Chitinases: Therapeutic Scaffolds for Allergy and Inflammation

Author(s): Kirtika Madan, Mansi Madan, Swapnil Sharma*, Sarvesh Paliwal

Journal Name: Recent Patents on Inflammation & Allergy Drug Discovery (Discontinued)

Volume 14 , Issue 1 , 2020

Abstract:

Background: Chitinases are the evolutionary conserved glycosidic enzymes that are characterized by their ability to cleave the naturally abundant polysaccharide chitin. The potential role of chitinases has been identified in the manifestation of various allergies and inflammatory diseases. In recent years, chitinases inhibitors are emerging as an alluring area of interest for the researchers and scientists and there is a dire need for the development of potential and safe chitinase antagonists for the prophylaxis and treatment of several diseases.

Objective: The present review expedites the role of chitinases and their inhibitors in inflammation and related disorders.

Methods: At first, an exhaustive survey of literature and various patents available related to chitinases were carried out. Useful information on chitinases and their inhibitor was gathered from the authentic scientific databases namely SCOPUS, EMBASE, PUBMED, GOOGLE SCHOLAR, MEDLINE, EMBASE, EBSCO, WEB OF SCIENCE, etc. This information was further analyzed and compiled up to prepare the framework of the review article. The search strategy was conducted by using queries with key terms “ chitin”, “chitinase”, “chitotrisidase”, “acidic mammalian chitinase”, “chitinase inhibitors”, “asthma” and “chitinases associated inflammatory disorders”, etc. The patents were searched using the key terms “chitinases and uses thereof”, “chitinase inhibitors”, “chitin-chitinase associated pathological disorders” etc. from www.google.com/patents, www.freepatentsonline.com, and www.scopus.com.

Results: The present review provides a vision for apprehending human chitinases and their participation in several diseases. The patents available also signify the extended role and effectiveness of chitinase inhibitors in the prevention and treatment of various diseases viz. asthma, acute and chronic inflammatory diseases, autoimmune diseases, dental diseases, neurologic diseases, metabolic diseases, liver diseases, polycystic ovary syndrome, endometriosis, and cancer. In this regard, extensive pre-clinical and clinical investigations are required to develop some novel, potent and selective drug molecules for the treatment of various inflammatory diseases, allergies and cancers in the foreseeable future.

Conclusion: In conclusion, chitinases can be used as potential biomarkers in prognosis and diagnosis of several inflammatory diseases and allergies and the design of novel chitinase inhibitors may act as key and rational scaffolds in designing some novel therapeutic agents in the treatment of variety of inflammatory diseases.

Keywords: Acidic Mammalian Chitinases (AMCase), allergy, allosamidin (Allo), chitinases, chitotriosidase (CHIT1), inflammatory disorders.

[1]
Henrissat B, Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 1993; 293(Pt 3): 781-8.
[http://dx.doi.org/10.1042/bj2930781] [PMID: 8352747 ]
[2]
Hamid R, Khan MA, Ahmad M, Ahmad MM, Abdin MZ, Musarrat J, et al. Chitinases: An update. J Pharm Bioallied Sci 2013; 5(1): 21-9.
[http://dx.doi.org/10.4103/0975-7406.106559] [PMID: 23559820]
[3]
Barikani M, Oliaei E, Siddiqi H, Honarkar H. Preparation and application of chitin and its derivatives: A review. Iran Polym J 2014; 23: 307-26.
[http://dx.doi.org/10.1007/s13726-014-0225-z]
[4]
Anitha A. Chitin and chitosan in selective biomedical applications. Prog Polym Sci 2014; 39: 1644-67.
[http://dx.doi.org/10.1016/j.progpolymsci.2014.02.008]
[5]
Solairaj D, Rameshthangam P, Muthukumaran P, Wilson J. Studies on electrochemical glucose sensing, antimicrobial activity and cytotoxicity of fabricated copper nanoparticle immobilized chitin nanostructure. Int J Biol Macromol 2017; 101: 668-79.
[http://dx.doi.org/10.1016/j.ijbiomac.2017.03.147] [PMID: 28363648 ]
[6]
Tang WJ, Fernandez J, Sohn JJ, Amemiya CT. Chitin is endogenously produced in vertebrates. Curr Biol 2015; 25(7): 897-900.
[http://dx.doi.org/10.1016/j.cub.2015.01.058] [PMID: 25772447 ]
[7]
Di Rosa M, Distefano G, Zorena K, Malaguarnera L. Chitinases and immunity: Ancestral molecules with new functions. Immunobiology 2016; 221(3): 399-411.
[http://dx.doi.org/10.1016/j.imbio.2015.11.014] [PMID: 26686909 ]
[8]
Adrangi S, Faramarzi MA. From bacteria to human: A journey into the world of chitinases. Biotechnol Adv 2013; 31(8): 1786-95.
[http://dx.doi.org/10.1016/j.biotechadv.2013.09.012] [PMID: 24095741 ]
[9]
Gooday GW. Aggressive and defensive roles for chitinases. EXS 1999; 87: 157-69.
[PMID: 10906958]
[10]
Nagpure A, Choudhary B, Gupta RK. Chitinases: In agriculture and human healthcare. Crit Rev Biotechnol 2014; 34(3): 215-32.
[http://dx.doi.org/10.3109/07388551.2013.790874] [PMID: 23859124 ]
[11]
Lee CG, Da Silva CA, Dela Cruz CS, Ahangari F, Ma B, Elias JA, et al. Role of chitin and chitinase/chitinase-like proteins in inflammation, tissue remodeling, and injury. Annu Rev Physiol 2011; 73: 479-501.
[http://dx.doi.org/10.1146/annurev-physiol-012110-142250] [PMID: 21054166]
[12]
Paoletti MG, Norberto L, Damini R, Musumeci S. Human gastric juice contains chitinase that can degrade chitin. Ann Nutr Metab 2007; 51(3): 244-51.
[http://dx.doi.org/10.1159/000104144] [PMID: 17587796 ]
[13]
Renkema GH, Boot RG, Muijsers AO, Donker-Koopman WE, Aerts JM. Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins. J Biol Chem 1995; 270(5): 2198-202.
[http://dx.doi.org/10.1074/jbc.270.5.2198] [PMID: 7836450 ]
[14]
Escott GM, Adams DJ. Chitinase activity in human serum and leukocytes. Infect Immun 1995; 63(12): 4770-3.
[http://dx.doi.org/10.1128/IAI.63.12.4770-4773.1995] [PMID: 7591134]
[15]
Hakala BE, White C, Recklies AD. Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family. J Biol Chem 1993; 268(34): 25803-10.
[PMID: 8245017]
[16]
Kuddus M, Ahmad IZ. Isolation of novel chitinolytic bacteria and production optimization of extracellular chitinase. J Genet Eng Biotechnol 2013; 11: 39-46.
[http://dx.doi.org/10.1016/j.jgeb.2013.03.001]
[17]
Rathore AS, Gupta RD. Chitinases from bacteria to human: Properties, applications and future perspectives. Enzyme Res 2015; 2015 791907
[http://dx.doi.org/10.1155/2015/791907] [PMID: 26664744]
[18]
Kim D-H, Park H-J, Lim S, Lee H-G, Choi JO, Oh JH, et al. Regulation of chitinase-3-like-1 in T cell elicites Th1 nad cytotoxic responses to inhibit lung metastasis. Nat Commun 2018; 9(503): 1-14.
[19]
Kidibule PE, Sanlos-Moriano P, Jimimez-Ortego E, Rmiriz-Escudero M, Limon MC, Rimacha M, et al. Use of chitin and chitosan to produce new chitooligosaccharides by chitinase Chit42: Enzymatic activity and structural basis of protein specificity. Microb Cell Fact 2018; 17(1): 47.
[http://dx.doi.org/10.1186/s12934-018-0895-x] [PMID: 29566690]
[20]
Shibata Y, Metzger WJ, Myrvik QN. Chitin particle-induced cell-mediated immunity is inhibited by soluble mannan: Mannose receptor-mediated phagocytosis initiates IL-12 production. J Immunol 1997; 159(5): 2462-7.
[PMID: 9278339]
[21]
Synstad B, Gåseidnes S, Van Aalten DM, Vriend G, Nielsen JE, Eijsink VG. Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase. Eur J Biochem 2004; 271(2): 253-62.
[http://dx.doi.org/10.1046/j.1432-1033.2003.03923.x] [PMID: 14717693 ]
[22]
Dahiya N, Tewari R, Hoondal GS. Biotechnological aspects of chitinolytic enzymes: A review. Appl Microbiol Biotechnol 2006; 71(6): 773-82.
[http://dx.doi.org/10.1007/s00253-005-0183-7] [PMID: 16249876 ]
[23]
Stoykov YM, Pavlo AI, Krastanov AI. Chitinase biotechnology: Production, purification and application. Eng Life Sci 2015; 15(1): 30-8.
[http://dx.doi.org/10.1002/elsc.201400173]
[24]
Kabir SR, Rehman MM, Tasnim S, Karim MR, Khatun N, Hasan I, et al. Purification and characterization of a novel chitinase from Trichosanthes dioica seed with antifungal activity. Int J Biol Macromol 2016; 84: 62-8.
[http://dx.doi.org/10.1016/j.ijbiomac.2015.12.006] [PMID: 26666429 ]
[25]
Vega K, Kalkum M. Chitin, chitinase responses, and invasive fungal infections. Int J Microbiol 2012; 2012 920459
[http://dx.doi.org/10.1155/2012/920459] [PMID: 22187561]
[26]
Roopavathy AS, Vigneshwari R, Jayapradha R. Chitinase production and applicatons. J Chem Pharm Res 2015; 7(5): 924-31.
[27]
Bussink AP, Speijer D, Aerts JM, Boot RG. Evolution of mammalian chitinase(-like) members of family 18 glycosyl hydrolases. Genetics 2007; 177(2): 959-70.
[http://dx.doi.org/10.1534/genetics.107.075846] [PMID: 17720922]
[28]
Elias JA, Homer RJ, Hamid Q, Lee CG. Chitinases and chitinase-like proteins in T(H)2 inflammation and asthma. J Allergy Clin Immunol 2005; 116(3): 497-500.
[http://dx.doi.org/10.1016/j.jaci.2005.06.028] [PMID: 16159614 ]
[29]
Rameshthangam P, Solairaj D, Arunachalam G, Ramasamy P. Chitin and chitinases: Biomedical and environmental applications of chitin and its derivatives. J Enz 2018; 1(1): 20-43.
[30]
Ober C, Chupp GL. The chitinase and chitinase-like proteins: A review of genetic and functional studies in asthma and immune-mediated diseases. Curr Opin Allergy Clin Immunol 2009; 9(5): 401-8.
[http://dx.doi.org/10.1097/ACI.0b013e3283306533] [PMID: 19644363]
[31]
MacDonald JM, Tarling CA, Taylor EJ, Dennis RJ, Myers DS, Knapp S, et al. Chitinase inhibition by chitobiose and chitotriose thiazolines. Angew Chem Int Ed Engl 2010; 49(14): 2599-602.
[http://dx.doi.org/10.1002/anie.200906644] [PMID: 20209544 ]
[32]
Boot RG, Renkema GH, Verhoek M, Strijland A, Bliek J, de Meulemeester TM. The human chitotriosidase gene. Nature of inherited enzyme deficiency. J Biol Chem 1998; 273(40): 25680-5.
[http://dx.doi.org/10.1074/jbc.273.40.25680] [PMID: 9748235 ]
[33]
Hollak CE, van Weely S, van Oers MH, Aerts JM. Marked elevation of plasma chitotriosidase activity. A novel hallmark of Gaucher disease. J Clin Invest 1994; 93(3): 1288-92.
[http://dx.doi.org/10.1172/JCI117084] [PMID: 8132768]
[34]
Wiesner DL, Specht CA, Lee CK, Smith KD, Mukaremera L, Lee ST, et al. Chitin recognition via chitotriosidase promotes pathologic type-2 helper T cell responses to cryptococcal infection. PLoS Pathog 2015; 11(3) e1004701
[http://dx.doi.org/10.1371/journal.ppat.1004701] [PMID: 25764512 ]
[35]
Di Rosa M, Malaguarnera G, De Gregorio C, D’Amico F, Mazzarino MC, Malaguarnera L. Modulation of chitotriosidase during macrophage differentiation. Cell Biochem Biophys 2013; 66(2): 239-47.
[http://dx.doi.org/10.1007/s12013-012-9471-x] [PMID: 23152091 ]
[36]
Malaguarnera L, Di Rosa M, Zambito AM. dell’ Ombra N, Di Marco R, Malaguarnera M. Potential role of chitotriosidase gene in non alcoholic fatty liver disease evolution. Am J Gastroenterol 2006; 101: 2060-9.
[http://dx.doi.org/10.1111/j.1572-0241.2006.00680.x] [PMID: 16848812]
[37]
van Eijk M, Scheij SS, van Roomen CP, Speijer D, Boot RG, Aerts JM. TLR- and NOD2-dependent regulation of human phagocyte-specific chitotriosidase. FEBS Lett 2007; 581(28): 5389-95.
[http://dx.doi.org/10.1016/j.febslet.2007.10.039] [PMID: 17976376]
[38]
Malaguarnera L, Simporè J, Prodi DA, Angius A, Sassu A, Persico I, et al. A 24-bp duplication in exon 10 of human chitotriosidase gene from the sub-Saharan to the Mediterranean area: Role of parasitic diseases and environmental conditions. Genes Immun 2003; 4(8): 570-4.
[http://dx.doi.org/10.1038/sj.gene.6364025] [PMID: 14647197 ]
[39]
Kim KW, Park J, Lee JH, Lee HS, Lee J, Lee KH, et al. Association of genetic variation in chitotriosidase with atopy in Korean children. Ann Allergy Asthma Immunol 2013; 110(6): 444-449.e1.
[http://dx.doi.org/10.1016/j.anai.2013.03.009] [PMID: 23706714 ]
[40]
Di Rosa M, Mangano K, De Gregorio C, Nicoletti F, Malaguarnera L. Association of chitotriosidase genotype with the development of non-alcoholic fatty liver disease. Hepatol Res 2013; 43(3): 267-75.
[http://dx.doi.org/10.1111/j.1872-034X.2012.01063.x] [PMID: 22971072]
[41]
Artieda M, Cenarro A, Gañán A, Lukic A, Moreno E, Puzo J, et al. Serum chitotriosidase activity, a marker of activated macrophages, predicts new cardiovascular events independently of C-reactive protein. Cardiology 2007; 108(4): 297-306.
[http://dx.doi.org/10.1159/000099099] [PMID: 17290100 ]
[42]
Bargagli E, Margollicci M, Nikiforakis N, Luddi A, Perrone A, Grosso S, et al. Chitotriosidase activity in the serum of patients with sarcoidosis and pulmonary tuberculosis. Respiration 2007; 74(5): 548-52.
[http://dx.doi.org/10.1159/000100555] [PMID: 17347558 ]
[43]
Iyer A, van Eijk M, Silva E, Hatta M, Faber W, Aerts JM, et al. Increased chitotriosidase activity in serum of leprosy patients: Association with bacillary leprosy. Clin Immunol 2009; 131(3): 501-9.
[http://dx.doi.org/10.1016/j.clim.2009.02.003] [PMID: 19307157 ]
[44]
Sotgiu S, Barone R, Zanda B, Arru G, Fois ML, Arru A, et al. Chitotriosidase in patients with acute ischemic stroke. Eur Neurol 2005; 54(3): 149-53.
[http://dx.doi.org/10.1159/000089935] [PMID: 16319488 ]
[45]
Di Rosa M, Dell’Ombra N, Zambito AM, Malaguarnera M, Nicoletti F, Malaguarnera L. Chitotriosidase and inflammatory mediator levels in Alzheimer’s disease and cerebrovascular dementia. Eur J Neurosci 2006; 23(10): 2648-56.
[http://dx.doi.org/10.1111/j.1460-9568.2006.04780.x] [PMID: 16817867 ]
[46]
Ries M, Schaefer E, Lührs T, Mani L, Kuhn J, Vanier MT, et al. Critical assessment of chitotriosidase analysis in the rational laboratory diagnosis of children with Gaucher disease and Niemann-Pick disease type A/B and C. J Inherit Metab Dis 2006; 29(5): 647-52.
[http://dx.doi.org/10.1007/s10545-006-0363-3] [PMID: 16972172 ]
[47]
Barone R, Di Gregorio F, Romeo MA, Schilirò G, Pavone L. Plasma chitotriosidase activity in patients with beta-thalassemia. Blood Cells Mol Dis 1999; 25(1): 1-8.
[http://dx.doi.org/10.1006/bcmd.1999.0221] [PMID: 10349508 ]
[48]
Gavala ML, Kelly EA, Esnault S, Kukreja S, Evans MD, Bertics PJ, et al. Segmental allergen challenge enhances chitinase activity and levels of CCL18 in mild atopic asthma. Clin Exp Allergy 2013; 43(2): 187-97.
[http://dx.doi.org/10.1111/cea.12032] [PMID: 23331560]
[49]
Lee CG, Herzog EL, Ahangari F, Zhou Y, Gulati M, Lee CM, et al. Chitinase 1 is a biomarker for and therapeutic target in scleroderma-associated interstitial lung disease that augments TGF-β1 signaling. J Immunol 2012; 189(5): 2635-44.
[http://dx.doi.org/10.4049/jimmunol.1201115] [PMID: 22826322 ]
[50]
Boot RG, Blommaart EF, Swart E, Ghauharali-Vander Vlugt K. Bij lN, Moe C, et alIdentification of a novel acidic mammalian chitinase distinct from chitotriosidase. J Biol Chem 2001; 276(9): 6770-8.
[http://dx.doi.org/10.1074/jbc.M009886200] [PMID: 11085997]
[51]
Zhu Z, Zheng T, Homer RJ, Kim YK, Chen NY, Cohn L, et al. Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation. Science 2004; 304(5677): 1678-82.
[http://dx.doi.org/10.1126/science.1095336] [PMID: 15192232]
[52]
Chou YT, Yao S, Czerwinski R, Fleming M, Krykbaev R, Xuan D, et al. Kinetic characterization of recombinant human acidic mammalian chitinase. Biochemistry 2006; 45(14): 4444-54.
[http://dx.doi.org/10.1021/bi0525977] [PMID: 16584180]
[53]
Zimmermann N, Mishra A, King NE, Fulkerson PC, Doepker MP, Nikolaidis NM, et al. Transcript signatures in experimental asthma: Identification of STAT6-dependent and -independent pathways. J Immunol 2004; 172(3): 1815-24.
[http://dx.doi.org/10.4049/jimmunol.172.3.1815] [PMID: 14734765]
[54]
Di Rosa M, Brundo VM, Malaguarnera L. New insights on chitinases immunologic activities. World J Immunol 2016; 6(2): 96-104.
[http://dx.doi.org/10.5411/wji.v6.i2.96]
[55]
Refos JM, Vonk AG, Ten Kate MT, Verbrugh HA, Bakker-Woudenberg IAJM, van de Sande WWJ. Chitinase induction prior to caspofungin treatment of experimental invasive Aspergillosis in neuropenic rats does not chance survival. Antimicrob Agents Chemother 2017; 62(1): 1-11.
[http://dx.doi.org/10.1128/AAC.00960-17] [PMID: 29084744]
[56]
Matsumoto T, Inoue H, Sato Y, Kita Y, Nakano T, Noda N, et al. Demethylallosamidin, a chitinase inhibitor, suppresses airway inflammation and hyperresponsiveness. Biochem Biophys Res Commun 2009; 390(1): 103-8.
[http://dx.doi.org/10.1016/j.bbrc.2009.09.075] [PMID: 19782048 ]
[57]
Seibold MA, Reese TA, Choudhry S, Salam MT, Beckman K, Eng C, et al. Differential enzymatic activity of common haplotypic versions of the human acidic mammalian chitinase protein. J Biol Chem 2009; 284(29): 19650-8.
[http://dx.doi.org/10.1074/jbc.M109.012443] [PMID: 19435888 ]
[58]
Bierbaum S. Nicke lR, Koch A, Lau S, Deichmann KA, Wahn U, et al Polymorphisms and haplotypes of acid mammalian chitinase are associated with bronchial asthma. Am J Respir Crit Care Med 2005; 172(12): 1505-9.
[http://dx.doi.org/10.1164/rccm.200506-890OC] [PMID: 16179638 ]
[59]
Shahidi F, Abuzaytoun R. Chitin, chitosan, and co-products: Chemistry, production, applications, and health effects. Adv Food Nutr Res 2005; 49: 93-135.
[http://dx.doi.org/10.1016/S1043-4526(05)49003-8] [PMID: 15797344]
[60]
Sunazuka T, Hirose T, Omura S. Rapid Identification via in situ click chemistry of a novel chitinase inhibitor. J Synt Org Chem 2016; 74(11): 62-8.
[61]
Sakuda S, Isogai A, Matsumoto S, Suzuki A, Koseki K. Structure of allosamisin, a novel insect chitinase inhibitor, produced by Streptomyces sp. Tetrahedron Lett 1986; 27: 2475-8.
[http://dx.doi.org/10.1016/S0040-4039(00)84560-8]
[62]
Kuranda MJ, Robbins PW. Chitinase is required for cell separation during growth of Saccharomyces cerevisiae. J Biol Chem 1991; 266(29): 19758-67.
[PMID: 1918080]
[63]
Tsai YL, Hayward RE, Langer RC, Fidock DA, Vinetz JM. Disruption of Plasmodium falciparum chitinase markedly impairs parasite invasion of mosquito midgut. Infect Immun 2001; 69(6): 4048-54.
[http://dx.doi.org/10.1128/IAI.69.6.4048-4054.2001] [PMID: 11349075]
[64]
Berecibar A, Grandjean C, Siriwardena A. Synthesis and biological activity of natural amino cyclopentitol glycosidase inhibitors: Mannostatins, trehazolin, allosamidins and their analogues. Chem Rev 1999; 99(3): 779-844.
[http://dx.doi.org/10.1021/cr980033l] [PMID: 11749432 ]
[65]
Sakuda S. Studies on the chitinase inhibitors, allosamidins Chitin enzymology 1996. 2.
[66]
Andersen OA, Nathubhai A, Dixon MJ, Eggleston IM, van Aalten DM. Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin. Chem Biol 2008; 15(3): 295-301.
[http://dx.doi.org/10.1016/j.chembiol.2008.02.015] [PMID: 18355729]
[67]
Gooyit M, Tricoche N, Lustigman S, Janda KD. Dual protonophore-chitinase inhibitors dramatically affect O. volvulus molting. J Med Chem 2014; 57(13): 5792-9.
[http://dx.doi.org/10.1021/jm5006435] [PMID: 24918716 ]
[68]
Cho SJ, Weiden MD, Lee CG. Chitotriosidase in the pathogenesis of inflammation, intestinal lung diseases and COPD. Allergy Asthma Immunol Res 2015; 7(1): 14-21.
[http://dx.doi.org/10.4168/aair.2015.7.1.14] [PMID: 25553258 ]
[69]
Withers SG, MacDonald JM, Tarling CA, Taylor EJ, Dennis RJ, Myers DS, et al. Chitinase inhibition by chitobiose and chitotriose thiazolines. Angew Chem Int Ed 2010; 49: 2599-602.
[http://dx.doi.org/10.1002/anie.200906644]
[70]
Rao FV, Andersen OA, Vora KA, Demartino JA, van Aalten DM. Methylxanthine drugs are chitinase inhibitors: Investigation of inhibition and binding modes. Chem Biol 2005; 12(9): 973-80.
[http://dx.doi.org/10.1016/j.chembiol.2005.07.009] [PMID: 16183021 ]
[71]
Houston DR1,Synstad B, Eijsink VG, Stark MJ, Eggleston IM, van Aalten DM. Structure-based exploration of cyclic dipeptide chitinase inhibitors. J Med Chem 2004; 47: 5713-20.
[http://dx.doi.org/10.1021/jm049940a] [PMID: 15509170 ]
[72]
Van Aalten DM, Vasella A, Peter MG, Netter C, Houston DR, Westereng B, et al. Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-δ-lactone. J Biol Chem 2004; 279(5): 3612-9.
[http://dx.doi.org/10.1074/jbc.M310057200] [PMID: 14597613 ]
[73]
Mazur M, Koralewski R, Borek B, et al. Substituted amino triazoles useful as human chitinase inhibitors.US10208020 (2019).
[74]
Anderberg J, Gray J, McPherson P, Nakamura K, Kampf JP. Methods for evaluating renal injury and renal failure using urine levels of chitinase - 3 - like protein 1. US20190120858 (2019).
[75]
Bernard D, Berville MD. Cosmetic use of chitinase - type proteins.US9926587 (2018).
[76]
Richard L, Steven VD. Chitinase administration to the airway to treat inflammation and age-related pulmonary fibrosis.WO2018191379 (2018).
[77]
Sanfilippo S, Posteraro B, Sanguinetti M, et al. New macrocyclic amidinourea derivatives, methods of preparation and uses thereof as chtinase inhibitors. US20160137617 (2016).
[78]
Golebiowski AA, Koralewski R, Czestkowski W, et al. Matyszewski, K., Olejniczak, S., Olczak, J., Beckett, P. Substituted amino triazoles useful as human chitinase inhibitors. US2016176843 (2016)
[79]
Golebiowski AA, Koralewski R, Czestkowski W, et al. Matyszewski, K., Olejniczak, S., Olczak, J., Beckett, P. Substituted amino triazoles useful as acidic mammallian chitinase inhibitors. US20160368894 (2016).
[80]
Corman MM, Gollebiowski A, Beckett RP, Mazur M, Olezniczak S. Substituted amino triazoles, and methods using same. WO2015095701 (2015).
[81]
Reed JL, White W, Coyle A, et al. C/CLPantagonists and methods of use there of. US20110059100 (2011).
[82]
Vora KA, Demartino JA, Mudgett JS, Poster J, Wolfe G. Novel human acidic mammalian chitinase and use thereof.US20090191552 (2009).
[83]
Reed JL, White W, Coyle A, Kozhich A, Elias J. C/CLP antagonists and methods of use thereof. WO2007027748 (2007).
[84]
Olafur BE, Jon ME, Johannes G, Finnbogi T. Use of chitooligomer formulations to modify abnormal activity of chitinase like proteins. WO2006054319 (2006).
[85]
Maximillian TF. Inhibitors of acidic mammalian chitinase as asthma therapeutics WO2004092404 (2004).
[86]
Elias J, Zhu Z. Methods, compositions and kits relating to chitinases and chitin like molecules and inflammatory disease. WO03009808 (2003).
[87]
Harman GE, Broadway RM, Tronsmom A, Lorito M, Hayes CK, Pietr AD. Purified chitinases and use thereof. US6251390 (2001).
[88]
Levitz SM. Innate recognition of fungal cell walls. PLoS Pathog 2010; 6(4) e1000758
[http://dx.doi.org/10.1371/journal.ppat.1000758] [PMID: 20421940 ]
[89]
Edwards DRV, Gallins P, Polk M, Ayala-Haedo J, Schwartz SG, Kovach JL, et al. Inverse association of female hormone replacement therapy with age-related macular degeneration and interactions with ARMS2 polymorphisms. Invest Ophthalmol Vis Sci 2010; 51(4): 1873-9.
[http://dx.doi.org/10.1167/iovs.09-4000] [PMID: 19933179]
[90]
Koller B, Müller-Wiefel AS, Rupec R, Korting HC, Ruzicka T. Chitin modulates innate immune responses of keratinocytes. PLoS One 2011; 6(2) e16594
[http://dx.doi.org/10.1371/journal.pone.0016594] [PMID: 21383982 ]
[91]
Mack I, Hector A, Ballbach M. Kohlhäuf lJ, FuchsKJ, Weber A, etal.The role of chitin, chitinases, and chitinase-like proteins in pediatric lung diseases. Mol Cell Pediatr 2015; 2(3): 1-8.
[92]
Shuhui L, Mok YK, Wong WSF. Role of mammalian chitinases in asthma. Int Arch Allergy Immunol 2009; 149(4): 369-77.
[http://dx.doi.org/10.1159/000205583] [PMID: 19295241 ]
[93]
Coffman FD. Chitinase 3-Like-1 (CHI3L1): A putative disease marker at the interface of proteomics and glycomics. Crit Rev Clin Lab Sci 2008; 45(6): 531-62.
[http://dx.doi.org/10.1080/10408360802334743] [PMID: 19003601 ]
[94]
Kzhyshkowska J, Yin S, Liu T, Riabov V, Mitrofanova I. Role of chitinase-like proteins in cancer. Biol Chem 2016; 397(3): 231-47.
[http://dx.doi.org/10.1515/hsz-2015-0269] [PMID: 26733160 ]
[95]
Patel S, Goyal A. Chitin and chitinase: Role in pathogenicity, allergenicity and health. Int J Biol Macromol 2017; 97: 331-8.
[http://dx.doi.org/10.1016/j.ijbiomac.2017.01.042] [PMID: 28093332]
[96]
Moreira MF, dos Santos AS, Marotta HR, Mansur JF, Ramos IB, Machado EA, et al. A chitin-like component in Aedes aegypti eggshells, eggs and ovaries. Insect Biochem Mol Biol 2007; 37(12): 1249-61.
[http://dx.doi.org/10.1016/j.ibmb.2007.07.017] [PMID: 17967344 ]
[97]
Blokesch M. Chitin colonization, chitin degradation and chitin-induced natural competence of Vibrio cholerae are subject to catabolite repression. Environ Microbiol 2012; 14(8): 1898-912.
[http://dx.doi.org/10.1111/j.1462-2920.2011.02689.x] [PMID: 22222000]
[98]
Iqbal RK, Anwar FN. Chitinases potential as biocontrol. Biomed J Sci Tech Res 2019; 14(5): 10994-1001.
[99]
Gomma EZ. Chitinase production by Bacillus thuringiensis and Bacillus licheniformis: Their potential in antifungal biocontrol. J Microbiol 2012; 50: 103-11.
[100]
Sinha M, Singh RP, Kushwaha GS, Iqbal N, Singh A, Kaushik S, et al. Current overview of allergens of plant pathogenesis related protein families. ScientificWorldJournal 2014; 2014 543195
[http://dx.doi.org/10.1155/2014/543195] [PMID: 24696647 ]
[101]
Aranda A, Campo P, Palacin A, Do˜na I, Gomez-Casado C, Galindo L, et al. Antigenic proteins involved in occupational rhinitis and asthma caused by obeche wood (Triplochiton scleroxylon). PLoS One 2013; 8(1) e53926
[http://dx.doi.org/10.1371/journal.pone.0053926] [PMID: 23349765 ]
[102]
Jeebhay MF, Robins TG, Lehrer SB, Lopata AL. Occupational seafood allergy: A review. Occup Environ Med 2001; 58(9): 553-62.
[http://dx.doi.org/10.1136/oem.58.9.553] [PMID: 11511741 ]
[103]
Duru S, Yüceege M, Ardıç S. Chitinases and lung diseases. Tuberk Toraks 2013; 61(1): 71-5.
[http://dx.doi.org/10.5578/tt.3773] [PMID: 23581271 ]
[104]
Resch Y, Blatt K, Malkus U, Fercher C, Swoboda I, Lupinek C, et al. molecular, structural and immunological characterization of Derp18, a chitinase-like house dust mite allergen. PLoS One 2016; 11(8) e0160641
[http://dx.doi.org/10.1371/journal.pone.0160641] [PMID: 27548813 ]
[105]
Reese TA, Liang HE, Tager AM, Luster AD, Van Rooijen N, Voehringer D, et al. Chitin induces accumulation in tissue of innate immune cells associated with allergy. Nature 2007; 447(7140): 92-6.
[http://dx.doi.org/10.1038/nature05746] [PMID: 17450126 ]
[106]
Poddighe D, Mathias CB, Freyschmidt EJ, Kombe D, Caplan B, Marseglia GL, et al. Basophils are rapidly mobilized following initial aeroallergen encounter in naïve mice and provide a priming source of IL-4 in adaptive immune responses. J Biol Regul Homeost Agents 2014; 28(1): 91-103.
[PMID: 24750795 ]


open access plus

Rights & PermissionsPrintExport Cite as

Article Details

VOLUME: 14
ISSUE: 1
Year: 2020
Published on: 30 March, 2020
Page: [46 - 57]
Pages: 12
DOI: 10.2174/1872213X14666200114184054

Article Metrics

PDF: 28
HTML: 3