Abstract
Cells use proteases to accomplish a variety of cellular functions primarily through activation or deactivation of target proteins. An interruption in the balance between activation and deactivation is implicated in a growing list of human diseases. This chapter briefly covers the classification of the human proteases along with their involvement in diseases finally concluding with the idea of protease inhibitors as drugs and mention of related databases.
References
Barett AJ, McDonald JK (1986) Nomenclature: protease, proteinase and peptidase. Biochem J 237:935
Polgar L (ed) (1989) Metalloproteases. In: Mechanisms of protease action, pp. 208–210. CRC Press, Boca Ratan, FL
Menard R, Storer A (1992) Oxyanion hole interactions in serine and cysteine proteases. Hoppe-seyler’s Z Biol Chem 373:393–400
Hedstrom L (2002) Serine protease mechansm and specificity. Chem Rev 102:4501–4523
Puente XS, Lopez-Otin C (2004) A genomic analysis of rat proteases and protease inhibitors. Genome Res 14:609–622
Ramachandran R, Hollenberg MD (2008) Proteinases and signalling: pathophysiological and therapeutic implications via PARs and more. Br J Pharmacol 153(Suppl 1):S263–S282
Dodson G, Wlodawr A (1998) Catalytic triads and their relatives. Trends Biochem Sci 23:347–352
Blow DM (1971) The enzymes, 3rd edn, vol 3. Boyer PD (ed) Academic Press, Boca Raton
Sharony R, Yu P-J, Park J, Galloway AC, Mignatti P, Pintucci G (2010) Protein targets of inflammatory serine proteases and cardiovascular disease. J Inflam 7:45
Twigg MS, Brockbank S, Lowry P, FitzGerald SP, Taggart C, Weldon S (2015) The role of serine proteases and antiproteases in cystic fibrosis. Mediators Inflamm. Article ID: 293053
Zhou XW, Blackman MJ, Howell SA, Carruthers VB (2004) Proteomic analysis of cleavage events reveals a dynamic two-step mechanism for proteolysis of a key parasite adhesive complex. Mol Cell Proteomics 3:565–576
Romaris F, North SJ, Gagliardo LF, Butcher BA, Ghosh K, Beiting DP, Panico M, Arasu P, Dell A, Morris HR, Appleton JA (2002) A putative serine protease among the excretory-secretory glycoproteins of L1 Trichinella spiralis. Mol Biochem Parasitol 122:149–160
Wang B, Wang ZQ, Jin J, Ren HJ, Liu LN, Cui J (2013) Cloning, expression and characterization of a Trichinella spiralis serine protease gene encoding a 35.5 kDa protein. Exp Parasitol 134:148–154
Poole CB, Jin J, McReynolds LA (2003) Cloning and biochemical characterization of blisterase, a subtilisin-like convertase from the filarial parasite, Onchocerca volvulus. J Biol Chem 278:36183–36190
Rees-Roberts D, Mullen LM, Gounaris K, Selkirk ME (2010) Inactivation of the complement anaphylatoxin C5a by secreted products of parasitic nematodes. Int J Parasitol 40:527–532
Hotez PZ, Cerami A (1983) Secretion of a proteolytic anticoagulant by Ancylostoma hookworms. J Exp Med 157:1594–1603
Kong Y, Chung YB, Cho SY, Choi SH, Kang SY (1994) Characterization of three neutral proteases of Spirometra mansoni plerocercoid. Parasitology 108:359–368
Mohamed SA, Fahmy AS, Mohamed TM, Hamdy SM (2005) Proteases in egg, miracidium and adult of Fasciola gigantica. Characterization of serine and cysteine proteases from adult. Comp Biochem Physiol B Biochem Mol Biol 142:192–200
Steinmann P, Keiser J, Bos R, Tanner M, Utzinger J (2006) Schistosomiasis and water resources development: systematic review, meta-analysis, and estimates of people at risk. Lancet Infect Dis 6:411–425
Horn M, Fajtová P, Rojo Arreola L, Ulrychová L, Bartošová-Sojková P et al (2014) Trypsin- and chymotrypsin-like serine proteases in schistosoma mansoni—‘the undiscovered country’. PLoS Negl Trop Dis 8(3):e2766. doi:10.1371/journal.pntd.0002766
Alam A (2014) Serine proteases of malaria parasite Plasmodium falciparum: potential as antimalarial drug targets. Interdisc Perspect Infect Dis. doi:10.1155/2014/453186
Berti PJ, Storer AC (1995) Alignment/phylogeny of the papain superfamily of cysteine proteases. J Mol Biol 246:273–283
Thornberry N, Bull HG, Calaycay JR, Chapman KT, Howard AD et al (1992) A novel heterodimeric cysteine protease is required for inteleukin-1 beta processing in monocytes. Nature 356:768–774
Nuñez G, Benedict MA, Hu Y, Inohara N (1998) Caspases: the proteases of the apoptotic pathway. Oncogene 17:3237–3245
Turk V, Turk B, Turk D (2001) Lysosomal cysteine proteases: facts and opportunities. EMBO J 20:4629–4633
Cataldo AM, Hamilton DJ, Nixon RA (1994) Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer disease. Brain Res 640:68–80
Grynspan F, Griffin WR, Cataldo A, Katayama S, Nixon RA (1997) Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer’s disease. Brain Res 763:145–158
Yamashima T (2012) Hsp70.1 and related lysosomal factors for necrotic neuronal death. J Neurochem 120:477–494
Werle B, Kraft C, Lah TT, Kos J, Schanzenbächer U, Kayser K et al (2000) Cathepsin B in infiltrated lymph nodes is of prognostic significance for patients with nonsmall cell lung carcinoma. Cancer 89:2282–2291
Donnelly S, Dalton JP, Robinson MW (2011) How pathogen-derived cysteine proteases modulate host immune responses. Adv Exp Med Biol 712:192–207
Salas F, Fichmann J, Lee GK, Scott MD, Rosenthal PJ (1995) Functional expression of falcipain, a Plasmodium falciparum cysteine proteinase, supports its role as a malarial hemoglobinase. Infect Immun 63(6):2120–2125
O’Brien TC, Mackey ZB, Fetter RD, Choe Y, O’Donoghue AJ, Zhou M, Craik CS, Caffrey CR, McKerrow JH (2008) A parasite cysteine protease is key to host protein degradation and iron acquisition 24; 283(43): 28934–28943
Vincents B, Onnerfjord P, Gruca M, Potempa J, Abrahamson M (2007) Down-regulation of human extracellular cysteine protease inhibitors by the secreted staphylococcal cysteine proteases, staphopain A and B. Biol Chem 388:437–446
Shah PK (1997) Inflammation, metalloproteinases, and increased proteolysis—an emerging pathophysiological paradigm in aortic aneurysm. Circulation 96:2115–2117
Nagase H, Visse R, Murphy G (2006) Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 69:562–573
Skiles JW, Monovich LG, Jeng AY (2000) Matrix metalloproteinase inhibitor in the treatment of cancer. Annu Rep Med Chem 35:167–176
Newby AC (2005) Dual role of matrix metalloproteinases (matrixins) in intimal thickening and atherosclerotic plaque rupture. Physiol Rev 85:1–31
Arend WP, Dayer J-M (1995) Inhibition of the production and effects of interleukin-1 and tumor necrosis factor alpha in rheumatoid arthritis. Arthritis Rheum 38:151–160
Candelario-Jalil E, Yang Y, Rosenberg GA (2009) Diverse roles of matrix metalloproteinases and tissue inhibitors of metalloproteinases in neuroinflammation and cerebral ischemia. Neuroscience 158:983–994
Klein T, Bischoff R (2011) Physiology and pathophysiology of matrix metalloproteases. Amino Acids 41:271–290
Giraudon P, Buart S, Bernard A, Thomasset N, Belin MF (1996) Extracellular matrix-remodeling metalloproteinases and infection of the central nervous system with retrovirus human T-lymphotropic virus type I (HTLV-I). Prog Neurobiol 49:169–184
Eggleson KK, Duffin KL, Goldberg DE (1999) Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum. J Biol Chem 274:32411–32417
Laliberté J, Carruthers VB (2011) Toxoplasma gondii toxolysin 4 is an extensively processed putative metalloproteinase secreted from micronemes. Mol Biochem Parasitol 177:49–56
Elkington PTG, Emerson JE, Lopez-Pascua LDC et al (2005) Mycobacterium tuberculosis up-regulates matrix metalloproteinase-1 secretion from human airway epithelial cells via a p38 MAPK switch. J Immunol 175:5333–5340
Okamoto T, Akaike T, Suga M et al (1997) Activation of human matrix metalloproteinases by various bacterial proteinases. J Biol Chem 272:6059–6066
DeCarlo AA Jr, Windsor LJ, Bodden MK, Harber GJ, Birkedal-Hansen B, Birkedal-Hansen H (1997) Activation and novel processing of matrix metalloproteinases by a thiol-proteinase from the oral anaerobe Porphyromonas gingivalis. J Dent Res 76:1260–1270
Banerjee R, Liu J, Beatty W, Pelosof L, Klemba M, Goldberg DE (2002) Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine. Proc Natl Acad Sci U S A 99:990–995
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2017 Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Chakraborty, S., Basu, S. (2017). Proteases—The Sharp Scissors in Human Diseases. In: Chakraborti, S., Dhalla, N. (eds) Pathophysiological Aspects of Proteases. Springer, Singapore. https://doi.org/10.1007/978-981-10-6141-7_27
Download citation
DOI: https://doi.org/10.1007/978-981-10-6141-7_27
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-10-6140-0
Online ISBN: 978-981-10-6141-7
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)