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Relevant bibliographies by topics / Human Chitinase

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Journal articles

Academic literature on the topic 'Human Chitinase'

Author: Grafiati

Published: 14 March 2023

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Journal articles on the topic "Human Chitinase"

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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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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6

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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7

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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