Acidic mammalian chitinase gene is highly expressed in the special oxyntic glands of <i>Manis javanica</i>

Ma, Jinge; Li, Linmiao; Jiang, Haiying; Zhang, Xiujuan; Li, Juan; Li, Guanyu; Chen, Jinping

doi:10.1002/2211-5463.12461

Cited by 14 publications

(14 citation statements)

References 36 publications

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“…Moreover, compared to those of carnivores, pangolins have longer intestinal tracts, 24 which may allow chitinase more time for chitin digestion in the intestine. Together with the chitinase expressed in its saliva and stomach, 27 these constitute an adaptation that allows the utilization of ants and termites as primary food sources.…”

Section: Discussionmentioning

confidence: 99%

Expression Profile of the Digestive Enzymes of Manis javanica Reveals Its Adaptation to Diet Specialization

Zhang

et al. 2019

ACS Omega

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The expression of animal digestive enzymes reflects important dietary adaptations. The pangolin, also known as scaly anteater, is a specialized myrmecophage that consumes mainly ants and termites, but its digestive enzymes have not been fully investigated. Therefore, in this study, we used shotgun proteomic analysis to examine the protein components of the saliva and intestinal juice of a Sunda pangolin (Manis javanica) that died shortly after being rescued. The intestinal juice contained greater variety of digestive enzymes, including α-amylase, maltase-glucoamylase, α,α-trehalase, sucrase-isomaltase, pepsin A, trypsin, pancreatic endopeptidase E, carboxypeptidase A1, carboxypeptidase B, dipeptidyl-peptidase 4, and pancreatic triacylglycerol lipase. The digestive enzymes identified in the saliva were maltase-glucoamylase and trypsin, and chitinase which was also found in the intestinal juice. Compared with other animals, the Sunda pangolin has less intestinal protease diversity and lacks key digestive enzymes, such as chymotrypsin and pancreatic elastase. The expression profile of the digestive enzymes of the Sunda pangolin reveals animal’s adaptation to a diet consisting mainly of ants and termites. Our results will facilitate the preparation of artificial food for rescued pangolins and for those in captivity for conservation breeding efforts.

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Section: Discussionmentioning

confidence: 99%

Expression Profile of the Digestive Enzymes of Manis javanica Reveals Its Adaptation to Diet Specialization

Zhang

et al. 2019

ACS Omega

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“…Acidic chitinase (Chia; also referred to acidic mammalian chitinase, “AMCase”; Boot et al 2001 , 2005 ) hydrolyzes the β-1, 4 glycoside bonds of chitin, a major structural polysaccharide in insects ( Bueter et al 2013 ; Wysokowski et al 2015 ; Van Dyken and Locksley 2018 ). Chia is expressed in the stomachs of insectivorous and omnivorous animals including bat ( Strobel et al 2013 ), mouse ( Ohno et al 2016 ), pangolin ( Ma et al 2018 ), crab-eating monkey ( Uehara et al 2018 , 2021 ), and common marmoset ( Tabata, Kashimura, et al 2019 ). In addition, omnivorous livestock animals, such as chicken and pig, express Chia at high levels in their stomachs and are able to degrade chitin and chitin-containing materials such as shrimp shells and mealworm larvae shells under normal gastrointestinal conditions ( Tabata, Kashimura, Wakita, Ohno, Sakaguchi, Sugahara, Imamura, et al 2017 ; Tabata, Kashimura, Wakita, Ohno, Sakaguchi, Sugahara, Kino, et al 2017 ; Tabata, Kashimura, Wakita, et al 2018 ; Tabata, Wakita, et al 2019 ).…”

Section: Introductionmentioning

confidence: 99%

Noninsect-Based Diet Leads to Structural and Functional Changes of Acidic Chitinase in Carnivora

Tabata

Itoigawa

Koinuma

et al. 2021

Molecular Biology and Evolution

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Acidic chitinase (Chia) digests the chitin of insects in the omnivorous stomach and the chitinase activity in carnivorous Chia is significantly lower than that of the omnivorous enzyme. However, mechanistic and evolutionary insights into the functional changes in Chia remain unclear. Here we show that a noninsect-based diet has caused structural and functional changes in Chia during the course of evolution in Carnivora. By creating mouse-dog chimeric Chia proteins and modifying the amino acid sequences, we revealed that F214L and A216G substitutions led to the dog enzyme activation. In 31 Carnivora, Chia was present as a pseudogene with stop codons in the open reading frame (ORF) region. Importantly, the Chia proteins of skunk, meerkat, mongoose, and hyena, which are insect-eating species, showed high chitinolytic activity. The cat Chia pseudogene product was still inactive even after ORF restoration. However, the enzyme was activated by matching the number and position of Cys residues to an active form and by introducing five meerkat Chia residues. Mutations affecting the Chia conformation and activity after pseudogenization have accumulated in the common ancestor of Felidae due to functional constraints. Evolutionary analysis indicates that Chia genes are under relaxed selective constraint in species with noninsect-based diets except for Canidae. These results suggest that there are two types of inactivating processes in Carnivora and that dietary changes affect the structure and activity of Chia.

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“…Various Chia has been reported in mammals and birds, while mouse Chia has been studied the most extensively so far [8,[21][22][23][24]52]. Recently, Du et al reported an increased yield of (GlcNAc) 2 by recombinant mouse Chia produced in Pichia pastris using industrial and agricultural applications [53].…”

Section: Discussionmentioning

confidence: 99%

Crab-Eating Monkey Acidic Chitinase (CHIA) Efficiently Degrades Chitin and Chitosan under Acidic and High-Temperature Conditions

et al. 2022

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Chitooligosaccharides, the degradation products of chitin and chitosan, possess anti-bacterial, anti-tumor, and anti-inflammatory activities. The enzymatic production of chitooligosaccharides may increase the interest in their potential biomedical or agricultural usability in terms of the safety and simplicity of the manufacturing process. Crab-eating monkey acidic chitinase (CHIA) is an enzyme with robust activity in various environments. Here, we report the efficient degradation of chitin and chitosan by monkey CHIA under acidic and high-temperature conditions. Monkey CHIA hydrolyzed α-chitin at 50 °C, producing N-acetyl-D-glucosamine (GlcNAc) dimers more efficiently than at 37 °C. Moreover, the degradation rate increased with a longer incubation time (up to 72 h) without the inactivation of the enzyme. Five substrates (α-chitin, colloidal chitin, P-chitin, block-type, and random-type chitosan substrates) were exposed to monkey CHIS at pH 2.0 or pH 5.0 at 50 °C. P-chitin and random-type chitosan appeared to be the best sources of GlcNAc dimers and broad-scale chitooligosaccharides, respectively. In addition, the pattern of the products from the block-type chitosan was different between pH conditions (pH 2.0 and pH 5.0). Thus, monkey CHIA can degrade chitin and chitosan efficiently without inactivation under high-temperature or low pH conditions. Our results show that certain chitooligosaccharides are enriched by using different substrates under different conditions. Therefore, the reaction conditions can be adjusted to obtain desired oligomers. Crab-eating monkey CHIA can potentially become an efficient tool in producing chitooligosaccharide sets for agricultural and biomedical purposes.

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Acidic mammalian chitinase gene is highly expressed in the special oxyntic glands of Manis javanica

Cited by 14 publications

References 36 publications

Expression Profile of the Digestive Enzymes of Manis javanica Reveals Its Adaptation to Diet Specialization

Expression Profile of the Digestive Enzymes of Manis javanica Reveals Its Adaptation to Diet Specialization

Noninsect-Based Diet Leads to Structural and Functional Changes of Acidic Chitinase in Carnivora

Crab-Eating Monkey Acidic Chitinase (CHIA) Efficiently Degrades Chitin and Chitosan under Acidic and High-Temperature Conditions

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