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Gene Review

CHIT1  -  chitinase 1 (chitotriosidase)

Homo sapiens

Synonyms: CHI3, CHIT, CHITD, Chitinase-1, Chitotriosidase-1
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Disease relevance of CHIT1

  • These results indicate that a CHIT1 genotype associated previously with susceptibility to filariasis in residents of southern India and TLR2 and TLR4 polymorphisms do not correlate with infection status or disease phenotype in this Melanesian population [1].
  • There was no association of infection status, lymphedema of an extremity, or hydrocele with chitotriosidase genotype (CHIT1) [1].
  • We conclude from our results that CHIT1 does not play a major role in the development of bronchial asthma in Caucasian children [2].
  • Chitotriosidase and human cartilage gp-39 (HC gp-39) are members of the chitinase family of proteins and are expressed in lipid-laden macrophages accumulated in various organs during Gaucher disease [3].
  • METHODS: A class I chitinase-specific complementary DNA from H. brasiliensis leaves was synthesized, subcloned, sequenced and overexpressed in fusion with the maltose-binding protein (MBP) in Escherichia coli [4].

Psychiatry related information on CHIT1

  • This pattern of chitinase expression is a common feature of strains representing all currently known genotypes of A. astaci, suggesting that it is an adaptation to the exclusively parasitic life-style of this species [5].

High impact information on CHIT1

  • The chitinase 3-like 1 gene (CHI3L1) is abnormally expressed in the hippocampus of subjects with schizophrenia and may be involved in the cellular response to various environmental events that are reported to increase the risk of schizophrenia [6].
  • Thus far, only one potent chitinase inhibitor has been described in detail, the pseudotrisaccharide allosamidin [7].
  • Recently, however, two potent natural-product cyclopentapeptide chitinase inhibitors, argifin and argadin, were reported [7].
  • Chitinase B (ChiB) from Serratia marcescens is a family 18 exo-chitinase whose catalytic domain has a TIM-barrel fold with a tunnel-shaped active site [8].
  • By using molecular dynamics simulations, we have examined the binding of a hexaNAG substrate and two potential hydrolysis intermediates (an oxazoline ion and an oxocarbenium ion) to a family 19 barley chitinase [9].

Chemical compound and disease context of CHIT1


Biological context of CHIT1

  • An association was observed between the HH variant CHIT1 genotype, which correlates with decreased activity and levels of chitotriosidase and susceptibility to filarial infection (MF+ and CP; P = 0.013) [15].
  • Comparison with YM1 and HCgp-39 shows how the chitinase has evolved into these mammalian lectins by the mutation of key residues in the active site, tuning the substrate binding specificity [16].
  • Assignment of human plasma methylumbelliferyl-tetra-N-acetylchitotetraoside hydrolase or chitinase to chromosome 1q by a linkage study [17].
  • We hypothesize that this is due to the production of soluble inducers following chitin hydrolysis by CHIT1 and that M. anisopliae uses enzymes expressed at low levels to sense the nature of the polymeric nutrient present in the immediate environment [18].
  • In this study we were interested in whether CHIT1 is also involved in the genetics of asthma [2].

Anatomical context of CHIT1

  • CHIT1 is expressed by activated macrophages and hydrolyzes artificial chitotrioside substrates, but its specific function in humans is unknown, since it is generally believed that man completely lacks endogenous chitin and endogenous substrates for chitinases [19].
  • Isolation and sequence of a novel human chondrocyte protein related to mammalian members of the chitinase protein family [20].
  • We have previously reported that the expression of HC gp-39, a 39-kDa secretory glycoprotein and member of the chitinase protein family, is associated with late stages of monocyte to macrophage maturation [21].
  • In contrast, the homologous cousin molecule YKL-40 (chitinase 3-like 1), which is elevated in serum and synovial fluid of patients with arthritis, showed no significant regulation in OA cartilage [22].
  • This chitinase has been shown to have lytic activity on Botrytis cinerea cell walls in vitro [23].

Associations of CHIT1 with chemical compounds

  • The chitotriosidase was shown to be active against colloidal chitin and is inhibited by the family 18 chitinase inhibitor allosamidin [16].
  • Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages [24].
  • To assess this hypothesis, we evaluated the CHIT1 mRNA levels in human monocytes/macrophages (HMMs) following treatment with interferon-gamma (IFNgamma), tumor necrosis factor-alpha (TNFalpha), and lipopolysaccharide (LPS) [25].
  • YKL-39 lacks the active site glutamate, which is essential for the activity of chitinases, and as expected has no chitinase activity [20].
  • OBJECTIVES: The present study aimed to produce a recombinant latex class I chitinase from Hevea brasiliensis leaves and to study its immunoglobulin (Ig)E-binding reactivity [4].

Physical interactions of CHIT1

  • The results suggest that human chitinase chitin-binding domain may be involved in tissue remodeling through binding to polysaccharides or extracellular matrix glycoproteins, and this recombinant protein can be used to elucidate biological functions of the enzyme [26].

Other interactions of CHIT1

  • We have identified two polymorphisms, CHIT1 and MBL2 that are associated with susceptibility to human filarial infection, findings that merit further follow-up in a larger study [15].
  • In man, chitotriosidase is the functional chitinolytic enzyme, whilst the homologous human cartilage 39-kDa glycoprotein (HC gp-39) does not exhibit chitinase activity and its function is unknown [24].
  • Strong induction of members of the chitinase family of proteins in atherosclerosis: chitotriosidase and human cartilage gp-39 expressed in lesion macrophages [3].
  • Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member [27].
  • We introduced the rice chitinase (Cht-2; RCC2) gene into calli of Italian ryegrass (Lolium multiflorum Lam.), with a hygromycin phosphotransferase (HPT) gene as a selectable marker, by particle bombardment [28].

Analytical, diagnostic and therapeutic context of CHIT1


  1. Polymorphisms of innate immunity genes and susceptibility to lymphatic filariasis. Hise, A.G., Hazlett, F.E., Bockarie, M.J., Zimmerman, P.A., Tisch, D.J., Kazura, J.W. Genes Immun. (2003) [Pubmed]
  2. Genetic polymorphisms of chitotriosidase in Caucasian children with bronchial asthma. Bierbaum, S., Superti-Furga, A., Heinzmann, A. Int. J. Immunogenet. (2006) [Pubmed]
  3. Strong induction of members of the chitinase family of proteins in atherosclerosis: chitotriosidase and human cartilage gp-39 expressed in lesion macrophages. Boot, R.G., van Achterberg, T.A., van Aken, B.E., Renkema, G.H., Jacobs, M.J., Aerts, J.M., de Vries, C.J. Arterioscler. Thromb. Vasc. Biol. (1999) [Pubmed]
  4. Molecular cloning, purification, and IgE-binding of a recombinant class I chitinase from Hevea brasiliensis leaves (rHev b 11.0102). Rihs, H.P., Dumont, B., Rozynek, P., Lundberg, M., Cremer, R., Brüning, T., Raulf-Heimsoth, M. Allergy (2003) [Pubmed]
  5. Analysis of chitinase expression in the crayfish plague fungus Aphanomyces astaci. Andersson, M.G., Cerenius, L. Dis. Aquat. Org. (2002) [Pubmed]
  6. Functional Variants in the Promoter Region of Chitinase 3-Like 1 (CHI3L1) and Susceptibility to Schizophrenia. Zhao, X., Tang, R., Gao, B., Shi, Y., Zhou, J., Guo, S., Zhang, J., Wang, Y., Tang, W., Meng, J., Li, S., Wang, H., Ma, G., Lin, C., Xiao, Y., Feng, G., Lin, Z., Zhu, S., Xing, Y., Sang, H., St Clair, D., He, L. Am. J. Hum. Genet. (2007) [Pubmed]
  7. High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: mimicry of carbohydrate substrate. Houston, D.R., Shiomi, K., Arai, N., Omura, S., Peter, M.G., Turberg, A., Synstad, B., Eijsink, V.G., van Aalten, D.M. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  8. Structural insights into the catalytic mechanism of a family 18 exo-chitinase. van Aalten, D.M., Komander, D., Synstad, B., Gåseidnes, S., Peter, M.G., Eijsink, V.G. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  9. The role of enzyme distortion in the single displacement mechanism of family 19 chitinases. Brameld, K.A., Goddard, W.A. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  10. Hepatotoxicity and mechanism of action of haloalkanes: carbon tetrachloride as a toxicological model. Weber, L.W., Boll, M., Stampfl, A. Crit. Rev. Toxicol. (2003) [Pubmed]
  11. Endogenous Nod-factor-like signal molecules promote early somatic embryo development in Norway spruce. Dyachok, J.V., Wiweger, M., Kenne, L., von Arnold, S. Plant Physiol. (2002) [Pubmed]
  12. Cloning and molecular characterization of the Hevea brasiliensis allergen Hev b 11, a class I chitinase. O'Riordain, G., Radauer, C., Hoffmann-Sommergruber, K., Adhami, F., Peterbauer, C.K., Blanco, C., Godnic-Cvar, J., Scheiner, O., Ebner, C., Breiteneder, H. Clin. Exp. Allergy (2002) [Pubmed]
  13. Shewanella sediminis sp. nov., a novel Na+-requiring and hexahydro-1,3,5-trinitro-1,3,5-triazine-degrading bacterium from marine sediment. Zhao, J.S., Manno, D., Beaulieu, C., Paquet, L., Hawari, J. Int. J. Syst. Evol. Microbiol. (2005) [Pubmed]
  14. Improving macromolecular electrostatics calculations. Nielsen, J.E., Andersen, K.V., Honig, B., Hooft, R.W., Klebe, G., Vriend, G., Wade, R.C. Protein Eng. (1999) [Pubmed]
  15. Genetic polymorphisms in molecules of innate immunity and susceptibility to infection with Wuchereria bancrofti in South India. Choi, E.H., Zimmerman, P.A., Foster, C.B., Zhu, S., Kumaraswami, V., Nutman, T.B., Chanock, S.J. Genes Immun. (2001) [Pubmed]
  16. Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins. Fusetti, F., von Moeller, H., Houston, D., Rozeboom, H.J., Dijkstra, B.W., Boot, R.G., Aerts, J.M., van Aalten, D.M. J. Biol. Chem. (2002) [Pubmed]
  17. Assignment of human plasma methylumbelliferyl-tetra-N-acetylchitotetraoside hydrolase or chitinase to chromosome 1q by a linkage study. Eiberg, H., Den Tandt, W.R. Hum. Genet. (1997) [Pubmed]
  18. Transformants of Metarhizium anisopliae sf. anisopliae overexpressing chitinase from Metarhizium anisopliae sf. acridum show early induction of native chitinase but are not altered in pathogenicity to Manduca sexta. Screen, S.E., Hu, G., St Leger, R.J. J. Invertebr. Pathol. (2001) [Pubmed]
  19. The evolutionary conservation of the human chitotriosidase gene in rodents and primates. Gianfrancesco, F., Musumeci, S. Cytogenet. Genome Res. (2004) [Pubmed]
  20. Isolation and sequence of a novel human chondrocyte protein related to mammalian members of the chitinase protein family. Hu, B., Trinh, K., Figueira, W.F., Price, P.A. J. Biol. Chem. (1996) [Pubmed]
  21. Molecular characterization of the gene for human cartilage gp-39 (CHI3L1), a member of the chitinase protein family and marker for late stages of macrophage differentiation. Rehli, M., Krause, S.W., Andreesen, R. Genomics (1997) [Pubmed]
  22. Enhanced expression of the human chitinase 3-like 2 gene (YKL-39) but not chitinase 3-like 1 gene (YKL-40) in osteoarthritic cartilage. Steck, E., Breit, S., Breusch, S.J., Axt, M., Richter, W. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  23. Characterization of ech-42, a Trichoderma harzianum endochitinase gene expressed during mycoparasitism. Carsolio, C., Gutiérrez, A., Jiménez, B., Van Montagu, M., Herrera-Estrella, A. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  24. Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages. Renkema, G.H., Boot, R.G., Au, F.L., Donker-Koopman, W.E., Strijland, A., Muijsers, A.O., Hrebicek, M., Aerts, J.M. Eur. J. Biochem. (1998) [Pubmed]
  25. Interferon-gamma, tumor necrosis factor-alpha, and lipopolysaccharide promote chitotriosidase gene expression in human macrophages. Malaguarnera, L., Musumeci, M., Di Rosa, M., Scuto, A., Musumeci, S. J. Clin. Lab. Anal. (2005) [Pubmed]
  26. Carbohydrate binding specificity of the recombinant chitin-binding domain of human macrophage chitinase. Ujita, M., Sakai, K., Hamazaki, K., Yoneda, M., Isomura, S., Hara, A. Biosci. Biotechnol. Biochem. (2003) [Pubmed]
  27. Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member. Saito, A., Ozaki, K., Fujiwara, T., Nakamura, Y., Tanigami, A. Gene (1999) [Pubmed]
  28. Increased resistance to crown rust disease in transgenic Italian ryegrass (Lolium multiflorum Lam.) expressing the rice chitinase gene. Takahashi, W., Fujimori, M., Miura, Y., Komatsu, T., Nishizawa, Y., Hibi, T., Takamizo, T. Plant Cell Rep. (2005) [Pubmed]
  29. Allelic frequency determination of the 24-bp chitotriosidase duplication in the Portuguese population by real-time PCR. Rodrigues, M.R., Sá Miranda, M.C., Amaral, O. Blood Cells Mol. Dis. (2004) [Pubmed]
  30. Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris. Broglie, K.E., Gaynor, J.J., Broglie, R.M. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  31. Screening-based Discovery and Structural Dissection of a Novel Family 18 Chitinase Inhibitor. Schüttelkopf, A.W., Andersen, O.A., Rao, F.V., Allwood, M., Lloyd, C., Eggleston, I.M., van Aalten, D.M. J. Biol. Chem. (2006) [Pubmed]
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