagnostic value and prognostic significance of plasmatic proteasome level in patients with melanoma. Exp Dermatol. 2010;19:1054–1059.
- Jakob C, Egerer K, Liebisch P, et al. Circulating proteasome levels are an independent prognostic factor for survival in multiple myeloma. Blood. 2007;109(5):2100–2105.
- Matuszczak E, Tylicka M, Dębek W, Hermanowicz A, Ostrowska H. The comparison of C-proteasome activity in the plasma of children after burn injury, mild head injury and blunt abdominal trauma. Adv Med Sci. 2015;60(2):253–258.
- Tylicka M, Matuszczak E, Dębek W, Hermanowicz A, Ostrowska H. Circulating proteasome activity following mild head injury in children. Childs Nerv Syst. 2014;30(7):1191–1196.
- Matuszczak E, Tylicka M, Dębek W, Hermanowicz A, Ostrowska H. Correlation between circulating proteasome activity, total protein and c-reactive protein levels following burn in children. Burns. 2014;40(5): 842–847.
- Sixt SU, Dahlmann B. Extracellular, circulating proteasomes and ubiquitin − incidence and relevance. Biochim Biophys Acta. 2008;1782(12):817–823.
- Sankiewicz A, Laudański P, Romanowicz L, et al. Development of surface plasmon resonance imaging biosensors for detection of ubiquitin carboxyl-terminal hydrolase L1. Anal Biochem. 2015;469:4–11.
- Gorodkiewicz E. Surface plasmon resonance imaging sensor for cathepsin determination based in immobilized cystatin. Protein Pept Lett. 2009;16(11):1379–1385.
- Gorodkiewicz E, Sieńczyk M, Regulska E, et al. Surface plasmon resonance imaging biosensor for cathepsin G based on a potent inhibitor: Development and applications. Anal Bochem. 2012;423:218–223.
- Gorodkiewicz E, Sankiewicz A, Laudański P. Surface plasmon resonance imaging biosensors for aromatase based on a potent inhibitor and a specific antibody: Sensor development and application for biological material. Cent Eur J Chem. 2014;12(5):557–567.
- Johnsson B, Lofas S, Lindquist G. Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal Biochem. 1991;198:268–277.
- Jeschke MG, Gauglitz GG, Kulp GA, et al. Long-term persistance of the pathophysiologic response to severe burn injury. PLoS ONE. 2011;6(7): e21245. doi: 10.1371/journal.pone.0021245
- Porter C, Herndon DN, Sidossis LS, et al. The impact of severe burns on skeletal muscle mitochondrial function. Burns. 2013;39(6):1039–1047.
- Sun L, Wu Z, Hayashi Y, et al. Microglial cathepsin B contributes to the initiation of peripheral inflammation-induced chronic pain. J Neurosci. 2012;32(33):11330–11342.
- Hook G, Jacobsen JS, Grabstein K, Kindy M, Hook V. Cathepsin B is a new drug target for traumatic brain injury therapeutics: Evidence for E64d as a promising lead drug candidate. Front Neurol. 2015;6:178. doi: 10.3389/fneur.2015.00178
- Assfalg-Machleidt I, Jochum M, Nast-Kolb D, et al. Cathepsin B-indicator for the release of lysosomal cysteine proteinases in severe trauma and inflammation. Biol Chem Hoppe Seyler. 1990;371(Suppl):211–222.
- Jochum M, Machleidt W, Fritz H. Phagocyte proteinases in multiple trauma and sepsis: Pathomechanisms and related therapeutic approaches. In: Neugebauer EA, Holaday JW, eds. Handbook of Mediators in Septic Shock. Boca Raton, FL: CRC Press; 1993:335–361.
- Canbay A, Guicciardi ME, Higuchi H, et al. Cathepsin B inactivation attenuates hepatic injury and fibrosis during cholestasis. J Clin Invest. 2003;112(2):152–159.
- Gondi CS, Rao JS. Cathepsin B as a cancer target. Expert Opin Ther Targets. 2013;17(3):281–291.
- Palermo C, Joyce JA. Cysteine cathepsin proteases as pharmacological targets in cancer. Trends Pharmacol Sci. 2008;29(1):22–28.
- Kos J, Mitrovic A, Mirkovic B. The current stage of cathepsin B inhibitors as potential anticancer agents. Future Med Chem. 2014;6(11):1355–1371.
- Cha IS, Kwon J, Mun JY, et al. Cathepsins in the kidney of olive flounder, Paralichthys olivaceus, and their responses to bacterial infection. Dev Comp Immunol. 2012;38(4):538–544.
- Canbay A, Feldstein AE, Higuchi H, et al. Kupffer cell engulfment of apoptotic bodies stimulates death ligand and cytokine expression. Hepatology. 2003;38(5):1188–1198.
- Cunnane G, Fitzgerald O, Beeton C, Cawston TE, Bresnihan B. Early joint erosions and serum levels of matrix metalloproteinase 1, matrix metalloproteinase 3, and tissue inhibitor of metalloproteinases 1 in rheumatoid arthritis. Arthritis Rheum. 2001;44(10):2263–2274.
- Mishiro T, Nakano S, Takahara S, et al. Relationship between cathepsin B and thrombin in rheumatoid arthritis. J Rheumatol. 2004;31(7): 1265–1273.
- Baici A, Müntener K, Willimann A, Zwicky R. Regulation of human cathepsin B by alternative mRNA splicing: Homeostasis, fatal errors and cell death. Biol Chem. 2006;387(8):1017–1021.
- Feng Y, Ni L, Wang Q. Administration of cathepsin B inhibitor CA-074Me reduces inflammation and apoptosis in polymyositis. J Dermatol Sci. 2013;72(2):158–167.
- Bien S, Ritter CA, Gratz M, et al. Nuclear factor-κB mediates up-regulation of cathepsin B by doxorubicin in tumor cells. Mol Pharmacol. 2004;65(5):1092–1102.