575
Views
1
CrossRef citations to date
0
Altmetric
Biochemistry & Molecular Biology

Characterization of mouse di-N-acetylchitobiase that can degrade chitin-oligosaccharides

, ORCID Icon, , , , & show all
Pages 2499-2507 | Received 10 Jun 2020, Accepted 30 Jul 2020, Published online: 16 Aug 2020

References

  • Koch BE, Stougaard J, Spaink HP. Keeping track of the growing number of biological functions of chitin and its interaction partners in biomedical research. Glycobiology. 2015;25:469–482.
  • Cohen-Kupiec R, Chet I. The molecular biology of chitin digestion. Curr Opin Biotechnol. 1998;9:270–277.
  • Shaikh SA, Deshpande MV. Chitinolytic enzymes: their contribution to basic and applied research. World J Microbiol Biotechnol. 1993;9:468–475.
  • Hollak CE, van Weely S, van Oers MH, et al. Marked elevation of plasma chitotriosidase activity. A novel hallmark of Gaucher disease. J Clin Invest. 1994;93:1288–1292.
  • Boot RG, Blommaart EF, Swart E, et al. Identification of a novel acidic mammalian chitinase distinct from chitotriosidase. J Biol Chem. 2001;276:6770–6778.
  • Kuranda MJ, Aronson NN Jr. A di-N-acetylchitobiase activity is involved in the lysosomal catabolism of asparagine-linked glycoproteins in rat liver. J Biol Chem. 1986;261:5803–5809.
  • Ohno M, Tsuda K, Sakaguchi M, et al. Chitinase mRNA levels by quantitative PCR using the single standard DNA: acidic mammalian chitinase is a major transcript in the mouse stomach. PLoS One. 2012;7:e50381.
  • Kimura M, Wakita S, Ishikawa K, et al. Functional properties of mouse chitotriosidase expressed in the periplasmic space of Escherichia coli. PLoS One. 2016;11:e0164367.
  • Boot RG, Bussink AP, Verhoek M, et al. Marked differences in tissue-specific expression of chitinases in mouse and man. J Histochem Cytochem. 2005;53:1283–1292.
  • Ohno M, Togashi Y, Tsuda K, et al. Quantification of chitinase mRNA levels in human and mouse tissues by real-time PCR: species-specific expression of acidic mammalian chitinase in stomach tissues. PLoS One. 2013;8:e67399.
  • Kashimura A, Okawa K, Ishikawa K, et al. Protein A-mouse acidic mammalian chitinase-V5-His expressed in periplasmic space of Escherichia coli possesses chitinase functions comparable to CHO-expressed protein. PLoS One. 2013;8:e78669.
  • Kashimura A, Kimura M, Okawa K, et al. Functional properties of the catalytic domain of mouse acidic mammalian chitinase expressed in Escherichia coli. Int J Mol Sci. 2015;16:4028–4042.
  • Ohno M, Kimura M, Miyazaki H, et al. Acidic mammalian chitinase is a proteases-resistant glycosidase in mouse digestive system. Sci Rep. 2016;6:37756.
  • Tabata E, Kashimura A, Wakita S, et al. Protease resistance of porcine acidic mammalian chitinase under gastrointestinal conditions implies that chitin-containing organisms can be sustainable dietary resources. Sci Rep. 2017;7:12963.
  • Tabata E, Kashimura A, Wakita S, et al. Gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry. Sci Rep. 2017;7:6662.
  • Tabata E, Kashimura A, Kikuchi A, et al. Chitin digestibility is dependent on feeding behaviors, which determine acidic chitinase mRNA levels in mammalian and poultry stomachs. Sci Rep. 2018;8:1461.
  • Stirling JL. Human N-acetyl-β-hexosaminidases: hydrolysis of N, N’ diacetylchitobiose by a low molecular weight enzyme. FEBS Lett. 1974;39:171–175.
  • Stirling JL. NN’-diacetylchitobiase activity in Tay-Sachs disease and Sandhoff’s disease. Biochem J. 1974;141:597–599.
  • Aronson NN Jr., Backes M, Kuranda MJ. Rat liver chitobiase: purification, properties, and role in the lysosomal degradation of Asn-linked glycoproteins. Arch Biochem Biophys. 1989;272:290–300.
  • Aronson NN Jr., Halloran BA. Optimum substrate size and specific anomer requirements for the reducing-end glycoside hydrolase di-N-acetylchitobiase. Biosci Biotechnol Biochem. 2006;70:1537–1541.
  • Boot RG, Renkema GH, Strijland A, et al. Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages. J Biol Chem. 1995;270:26252–26256.
  • Liu B, Ahmad W, Aronson NN Jr. Structure of the human gene for lysosomal di-N-acetylchitobiase. Glycobiology. 1999;9:589–593.
  • Terwisscha van Scheltinga AC, Armand S, Kalk KH, et al. Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and x-ray structure of a complex with allosamidin evidence for substrate assisted catalysis. Biochemistry. 1995;34:15619–15623.
  • van Aalten DMF, Komander D, Synstad B, et al. Structural insights into the catalytic mechanism of a family 18 exo-chitinase. Proc Nat Acad Sci. 2001;98:8979–8984.
  • Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods. 2001;25:402–408.
  • McIlvaine TC. A buffer solution for colorimetric comparison. J Biol Chem. 1921;49:183–186.
  • Reissig JL, Storminger JL, Leloir LF. A modified colorimetric method for the estimation of N-acetylamino sugars. J Biol Chem. 1955;217:959–966.
  • Jackson P. The use of polyacrylamide-gel electrophoresis for the high-resolution separation of reducing saccharides labelled with the fluorophore 8-aminonaphthalene-1,3,6-trisulphonic acid. Detection of picomolar quantities by an imaging system based on a cooled charge-coupled device. Biochem J. 1990;270:705–713.
  • Wakita S, Kimura M, Kato N, et al. Improved fluorescent labeling of chitin oligomers: chitinolytic properties of acidic mammalian chitinase under somatic tissue pH conditions. Carbohydr Polym. 2017;164:145–153.
  • Balducci C, Bibi L, Berg T, et al. Molecular cloning and structural organization of the gene encoding the mouse lysosomal di-N-acetylchitobiase (ctbs). Gene. 2008;416:85–91.
  • Hantzopoulos PA, Calhoun DH. Expression of the human alpha-galactosidase A in Escherichia coli K-12. Gene. 1987;57:159–169.
  • Mosquera A, Rodríguez A, Soto C, et al. Characterization of a recombinant N-acetylgalactosamine-6-sulfate sulfatase produced in E. coli for enzyme replacement therapy of Morquio A disease. Process Biochem. 2012;47:2097–2102.
  • Morales-Álvarez ED, Rivera-Hoyos CM, Baena-Moncada AM, et al. Low-scale expression and purification of an active putative iduronate 2-sulfate sulfatase-Like enzyme from Escherichia coli K12. J Microbiol. 2013;51:213–221.
  • McConnell EL, Basit AW, Murdan S. Measurements of rat and mouse gastrointestinal pH, fluid and lymphoid tissue, and implications for in-vivo experiments. J Pharm Pharmacol. 2008;60:63–70.
  • Stinchi S, Lüllmann-Rauch R, Hartmann D, et al. Targeted disruption of the lysosomal α-mannosidase gene results in mice resembling a mild form of human α-mannosidosis. Hum Mol Genet. 1999;8:1365–1372.
  • Park C, Meng L, Stanton LH, et al. Characterization of a human core-specific lysosomal α1,6-mannosidase involved in N-glycan catabolism. J Biol Chem. 2005;280:37204–37216.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.