Chitinase, Acidic (CHIA) ELISA Kits

Human Chitinase, Acidic (CHIA) interaction partners

1. rs10494132 polymorphism of CHIA might be a risk factor for asthma.

2. we showed that M at the position 61 is highly conserved in the many mammals other than orangutan and humans. In addition, introduction of M61R and M61I to WT mouse AMCase lead to a significant reduction of its chitinolytic activity. Taken together, our present and previous data by Seibold et al. (2009) indicate that G339T (R61M) in humans is associated with asthma protection in the fashion of gain of function

3. This is the first report on the association between low-frequency and common variants in the chitinases-related genes CHIA and CHI3L1 with the intensity of specific IgE to ABA-1 in a population naturally exposed to Ascaris and with Bet v 1 in a Swedish population.

4. These data provide the experimental evidence that telomere shortening and related inflammatory proteins are associated with human IgAN, and it could be a new direction for the disease progression study.

5. loss of acidic chitinase expression is a promising marker for corpus atrophy

6. results showed that the expression of AMCase and CHIT-1 were differently modulated in monocyte macrophages at different stage of maturation. The behavior of these two active chitinase suggests that in the immune response their role is complementary.

7. study demonstrated genetic associations between chitinase gene variants and lung function level and rate of decline in chronic obstructive pulmonary disease patients from the Lung Health Study; also functional effect of the rs3818822 polymorphism on AMCase levels and activity was demonstrated

8. increased chitinolytic activity in nasal polyps

9. Report increased CSF chitinase levels in patients with neuromyelitis optica and relapsing remitting multiple sclerosis.

10. A ten base pair insertion in the second exon in the 5'UTR region of the AMCase gene may modify the gene expression and thus may affect the severity of asthma.

11. AMCase and eotaxin-3 may be important mediators in the pathogenesis of nasal polyps. The increased AMCase and eotaxin-3 might lead to nasal polyp formation and growth.

12. Results showed the presence of CHIT1 and AMCase mRNA in gastric mucosa and the correlation with the presence of H. pylori was significant only for CHIT1 but not for AMCase expression.

13. Environmental exposure to fungi does not modify the effect of CHIA SNPs on severe asthma exacerbations

14. The levels of expression of AMCase and chitotriosidase mRNAs and proteins were increased in allergic turbinate mucosa compared with normal turbinate mucosa.

15. Our study found no associations between single nucleotide polymorphisms in the genes CHIT1, CHIA, and CHI3L1 and asthma, changes in lung physiology, or allergy-related phenotypes in subjects with mild-to-moderate asthma

16. expressed in exaggerated quantities in human asthma

17. human AMCase has only one pH optimum for k(cat)/K(m) between pH 4 and 5. Steady state kinetics shows that human AMCase has "low" intrinsic transglycosidase activity, which leads to the observation of apparent substrate inhibition.

18. results establish a significant association of CHIA with atopic asthma and serum total IgE levels in the Indian population

19. lung epithelial cells secrete AMCase via an EGFR-dependent pathway that is activated by ADAM17 and mediates its effects via Ras.

20. The three-dimensional (3D) model of the human acidic mammalian chitinase (hAMCase) was constructed based on the crystal structure of the human chitotriosidase (EC 3.2.1.44, PDB code 1HKK) by using InsightII/Homology module.

Mouse (Murine) Chitinase, Acidic (CHIA) interaction partners

1. The results indicate that mouse AMCase catalyzes hydrolysis as well as transglycosylation and suggest that this enzyme can play a novel role under physiological conditions in peripheral tissues, such as the lungs.

2. we showed that M at the position 61 is highly conserved in the many mammals other than orangutan and humans. In addition, introduction of M61R and M61I to WT mouse AMCase lead to a significant reduction of its chitinolytic activity. Taken together, our present and previous data by Seibold et al. (2009) indicate that G339T (R61M) in humans is associated with asthma protection in the fashion of gain of function

3. AMCase-deficient mice exhibit premature morbidity and mortality, concomitant with accumulation of environmentally derived chitin polymers in the airways and expression of pro-fibrotic cytokines. Over time, these mice develop spontaneous pulmonary fibrosis.

4. Data show that acidic mammalian chitinase (AMCase) functions as a critical initiator of protective type 2 responses to intestinal nematodes, but is largely dispensable for allergic responses in the lung.

5. AMCase expression was significantly decreased in experimental autoimmune encephalitis mice compared to PBS-controls.

6. Protein A-mouse acidic mammalian chitinase-V5-His expressed in periplasmic space of Escherichia coli possesses chitinase functions comparable to CHO-expressed protein.

7. AMCase mRNA is a major transcript in mouse stomach acting as a digestive enzyme that breaks down polymeric chitin and as part of the host defense against chitin-containing pathogens in the gastric contents.

8. Although exposure to allergen stimulates the expression of AMCase and increased chitinolytic activity in murine airways, the overexpression or inhibition of AMCase exerts only a subtle impact on AAD.

9. findings show that acidic mammalian chitinase 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

10. AMCase provides the first positive molecular marker of distal Clara cell secretory protein-expressing cells under these conditions.

11. lung epithelial cells secrete AMCase via an EGFR-dependent pathway that is activated by ADAM17 and mediates its effects via Ras.