Immunohistochemical demonstration of acidic mammalian chitinase in the mouse salivary gland and gastric mucosa

Goto, Marie; Fujimoto, Wakako; Nio, Junko; Iwanaga, Toshihiko; Ḱawasaki, Takao

doi:10.1016/s0003-9969(03)00150-x

Cited by 18 publications

(21 citation statements)

References 16 publications

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“…Glutamine synthase mRNA is also found in this region of the stomach, in a cell layer just beneath that of the chitotriosidase-expressing cells (Figures 5G and 5H). In agreement with the results of Suzuki et al (2002) and Goto et al (2003), we found that AMCase is expressed in the glandular portion of the stomach, at the bottom of the gastric glands in chief cells (Figures 5D and 5E). The pyloric glands in the antrum of the stomach show no expression of the chitinases.…”

Section: Resultssupporting

confidence: 91%

Marked Differences in Tissue-specific Expression of Chitinases in Mouse and Man

Boot

Bussink

Verhoek

et al. 2005

J Histochem Cytochem.

123

138

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S U M M A R Y Two distinct chitinases have been identified in mammals: a phagocyte-specific enzyme named chitotriosidase and an acidic mammalian chitinase (AMCase) expressed in the lungs and gastrointestinal tract. Increased expression of both chitinases has been observed in different pathological conditions: chitotriosidase in lysosomal lipid storage disorders like Gaucher disease and AMCase in asthmatic lung disease. Recently, it was reported that AMCase activity is involved in the pathogenesis of asthma in an induced mouse model. Inhibition of chitinase activity was found to alleviate the inflammation-driven pathology. We studied the tissue-specific expression of both chitinases in mice and compared it to the situation in man. In both species AMCase is expressed in alveolar macrophages and in the gastrointestinal tract. In mice, chitotriosidase is expressed only in the gastrointestinal tract, the tongue, fore-stomach, and Paneth cells in the small intestine, whereas in man the enzyme is expressed exclusively by professional phagocytes. This species difference seems to be mediated by distinct promoter usage. In conclusion, the pattern of expression of chitinases in the lung differs between mouse and man. The implications for the development of anti-asthma drugs with chitinases as targets are discussed.

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Section: Resultssupporting

confidence: 91%

Marked Differences in Tissue-specific Expression of Chitinases in Mouse and Man

Boot

Bussink

Verhoek

et al. 2005

J Histochem Cytochem.

123

138

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“…Only 13/25 (patients 5,6,12,13,15,[17][18][19][20][22][23][24][25] showed signs of reflux esophagitis associated with chronic gastritis. Eight patients (3, 7-9, 11, 14, 16, 21) showed antral gastritis, gastric micropolyposis and mucosal gastric hypertrophy, and 9 patients (patients 11, 13, 16-18, 20, 21, 24, 25) resulted positive at H. pylori urease test and at 13 C-urea breath test.…”

Section: Resultsmentioning

confidence: 98%

“…To date, however, its function is obscure [9] . AMCase has also been found in the mouse and rat stomach where it has been shown at the cellular level (immunohistochemically) and at the level of RNA expression [9,23,24] .…”

Section: Introductionmentioning

confidence: 95%

Human Gastric Juice Contains Chitinase That Can Degrade Chitin

et al. 2007

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Chitin digestion by humans has generally been questioned or denied. Only recently chitinases have been found in several human tissues and their role has been associated with defense against parasite infections and to some allergic conditions. In this pilot study we tested the gastric juices of 25 Italian subjects on the artificial substrates 4-methylumbelliferyl-β-D-N,N’,diacetylchitobiose or/and fluorescein isothiocyanate (FITC) chitin to demonstrate the presence of a chitinase activity. Since this chitinase activity was demonstrated at acidic pH, it is currently referred to acidic mammalian chitinase (AMCase). AMCase activity was present in gastric juices of twenty of 25 Italian patients in a range of activity from 0.21 to 36.27 nmol/ml/h and from 8,881 to 1,254,782 fluorescence emission (CPS), according to the used methods. In the remaining five of 25 gastric juices, AMCase activity was almost absent in both assay methods. An allosamidine inhibition test and the measurement at different pH values confirmed that this activity was characteristic of AMCase. The absence of activity in 20% of the gastric juices may be a consequence of virtual absence of chitinous food in the Western diet.

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“…Recently, two functional chitinases, chitotriosidase and acidic mammalian chitinase (AMCase), have been identified in mammalian species [2,3,15]. Human and mouse AMCase having a molecular mass of 50 kDa is secreted from the stomach and salivary gland into the gut lumen and activated under acidic conditions at an optimal pH 2 [2,8]. AMCase-like proteins have also been found in the stomach of chickens and frogs [6,11,18].…”

mentioning

confidence: 99%

“…Proteins were then transferred onto a polyvinylidene difluoride membrane (Hybond-P; Amersham, Buckinghamshire, UK). The membrane was subsequently blocked with 5% dried skimmed milk in 0.01 M phosphate-buffered saline (pH 7.2) containing 0.05% Tween 20 (PBS-T), and then incubated with affinity-purified rabbit anti-bovine gut chitinase antibody (90 ng/ml) diluted in PBS-T [6,8]. The bound antibody was visualized using peroxidase-labeled anti-rabbit IgG (Bio-Rad) and an enhanced chemiluminescence system (Amersham).…”

mentioning

confidence: 99%

Quantitative Changes in Serum Concentration of Bovine Gut Chitinase in Theileria Infection

Fujimoto

Kimura

Suzuki

et al. 2004

The Journal of Veterinary Medical Science

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ABSTRACT. Bovine gut chitinase is exclusively produced in the liver and secreted into the blood. In the present study, we established a semi-quantitative method by Western blot analysis for measurement of the chitinase content in blood and examined its alteration during postnatal development and experimental infection with hemoprotozoan parasite in cattle. Its serum levels from 1 week to 1 year of age showed a significant increase only in 3-4-month-old group. The plasma concentration of the gut chitinase was not changed during acute inflammation caused by lipopolysaccharide but increased gradually after a Theileria injection and peaked at 52 days post-infection. It appears that the increase in the blood chitinase levels might be a defensive response in cattle against protozoan infection. KEY WORDS: bovine serum, chitinase, Theileria sergenti.

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Immunohistochemical demonstration of acidic mammalian chitinase in the mouse salivary gland and gastric mucosa

Cited by 18 publications

References 16 publications

Marked Differences in Tissue-specific Expression of Chitinases in Mouse and Man

Marked Differences in Tissue-specific Expression of Chitinases in Mouse and Man

Human Gastric Juice Contains Chitinase That Can Degrade Chitin

Quantitative Changes in Serum Concentration of Bovine Gut Chitinase in Theileria Infection

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