ArticleMolecular biology and evolution2016
Loss and Gain of Human Acidic Mammalian Chitinase Activity by Nonsynonymous SNPs.
Article in Molecular biology and evolution, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 47 citations in OpenAlex.
- Humanizing acidic mammalian chitinase variants establish lung immune conditioning and control environmentally driven inflammation and fibrosis.Cell reports · 2026Article
- Evolution of Acidic Mammalian Chitinase Gene (Ecology and evolution · 2026Article
- Key Amino Acids Controlling pH Optima in Avian Chia Paralogs: Mechanistic Insights into Functional Divergence.Molecules (Basel, Switzerland) · 2026Article
- Elucidation of the Catalytic Apparatus and Mechanism of Human Chitotriosidase‑1.ACS catalysis · 2025Article
- Hyperactivation of human acidic chitinase (Chia) for potential medical use.The Journal of biological chemistry · 2025Article
- A Simplified Method for Evaluating Chitin-Binding Activity Applied to YKL-40 (HC-gp39, CHI3L1) and Chitotriosidase.Molecules (Basel, Switzerland) · 2024Article
- An ILC2-chitinase circuit restores lung homeostasis after epithelial injury.Science immunology · 2024Article
- Article
- A type 2 immune circuit in the stomach controls mammalian adaptation to dietary chitin.Science (New York, N.Y.) · 2023Article
- Evolutionary activation of acidic chitinase in herbivores through the H128R mutation in ruminant livestock.iScience · 2023Article
- Irreversible evolutionary loss of chitin-degrading ability in the chitinase-like protein Ym1 under positive selection in rodents.Protein science : a publication of the Protein Society · 2023Article
- Crab-Eating Monkey Acidic Chitinase (CHIA) Efficiently Degrades Chitin and Chitosan under Acidic and High-Temperature Conditions.Molecules (Basel, Switzerland) · 2022Article
- Noninsect-Based Diet Leads to Structural and Functional Changes of Acidic Chitinase in Carnivora.Molecular biology and evolution · 2022Article
- Occupational exposure to gasoline in gasoline station male attendants promotes M1 polarization in macrophages.Environmental science and pollution research international · 2022Article
- Mouse Acidic Chitinase Effectively Degrades Random-Type Chitosan to Chitooligosaccharides of Variable Lengths under Stomach and Lung Tissue pH Conditions.Molecules (Basel, Switzerland) · 2021Article
- Robust chitinolytic activity of crab-eating monkey (Macaca fascicularis) acidic chitinase under a broad pH and temperature range.Scientific reports · 2021Article
- Chitinases and Chitinase-Like Proteins as Therapeutic Targets in Inflammatory Diseases, with a Special Focus on Inflammatory Bowel Diseases.International journal of molecular sciences · 2021Review
- A Helminth-Derived Chitinase Structurally Similar to Mammalian Chitinase Displays Immunomodulatory Properties in Inflammatory Lung Disease.Journal of immunology research · 2021Article
- Differences in the chitinolytic activity of mammalian chitinases on soluble and insoluble substrates.Protein science : a publication of the Protein Society · 2020Article
- Chitinases and Chitinase-Like Proteins in Obstructive Lung Diseases - Current Concepts and Potential Applications.International journal of chronic obstructive pulmonary disease · 2020Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acidic mammalian chitinase (AMCase) is implicated in asthma, allergic inflammation, and food processing. Little is known about genetic and evolutional regulation of chitinolytic activity of AMCase. Here, we relate human AMCase polymorphisms to the mouse AMCase, and show that the highly active variants encoded by nonsynonymous single-nucleotide polymorphisms (nsSNPs) are consistent with the mouse AMCase sequence. The chitinolytic activity of the recombinant human AMCase was significantly lower than that of the mouse counterpart. By creating mouse-human chimeric AMCase protein we found that the presence of the N-terminal region of human AMCase containing conserved active site residues reduced the enzymatic activity of the molecule. We were able to significantly increase the activity of human AMCase by amino acid substitutions encoded by nsSNPs (N45, D47, and R61) with those conserved in the mouse homologue (D45, N47, and M61). For abolition of the mouse AMCase activity, introduction of M61R mutation was sufficient. M61 is conserved in most of primates other than human and orangutan as well as in other mammals. Orangutan has I61 substitution, which also markedly reduced the activity of the mouse AMCase, indicating that the M61 is a crucial residue for the chitinolytic activity. Altogether, our data suggest that human AMCase has lost its chitinolytic activity by integration of nsSNPs during evolution and that the enzyme can be reactivated by introducing amino acids conserved in the mouse counterpart.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.