13
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Chitinases: An update

      review-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Chitin, the second most abundant polysaccharide in nature after cellulose, is found in the exoskeleton of insects, fungi, yeast, and algae, and in the internal structures of other vertebrates. Chitinases are enzymes that degrade chitin. Chitinases contribute to the generation of carbon and nitrogen in the ecosystem. Chitin and chitinolytic enzymes are gaining importance for their biotechnological applications, especially the chitinases exploited in agriculture fields to control pathogens. Chitinases have a use in human health care, especially in human diseases like asthma. Chitinases have wide-ranging applications including the preparation of pharmaceutically important chitooligosaccharides and N-acetyl D glucosamine, preparation of single-cell protein, isolation of protoplasts from fungi and yeast, control of pathogenic fungi, treatment of chitinous waste, mosquito control and morphogenesis, etc. In this review, the various types of chitinases and the chitinases found in different organisms such as bacteria, plants, fungi, and mammals are discussed.

          Related collections

          Most cited references 121

          • Record: found
          • Abstract: found
          • Article: not found

          New families in the classification of glycosyl hydrolases based on amino acid sequence similarities.

          301 glycosyl hydrolases and related enzymes corresponding to 39 EC entries of the I.U.B. classification system have been classified into 35 families on the basis of amino-acid-sequence similarities [Henrissat (1991) Biochem. J. 280, 309-316]. Approximately half of the families were found to be monospecific (containing only one EC number), whereas the other half were found to be polyspecific (containing at least two EC numbers). A > 60% increase in sequence data for glycosyl hydrolases (181 additional enzymes or enzyme domains sequences have since become available) allowed us to update the classification not only by the addition of more members to already identified families, but also by the finding of ten new families. On the basis of a comparison of 482 sequences corresponding to 52 EC entries, 45 families, out of which 22 are polyspecific, can now be defined. This classification has been implemented in the SWISS-PROT protein sequence data bank.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation.

            Chitin is a surface component of parasites and insects, and chitinases are induced in lower life forms during infections with these agents. Although chitin itself does not exist in humans, chitinases are present in the human genome. We show here that acidic mammalian chitinase (AMCase) is induced via a T helper-2 (Th2)-specific, interleukin-13 (IL-13)-mediated pathway in epithelial cells and macrophages in an aeroallergen asthma model and expressed in exaggerated quantities in human asthma. AMCase neutralization ameliorated Th2 inflammation and airway hyperresponsiveness, in part by inhibiting IL-13 pathway activation and chemokine induction. AMCase may thus be an important mediator of IL-13-induced responses in Th2-dominated disorders such as asthma.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family.

              One of the major secreted proteins of human articular chondrocytes in monolayer or explant culture and of synovial fibroblasts is a glycoprotein with an apparent molecular weight of approximately 39,000, referred to as human cartilage glycoprotein-39 (HC gp-39). The protein was purified, and its complete cDNA sequence was determined. It contained an open reading frame coding for a 383-amino acid long peptide. Comparison of the deduced amino acid sequence with known sequences revealed that HC gp-39 contained regions displaying significant homology with a group of bacterial and fungal chitinases and a similar enzyme found in the nematode, Brugia malayi. In addition significant homologies were observed with three mammalian secretory proteins of as yet unknown function, suggesting that a related protein family exists in mammals. The human protein does not possess any glycosidic activity against chitinase substrates, arguing against any function as an endoglycosidase with specificity for N-acetylglucosamine. Analysis by Northern blotting and by reverse transcription/polymerase chain reaction showed mRNA for HC gp-39 to be present in human articular chondrocytes as well is in liver, while mRNA was undetectable in muscle tissues, lung, pancreas, mononuclear cells, or fibroblasts. Neither the protein nor mRNA for HC gp-39 was detectable in normal newborn or adult human articular cartilage obtained at surgery, while mRNA for HC gp-39 was detectable both in synovial specimens and in cartilage obtained from patients with rheumatoid arthritis. These observations suggest that the expression of HC gp-39 may be related to a response of these cells to an altered tissue environment.
                Bookmark

                Author and article information

                Journal
                J Pharm Bioallied Sci
                J Pharm Bioallied Sci
                JPBS
                Journal of Pharmacy & Bioallied Sciences
                Medknow Publications & Media Pvt Ltd (India )
                0976-4879
                0975-7406
                Jan-Mar 2013
                : 5
                : 1
                : 21-29
                Affiliations
                Department of Biochemistry, Faculty of Science, Jamia Hamdard, New Delhi, India
                [1 ]Department of Biotechnology, Faculty of Science, Jamia Hamdard, New Delhi, India
                [2 ]Department of Microbiology, Faculty of Agricultural Sciences, AMU, Aligarh, India
                Author notes
                Address for correspondence: Dr. Saleem Javed, E-mail: saleemjaved70@ 123456yahoo.co.in
                Article
                JPBS-5-21
                10.4103/0975-7406.106559
                3612335
                23559820
                Copyright: © Journal of Pharmacy and Bioallied Sciences

                This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                Categories
                Review Article

                Comments

                Comment on this article