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Journal articles on the topic 'Human Chitinase'

Author: Grafiati

Published: 14 March 2023

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1

Schimpl, Marianne, Christina L. Rush, Marie Betou, Ian M. Eggleston, Anneliese D. Recklies, and Daan M. F. van Aalten. "Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide-binding properties." Biochemical Journal 446, no. 1 (2012): 149–57. http://dx.doi.org/10.1042/bj20120377.

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The chitinase-like proteins YKL-39 (chitinase 3-like-2) and YKL-40 (chitinase 3-like-1) are highly expressed in a number of human cells independent of their origin (mesenchymal, epithelial or haemapoietic). Elevated serum levels of YKL-40 have been associated with a negative outcome in a number of diseases ranging from cancer to inflammation and asthma. YKL-39 expression has been associated with osteoarthritis. However, despite the reported association with disease, the physiological or pathological role of these proteins is still very poorly understood. Although YKL-39 is homologous to the tw

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2

Pinteac, Rucsanda, Xavier Montalban, and Manuel Comabella. "Chitinases and chitinase-like proteins as biomarkers in neurologic disorders." Neurology - Neuroimmunology Neuroinflammation 8, no. 1 (2020): e921. http://dx.doi.org/10.1212/nxi.0000000000000921.

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Chitinases are hydrolytic enzymes widely distributed in nature. Despite their physiologic and pathophysiologic roles are not well understood, chitinases are emerging as biomarkers in a broad range of neurologic disorders, where in many cases, protein levels measured in the CSF have been shown to correlate with disease activity and progression. In this review, we will summarize the structural features of human chitinases and chitinase-like proteins and their potential physiologic and pathologic functions in the CNS. We will also review existing evidence for the role of chitinases and chitinase-

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3

Madan, Kirtika, Mansi Madan, Swapnil Sharma, and Sarvesh Paliwal. "Chitinases: Therapeutic Scaffolds for Allergy and Inflammation." Recent Patents on Inflammation & Allergy Drug Discovery 14, no. 1 (2020): 46–57. http://dx.doi.org/10.2174/1872213x14666200114184054.

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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 ro

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4

Vega, Karina, Diana Diaz-Arevalo, Karine Bagramyan, Teresa Hong, and Markus Kalkum. "A positive feedback mechanism in the regulation of mammalian chitinase responses (56.29)." Journal of Immunology 186, no. 1_Supplement (2011): 56.29. http://dx.doi.org/10.4049/jimmunol.186.supp.56.29.

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Abstract Immunosuppressed patients are highly susceptible to invasive fungal infections (IFI) such as invasive pulmonary aspergillosis, which is predominantly caused by the fungus Aspergillus fumigatus. An important component of the fungal cell wall is chitin, a polymer of N-acetyl-D-glucosamine (GlcNAc). Chitin is not produced by humans, however, the chitin degrading enzymes (chitinases) chitotriosidase (Chit-1) and acidic mammalian chitinase (AMCase) are. Chitinase is predominantly produced by activated macrophages, and may possibly aid in the defense against chitin-containing pathogens. We

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Mazur, Marzena, Anna Zielińska, Marcin M. Grzybowski, Jacek Olczak, and Jakub Fichna. "Chitinases and Chitinase-Like Proteins as Therapeutic Targets in Inflammatory Diseases, with a Special Focus on Inflammatory Bowel Diseases." International Journal of Molecular Sciences 22, no. 13 (2021): 6966. http://dx.doi.org/10.3390/ijms22136966.

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Chitinases belong to the evolutionarily conserved glycosyl hydrolase family 18 (GH18). They catalyze degradation of chitin to N-acetylglucosamine by hydrolysis of the β-(1-4)-glycosidic bonds. Although mammals do not synthesize chitin, they possess two enzymatically active chitinases, i.e., chitotriosidase (CHIT1) and acidic mammalian chitinase (AMCase), as well as several chitinase-like proteins (YKL-40, YKL-39, oviductin, and stabilin-interacting protein). The latter lack enzymatic activity but still display oligosaccharides-binding ability. The physiologic functions of chitinases are still

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Dessens, Johannes T., Jacqui Mendoza, Charles Claudianos, et al. "Knockout of the Rodent Malaria Parasite Chitinase PbCHT1 Reduces Infectivity to Mosquitoes." Infection and Immunity 69, no. 6 (2001): 4041–47. http://dx.doi.org/10.1128/iai.69.6.4041-4047.2001.

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ABSTRACT During mosquito transmission, malaria ookinetes must cross a chitin-containing structure known as the peritrophic matrix (PM), which surrounds the infected blood meal in the mosquito midgut. In turn, ookinetes produce multiple chitinase activities presumably aimed at disrupting this physical barrier to allow ookinete invasion of the midgut epithelium. Plasmodium chitinase activities are demonstrated targets for human and avian malaria transmission blockade with the chitinase inhibitor allosamidin. Here, we identify and characterize the first chitinase gene of a rodent malaria parasite

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Suzuki, Masako, Wakako Fujimoto, Marie Goto, Masami Morimatsu, Bunei Syuto, and Toshihiko Iwanaga. "Cellular Expression of Gut Chitinase mRNA in the Gastrointestinal Tract of Mice and Chickens." Journal of Histochemistry & Cytochemistry 50, no. 8 (2002): 1081–89. http://dx.doi.org/10.1177/002215540205000810.

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Recently, the second mammalian chitinase, designated acidic mammalian chitinase (AMCase), has been identified in human, mouse, and cow. In contrast to the earlier identified macrophage-derived chitinase (chitotriosidase), this chitinase is richly expressed in the gastrointestinal (GI) tract, suggesting its role in digestion of chitin-containing foods as well as defense against chitin-coated microorganisms and parasites. This in situ hybridization study first revealed cellular localization of the gut-type chitinase in the mouse and chicken. In adult mice, the parotid gland, von Ebner's gland, a

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8

Tachu, Babila, Smitha Pillai, Richard Lucius, and Thomas Pogonka. "Essential Role of Chitinase in the Development of the Filarial Nematode Acanthocheilonema viteae." Infection and Immunity 76, no. 1 (2007): 221–28. http://dx.doi.org/10.1128/iai.00701-07.

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ABSTRACT Chitinases of pathogens have been proposed as potential targets of vaccines or specific inhibitors. We studied the genomic organization, transcript levels, developmental expression, and biological function of chitinases in the rodent filarial nematode Acanthocheilonema viteae, a model organism for human-pathogenic filarial worms. Characterization of nine genomic clones from an A. viteae phage library and Southern blot experiments revealed the existence of three different chitinase genes, two of which could theoretically yield functional transcripts. The deduced proteins of these genes

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9

Schlein, Y., and R. L. Jacobson. "Haemoglobin inhibits the development of infective promastigotes and chitinase secretion inLeishmania majorcultures." Parasitology 109, no. 1 (1994): 23–28. http://dx.doi.org/10.1017/s0031182000077726.

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SUMMARYHaemoglobin or blood in the growth medium ofLeishmania majorinhibited the formation of infective promastigotes and the secretion of chitinases. Inoculation of mice with stationary-phase parasites from control medium caused infections in 20/29 mice, compared to 3/20 mice injected with parasites grown with 10% rabbit blood, or 1/30 mice that received parasites grown with rabbit haemoglobin. The concentration of peanut lectin (PNA) required to agglutinate promastigotes was used as an index of their infectivity, ranging from a high concentration for infective populations to a low concentrat

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10

Fadel, Firas, Yuguang Zhao, Alexandra Cousido-Siah, Eduardo Howard, André Mitschler, and Alberto Podjarny. "Structural and mechanistic studies of human chitinase." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C445. http://dx.doi.org/10.1107/s2053273314095540.

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Chitinases are enzymes that hydrolyze chitin, a glucosamine polymer synthesized by lower organisms for structural purposes [1]. While humans do not synthetize chitin, they express two active chitinases, Chitotriosidase (hCHIT1) and Acidic Mammalian Chitinase (hAMCase). Both enzymes attracted attention due to their upregulation in immune system disorders [2,3]. They consist of a catalytic domain of 39 kDa and a chitin binding domain, joined by a hinge. The active site shows a cluster of three conserved acidic residues, E140, D138 and D136, linked by H-bonds, where D138 and E140 are involved in

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11

Vega, Karina, and Markus Kalkum. "Chitin, Chitinase Responses, and Invasive Fungal Infections." International Journal of Microbiology 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/920459.

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The human immune system is capable of recognizing and degrading chitin, an important cell wall component of pathogenic fungi. In the context of host-immune responses to fungal infections, herein we review the particular contributions and interplay of fungus and chitin recognition, and chitin-degrading enzymes, known as chitinases. The mechanisms of host chitinase responses may have implications for diagnostic assays as well as novel therapeutic approaches for patients that are at risk of contracting fatal fungal infections.

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12

Iershov, Anton, Konstantin Odynets, Alexander Kornelyuk, and Vadim Kavsan. "Homology modeling of 3D structure of human chitinase-like protein CHI3L2." Open Life Sciences 5, no. 4 (2010): 407–20. http://dx.doi.org/10.2478/s11535-010-0039-8.

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AbstractThe human genome encodes six proteins of family 18 glycosyl hydrolases, two active chitinases and four chitinase-like lectins (chi-lectins) lacking catalytic activity. The present article is dedicated to homology modeling of 3D structure of human chitinase 3-like 2 protein (CHI3L2), which is overexpressed in glial brain tumors, and its structural comparison with homologous chi-lectin CHI3L1. Two crystal structures of CHI3L1 in free state (Protein Data Bank codes 1HJX and 1NWR) were used as structural templates for the homology modeling by Modeller 9.7 program, and the best quality mode

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13

Rathore, Abhishek Singh, and Rinkoo D. Gupta. "Chitinases from Bacteria to Human: Properties, Applications, and Future Perspectives." Enzyme Research 2015 (November 19, 2015): 1–8. http://dx.doi.org/10.1155/2015/791907.

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Chitin is the second most plenteous polysaccharide in nature after cellulose, present in cell walls of several fungi, exoskeletons of insects, and crustacean shells. Chitin does not accumulate in the environment due to presence of bacterial chitinases, despite its abundance. These enzymes are able to degrade chitin present in the cell walls of fungi as well as the exoskeletons of insect. They have shown being the potential agents for biological control of the plant diseases caused by various pathogenic fungi and insect pests and thus can be used as an alternative to chemical pesticides. There

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Kzhyshkowska, Julia, Alexei Gratchev, and Sergij Goerdt. "Human Chitinases and Chitinase-Like Proteins as Indicators for Inflammation and Cancer." Biomarker Insights 2 (January 2007): 117727190700200. http://dx.doi.org/10.1177/117727190700200023.

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Human Glyco_18 domain-containing proteins constitute a family of chitinases and chitinase-like proteins. Chitotriosidase and AMCase are true enzymes which hydrolyse chitin and have a C-terminal chitin-binding domain. YKL-40, YKL-39, SI-CLP and murine YM1/2 proteins possess solely Glyco_18 domain and do not have the hydrolytic activity. The major sources of Glyco_18 containing proteins are macrophages, neutrophils, epithelial cells, chondrocytes, synovial cells, and cancer cells. Both macrophages and neutrophils use the regulated secretory mechanism for the release of Glyco_18 containing protei

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15

Chandra, Kasturi, Atish Roy Chowdhury, Ritika Chatterjee, and Dipshikha Chakravortty. "GH18 family glycoside hydrolase Chitinase A of Salmonella enhances virulence by facilitating invasion and modulating host immune responses." PLOS Pathogens 18, no. 4 (2022): e1010407. http://dx.doi.org/10.1371/journal.ppat.1010407.

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Salmonella is a facultative intracellular pathogen that has co-evolved with its host and has also developed various strategies to evade the host immune responses. Salmonella recruits an array of virulence factors to escape from host defense mechanisms. Previously chitinase A (chiA) was found to be upregulated in intracellular Salmonella. Although studies show that several structurally similar chitinases and chitin-binding proteins (CBP) of many human pathogens have a profound role in various aspects of pathogenesis, like adhesion, virulence, and immune evasion, the role of chitinase in the int

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16

HOUSTON, Douglas R., Ian EGGLESTON, Bj⊘rnar SYNSTAD, Vincent G. H. EIJSINK, and Daan M. F. van AALTEN. "The cyclic dipeptide CI-4 [cyclo-(l-Arg-d-Pro)] inhibits family 18 chitinases by structural mimicry of a reaction intermediate." Biochemical Journal 368, no. 1 (2002): 23–27. http://dx.doi.org/10.1042/bj20021034.

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Family 18 chitinases are attractive targets for the development of new inhibitors with chemotherapeutic potential against fungi, insects and protozoan/nematodal parasites. Although several inhibitors have been identified, these are based on complex chemistry, which hampers iterative structure-based optimization. Here we report the details of chitinase inhibition by the natural product peptide CI-4 [cyclo-(l-Arg-d-Pro)], which possesses activity against the human pathogenic fungus Candida albicans, and describe a 1.7Å (0.17nm) crystal structure of CI-4 in complex with the enzyme. The structure

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17

Marbán-González, Alberto, Armando Hernández-Mendoza, Mario Ordóñez, Rodrigo Said Razo-Hernández, and José Luis Viveros-Ceballos. "Discovery of Octahydroisoindolone as a Scaffold for the Selective Inhibition of Chitinase B1 from Aspergillus fumigatus: In Silico Drug Design Studies." Molecules 26, no. 24 (2021): 7606. http://dx.doi.org/10.3390/molecules26247606.

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Chitinases represent an alternative therapeutic target for opportunistic invasive mycosis since they are necessary for fungal cell wall remodeling. This study presents the design of new chitinase inhibitors from a known hydrolysis intermediate. Firstly, a bioinformatic analysis of Aspergillus fumigatus chitinase B1 (AfChiB1) and chitotriosidase (CHIT1) by length and conservation was done to obtain consensus sequences, and molecular homology models of fungi and human chitinases were built to determine their structural differences. We explored the octahydroisoindolone scaffold as a potential new

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18

Reichard, Utz, Chiung-Yu Hung, Pei W. Thomas, and Garry T. Cole. "Disruption of the Gene Which Encodes a Serodiagnostic Antigen and Chitinase of the Human Fungal PathogenCoccidioides immitis." Infection and Immunity 68, no. 10 (2000): 5830–38. http://dx.doi.org/10.1128/iai.68.10.5830-5838.2000.

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ABSTRACT Disruption of genes in medically important fungi has proved to be a powerful tool for evaluation of putative virulence factors and identification of potential protein targets for novel antifungal drugs. Chitinase has been suggested to play a pivotal role in autolysis of the parasitic cell wall of Coccidioides immitis during the asexual reproductive cycle (endosporulation) of this systemic pathogen. Two chitinase genes (CTS1 and CTS2) of C. immitis have been cloned. Preliminary evidence has suggested that expression of CTS1 is markedly increased during endospore formation. The secreted

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19

Escott, G. M., and D. J. Adams. "Chitinase activity in human serum and leukocytes." Infection and immunity 63, no. 12 (1995): 4770–73. http://dx.doi.org/10.1128/iai.63.12.4770-4773.1995.

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20

Gratchev, A. N., D. V. Samoilova, S. N. Kurochkin, and O. V. Kovaleva. "Development of a novel monoclonal antibody against chitinase-like protein YKL-39 applicable for immunohistochemistry." Russian Journal of Biotherapy 18, no. 2 (2019): 27–31. http://dx.doi.org/10.17650/1726-9784-2019-18-2-27-31.

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Introduction. Mammalian chitinase-like proteins are produced in the areas of inflammation and in tumors. Some members of chitinase-like proteins family are studied as potential biomarkers of tumors (glioma, prostate and ovary). YKL-39 also known as chitinase-3-like 2 (CHI3L2) is a secreted protein produced by chondrocytes. Its high expression is also found in synoviocytes, lung heart and macrophages.The aim of this study was the development of highly specific monoclonal antibodies against human YKL-39. Materials and methods. Using recombinant full-length human YKL-39 as immunogen using hybrido

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Kzhyshkowska, Julia, Srinivas Mamidi, Alexei Gratchev, et al. "Novel stabilin-1 interacting chitinase-like protein (SI-CLP) is up-regulated in alternatively activated macrophages and secreted via lysosomal pathway." Blood 107, no. 8 (2006): 3221–28. http://dx.doi.org/10.1182/blood-2005-07-2843.

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Abstract Mammalian Glyco_18-domain–containing proteins include catalytically active chitinases and chitinase-like proteins with cytokine activity involved in host defense and Th2-type inflammatory reactions. Here, we describe a novel human Glyco_18-domain–containing protein, SI-CLP, as an interacting partner of the endocytic/sorting receptor stabilin-1. Similarly to the chitinase-like cytokines YKL-39, YKL-40, and YM1/2, SI-CLP lacks a chitin-binding domain and catalytic amino acids. Using a novel mAb 1C11, we demonstrated that SI-CLP is sorted into late endosomes and secretory lysosomes in hu

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22

Chou, Yi-Te, Shihua Yao, Robert Czerwinski, et al. "Kinetic Characterization of Recombinant Human Acidic Mammalian Chitinase." Biochemistry 45, no. 14 (2006): 4444–54. http://dx.doi.org/10.1021/bi0525977.

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23

Cordeiro, Rossana Aguiar, Valdirene Moreira Gomes, Ana Fontenele Urano Carvalho, and Vânia Maria Maciel Melo. "Effect of proteins from the red seaweed Hypnea musciformis (Wulfen) Lamouroux on the growth of human pathogen yeasts." Brazilian Archives of Biology and Technology 49, no. 6 (2006): 915–21. http://dx.doi.org/10.1590/s1516-89132006000700008.

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A protein fraction, rich in lectin, obtained from the red seaweed Hypnea musciformis by precipitation with ammonium sulfate (F40/70) was screened for chitinase and beta-1,3-glucanase activity and assessed for antifungal potential against the human pathogen yeasts Candida albicans and C. guilliermondii. The F40/70 fraction showed chitinase and beta-1,3-glucanase enzymes, with specific activities of 276.43 and 1880.7 Units.mg -1 protein, respectively. It was capable of inhibiting the growth of C. guilliermondii at the concentrations of 45, 100 and 450 µg protein.ml -1 but it showed only a discre

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Dohnálek, Jan, Jarmila Dušková, Galina Tishchenko, et al. "Chitinase Chit62J4 Essential for Chitin Processing by Human Microbiome Bacterium Clostridium paraputrificum J4." Molecules 26, no. 19 (2021): 5978. http://dx.doi.org/10.3390/molecules26195978.

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Commensal bacterium Clostridium paraputrificum J4 produces several extracellular chitinolytic enzymes including a 62 kDa chitinase Chit62J4 active toward 4-nitrophenyl N,N′-diacetyl-β-d-chitobioside (pNGG). We characterized the crude enzyme from bacterial culture fluid, recombinant enzyme rChit62J4, and its catalytic domain rChit62J4cat. This major chitinase, securing nutrition of the bacterium in the human intestinal tract when supplied with chitin, has a pH optimum of 5.5 and processes pNGG with Km = 0.24 mM and kcat = 30.0 s−1. Sequence comparison of the amino acid sequence of Chit62J4, det

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Gouda, Hiroaki, Shinichi Terashima, Kanami Iguchi, et al. "Molecular modeling of human acidic mammalian chitinase in complex with the natural-product cyclopentapeptide chitinase inhibitor argifin." Bioorganic & Medicinal Chemistry 17, no. 17 (2009): 6270–78. http://dx.doi.org/10.1016/j.bmc.2009.07.045.

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26

Paoletti, Maurizio G., Lorenzo Norberto, Roberta Damini, and Salvatore Musumeci. "Human Gastric Juice Contains Chitinase That Can Degrade Chitin." Annals of Nutrition and Metabolism 51, no. 3 (2007): 244–51. http://dx.doi.org/10.1159/000104144.

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27

Yoo, Yeeun, and Hyoung T. Choi. "Antifungal chitinase against human pathogenic yeasts from Coprinellus congregatus." Journal of Microbiology 52, no. 5 (2014): 441–43. http://dx.doi.org/10.1007/s12275-014-3257-3.

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Bakri, Marwah M., Aisha M. H. Al-Rajhi, Emad Abada, et al. "Mycostimulator of chitinolytic activity: Thermodynamic studies and its activity against human and food-borne microbial pathogens." BioResources 17, no. 3 (2022): 4378–94. http://dx.doi.org/10.15376/biores.17.3.4378-4394.

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Chitinolytic activity and antibiosis are gaining prominence in various biotechnological fields. Dead fungal biomass (DFB) was used as a mycostimulator of chitinase production and antibiosis by Aspergillus fumigatus. The presence of DFB stimulated the synthesis of various secondary metabolites by A. fumigatus that were detected by gas chromatography-mass spectrometry analysis such as 6,8-Di-C-á-glucosylluteolin; bistrimethylsilyl N-acetyl eicosasphinga-4,11-dienine; curan-17-oic acid, 19,20-dihydroxy-, methyl ester, (19S)-; spiro[5à-androstane-3,2′-thiazolidine; retinal; Androsta-1,4-dien-3-one

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Pantoom, Supansa, Ingrid R. Vetter, Heino Prinz, and Wipa Suginta. "Potent Family-18 Chitinase Inhibitors." Journal of Biological Chemistry 286, no. 27 (2011): 24312–23. http://dx.doi.org/10.1074/jbc.m110.183376.

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Six novel inhibitors of Vibrio harveyi chitinase A (VhChiA), a family-18 chitinase homolog, were identified by in vitro screening of a library of pharmacologically active compounds. Unlike the previously identified inhibitors that mimicked the reaction intermediates, crystallographic evidence from 14 VhChiA-inhibitor complexes showed that all of the inhibitor molecules occupied the outer part of the substrate-binding cleft at two hydrophobic areas. The interactions at the aglycone location are well defined and tightly associated with Trp-397 and Trp-275, whereas the interactions at the glycone

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Kzhyshkowska, Julia, Shuiping Yin, Tengfei Liu, Vladimir Riabov, and Irina Mitrofanova. "Role of chitinase-like proteins in cancer." Biological Chemistry 397, no. 3 (2016): 231–47. http://dx.doi.org/10.1515/hsz-2015-0269.

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Abstract Chitinase-like proteins (CLPs) are lectins combining properties of cytokines and growth factors. Human CLPs include YKL-40, YKL-39 and SI-CLP that are secreted by cancer cells, macrophages, neutrophils, synoviocytes, chondrocytes and other cells. The best investigated CLP in cancer is YKL-40. Serum and plasma levels of YKL-40 correlate with poor prognosis in breast, lung, prostate, liver, bladder, colon and other types of cancers. In combination with other circulating factors YKL-40 can be used as a predictive biomarker of cancer outcome. In experimental models YKL-40 supports tumor i

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Cole, Garry T., Elizabeth J. Pishko, and Kalpathi R. Seshan. "Possible roles of wall hydrolases in the morphogenesis of Coccidioides immitis." Canadian Journal of Botany 73, S1 (1995): 1132–41. http://dx.doi.org/10.1139/b95-369.

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We have used the human respiratory pathogen, Coccidioides immitis, as an experimental model to explore possible interrelationships of wall-associated hydrolases, cell growth, and reproduction. Preliminary evidence has been presented that suggests that certain wall hydrolases (glucanase, chitinase) may play key roles in cell development in this systemic pathogen. Initial differentiation of the parasitic cells from cylindrical arthroconidia involves a period of isotropic growth and results in formation of a multinucleate spherule (approximately 60 μm diameter). An endo-1,3-β-glucanase that may p

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Tyurin, YU A., E. O. Sukmanskaya, S. N. Kulikov, and R. S. Fassakhov. "Chitinase-like protein YKL-40 from nasal mucosa as a biomarker of allergic rhinitis." Russian Journal of Allergy 9, no. 4 (2012): 13–17. http://dx.doi.org/10.36691/rja677.

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Background. Chitinase-like protein YKL-40 plays an important role in human atopic diseases. The aim of this study was to determine of the level of chitinase-like protein YKL-40 in the secretions of nasal mucosa of patients with chronic allergic rhinitis. Methods. Samples of allergic nasal mucosa were obtained from twelve patients with perennial allergic rhinitis. Measurement of nasal YKL-40 levels was performed with modification in duplicate using commercially available ELISA kits for YKL-40. The amount of nasal eosinophils and neutrophils were also determined. Results. There were significant

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Hong, Jeong Hee, Jung Yeon Hong, Boryung Park, et al. "Chitinase Activates Protease-Activated Receptor-2 in Human Airway Epithelial Cells." American Journal of Respiratory Cell and Molecular Biology 39, no. 5 (2008): 530–35. http://dx.doi.org/10.1165/rcmb.2007-0410oc.

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Rao, Francesco V., Douglas R. Houston, Rolf G. Boot, Johannes M. F. G. Aerts, Shohei Sakuda, and Daan M. F. Van Aalten. "Crystal Structures of Allosamidin Derivatives in Complex with Human Macrophage Chitinase." Journal of Biological Chemistry 278, no. 22 (2003): 20110–16. http://dx.doi.org/10.1074/jbc.m300362200.

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35

Andryianau, Gleb, Michal Kowalski, Michal C. Piotrowicz, et al. "Benzoxazepine-Derived Selective, Orally Bioavailable Inhibitor of Human Acidic Mammalian Chitinase." ACS Medicinal Chemistry Letters 11, no. 6 (2020): 1228–35. http://dx.doi.org/10.1021/acsmedchemlett.0c00092.

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36

Tjoelker, Larry W., Larry Gosting, Steve Frey, et al. "Structural and Functional Definition of the Human Chitinase Chitin-binding Domain." Journal of Biological Chemistry 275, no. 1 (2000): 514–20. http://dx.doi.org/10.1074/jbc.275.1.514.

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37

Boot, Rolf G., G. Herma Renkema, Anneke Strijland, Anton Jan van Zonneveld, and Johannes M. F. G. Aerts. "Cloning of a cDNA Encoding Chitotriosidase, a Human Chitinase Produced by Macrophages." Journal of Biological Chemistry 270, no. 44 (1995): 26252–56. http://dx.doi.org/10.1074/jbc.270.44.26252.

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Okawa, Kazuaki, Misa Ohno, Akinori Kashimura, et al. "Loss and Gain of Human Acidic Mammalian Chitinase Activity by Nonsynonymous SNPs." Molecular Biology and Evolution 33, no. 12 (2016): 3183–93. http://dx.doi.org/10.1093/molbev/msw198.

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HONG, J., K. LEE, K. KIM, H. JEE, M. SOHN, and K. KIM. "Effect Of Chitinase On Il-8 Production In Human Respiratory Epithelial Cells." Journal of Allergy and Clinical Immunology 121, no. 2 (2008): S205. http://dx.doi.org/10.1016/j.jaci.2007.12.765.

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Dinkelaar, Jasper, Boudewijn A. Duivenvoorden, Tom Wennekes, et al. "A Preparative Synthesis of Human Chitinase Fluorogenic Substrate (4′-Deoxychitobiosyl)-4-methylumbelliferone." European Journal of Organic Chemistry 2010, no. 13 (2010): 2565–70. http://dx.doi.org/10.1002/ejoc.201000080.

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Colussi, Paul A., Charles A. Specht, and Christopher H. Taron. "Characterization of a Nucleus-Encoded Chitinase from the Yeast Kluyveromyces lactis." Applied and Environmental Microbiology 71, no. 6 (2005): 2862–69. http://dx.doi.org/10.1128/aem.71.6.2862-2869.2005.

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ABSTRACT Endogenous proteins secreted from Kluyveromyces lactis were screened for their ability to bind to or to hydrolyze chitin. This analysis resulted in identification of a nucleus-encoded extracellular chitinase (KlCts1p) with a chitinolytic activity distinct from that of the plasmid-encoded killer toxin α-subunit. Sequence analysis of cloned KlCTS1 indicated that it encodes a 551-amino-acid chitinase having a secretion signal peptide, an amino-terminal family 18 chitinase catalytic domain, a serine-threonine-rich domain, and a carboxy-terminal type 2 chitin-binding domain. The associatio

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Mnkai, Jonathan, Manuel Ritter, Lucas Maganga, et al. "Increased HIV Incidence in Wuchereria bancrofti Microfilaria Positive Individuals in Tanzania." Pathogens 12, no. 3 (2023): 387. http://dx.doi.org/10.3390/pathogens12030387.

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Background: Infections with Wuchereria bancrofti are associated with reduced immunity against concomitant infections. Indeed, our previous study described a 2.3-fold increased HIV incidence among individuals with W. bancrofti infection, as measured by the circulating filarial antigen of the adult worm. This new study aimed to retrospectively determine microfilariae status of the participants to assess if the previously described increased HIV susceptibility was associated with the presence of MF in the same cohort. Methods: CFA positive but HIV negative biobanked human blood samples (n = 350)

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Fadel, Firas, Yuguang Zhao, Raul Cachau, et al. "New insights into the enzymatic mechanism of human chitotriosidase (CHIT1) catalytic domain by atomic resolution X-ray diffraction and hybrid QM/MM." Acta Crystallographica Section D Biological Crystallography 71, no. 7 (2015): 1455–70. http://dx.doi.org/10.1107/s139900471500783x.

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Chitotriosidase (CHIT1) is a human chitinase belonging to the highly conserved glycosyl hydrolase family 18 (GH18). GH18 enzymes hydrolyze chitin, anN-acetylglucosamine polymer synthesized by lower organisms for structural purposes. Recently, CHIT1 has attracted attention owing to its upregulation in immune-system disorders and as a marker of Gaucher disease. The 39 kDa catalytic domain shows a conserved cluster of three acidic residues, Glu140, Asp138 and Asp136, involved in the hydrolysis reaction. Under an excess concentration of substrate, CHIT1 and other homologues perform an additional a

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Kucerova, Lucie, Vaclav Broz, Badrul Arefin, et al. "The Drosophila Chitinase-Like Protein IDGF3 Is Involved in Protection against Nematodes and in Wound Healing." Journal of Innate Immunity 8, no. 2 (2015): 199–210. http://dx.doi.org/10.1159/000442351.

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Chitinase-like proteins (CLPs) of the 18 glycosyl hydrolase family retain structural similarity to chitinases but lack enzymatic activity. Although CLPs are upregulated in several human disorders that affect regenerative and inflammatory processes, very little is known about their normal physiological function. We show that an insect CLP (Drosophila imaginal disc growth factor 3, IDGF3) plays an immune-protective role during entomopathogenic nematode (EPN) infections. During these infections, nematodes force their entry into the host via border tissues, thus creating wounds. Whole-genome trans

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Makarova, S. I., D. V. Mitrofanov, A. B. Shintyapina, et al. "Search for associations between polymorphic variants of human acid chitinase gene and bronchial asthma in children of Novosibirsk." Siberian Journal of Clinical and Experimental Medicine 36, no. 4 (2022): 92–98. http://dx.doi.org/10.29001/2073-8552-2021-36-4-92-98.

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High prevalence of bronchial asthma among the population (about 300 million people all over the world) provides rationale for the search for candidate genes of disease. Human acidic chitinase (CHIA (AMCase)), encoded by the CHIA gene, is involved in the degradation of chitin, a component of the fungal cell wall and arthropod exoskeleton, which, if present in food or house dust, is a provoking factor for the bronchial asthma (BA) development. Functionally significant mutations in the CHIA gene may apparently increase the risk of susceptibility to BA.Aim. The aim of the study was to assess the a

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Song, Si-Youn, Young Jung Seo, Yong-Woon Kim, So-Young Park, Chang Hoon Bae, and Yong-Dae Kim. "Effect of Onchocerca Volvulus Chitinase on MUC5B Expression in Human Airway Epithelial Cells." American Journal of Rhinology & Allergy 27, no. 1 (2013): 3–7. http://dx.doi.org/10.2500/ajra.2013.27.3830.

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Görgens, S. W., M. Hjorth, K. Eckardt, et al. "The exercise-regulated myokine chitinase-3-like protein 1 stimulates human myocyte proliferation." Acta Physiologica 216, no. 3 (2015): 330–45. http://dx.doi.org/10.1111/apha.12579.

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Hong, J. Y., K. E. Lee, K. W. Kim, et al. "Effect of Chitinase on Il-8 Gene Expression in Human Respiratory Epithelial Cells." Journal of Allergy and Clinical Immunology 119, no. 1 (2007): S290. http://dx.doi.org/10.1016/j.jaci.2006.12.505.

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UJITA, Minoru, Kaori SAKAI, Keishi HAMAZAKI, Masahiko YONEDA, Shigeki ISOMURA, and Akira HARA. "Carbohydrate Binding Specificity of the Recombinant Chitin-binding Domain of Human Macrophage Chitinase." Bioscience, Biotechnology, and Biochemistry 67, no. 11 (2003): 2402–7. http://dx.doi.org/10.1271/bbb.67.2402.

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Kim, Young-Dae, Chang-Hoon Bae, and Si-Youn Song. "Effect of Onchocerca Volvulus Chitinase on MUC5B Expression in Human Airway Epithelial Cells." Otolaryngology–Head and Neck Surgery 149, no. 2_suppl (2013): P257. http://dx.doi.org/10.1177/0194599813496044a348.

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