Expression of Chitinases in Hypertrophied Adenoids of Children

Heo, Kyung Wook; Hur, Dae Young; Park, Seong Kook; Yang, Young Il; Kwak, Hyun Ho; Kim, Tae Yong

doi:10.1177/0194599811410656

Cited by 7 publications

(7 citation statements)

References 20 publications

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“…Elevated or reduced AMCase levels have been reported in numerous diseases such as asthma, allergic inflammation, ocular allergy, dry eye syndrome, stomach cancer, adenoid hypertrophy, conjunctivitis, neuromyelitis, gastritis, or nasal polyp formation (Zhu et al 2004; Reese et al 2007; Bucolo et al 2008; Seibold et al 2008; Cozzarini et al 2009; Musumeci et al 2009; Park et al 2009; Bucolo et al 2011; Correale and Fiol 2011; Heo et al 2011; Nookaew et al 2013). In addition, AMCase is an important downstream effector of interleukin-13 stimulation in Th2 helper cell-mediated immune responses to pathogens, parasites and ovalbumin (Zhu et al 2004; Hartl et al 2009).…”

Section: Discussionmentioning

confidence: 99%

Loss and Gain of Human Acidic Mammalian Chitinase Activity by Nonsynonymous SNPs

et al. 2016

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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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Section: Discussionmentioning

confidence: 99%

Loss and Gain of Human Acidic Mammalian Chitinase Activity by Nonsynonymous SNPs

et al. 2016

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“…In fact, the role of LPR in the presence and detectability of pepsinogen in the middle ear cavity and surface of adenoids samples is controversial. The “reverse hypothesis” considered that pepsinogen spreads from serum, becomes concentrated in the middle ear cavity, and flows toward adenoid tissues through the nasopharynx and eustachian tube . However, this presumption is difficult to address using empirical methods.…”

Section: Discussionmentioning

confidence: 99%

Role of pepsin and pepsinogen: Linking laryngopharyngeal reflux with otitis media with effusion in children

Luo

Yang²,

Sheng

et al. 2014

The Laryngoscope

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“…To our knowledge, no study has examined the effect of adenostonsillectomy on markers of airway inflammation; we chose to explore chitinases given previous, separate findings linking them to both asthma and adenotonsillectomy (14,16). In this study, we have demonstrated that asthma control and healthcare utilization significantly improve after adenotonsillectomy and that this improvement is associated with a decrease in chitinase activity in the circulation that is not evident in children without asthma.…”

Section: Discussionmentioning

confidence: 99%

“…There are two major chitinases in humans; chitotriosidase is a true enzyme with the ability to hydrolyze chitin, while YKL-40 is a chitinase-like protein, which has the ability to bind to chitin but not to degrade it (13). The enzymatically active chitinase, chitotriosidase (CHIT1) is overexpressed in adenoid tissue of children undergoing adenotonsillectomy with concurrent chronic rhinosinusitis, otitis media with effusion, and allergic rhinitis compared to subjects without concomitant upper airway disease (14). Additionally, proteins in the chitinase family have been demonstrated as markers of the systemic component of asthmatic disease.…”

Section: Introductionmentioning

confidence: 99%

Improvement in asthma control and inflammation in children undergoing adenotonsillectomy

Levin

Gagnon

et al. 2013

Pediatr Res

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Background Observational studies suggest that asthma control improves after adenotonsillectomy, but longitudinal studies that correlate the effect of the procedure on the levels of biomarkers associated with airway inflammation are limited. Methods We conducted a longitudinal, observational study on pediatric patients, both with and without asthma, undergoing adenotonsillectomy. Asthma Control Test (ACT) scores and chitinase activity in the circulation were measured at time of surgery and at 6-month follow-up. Results 66 children with asthma and 64 control subjects were enrolled. Mean ACT scores improved by 3 points (p< 0.001) after 6 months. 85% of children with poorly-controlled asthma demonstrated an increase in ACT score of at least 3 points or a decrease in Emergency Department/Urgent Care visits, oral corticosteroid courses, or rescue short acting bronchodilator usage. Chitinase activity decreased significantly in asthmatics who improved (p< 0.01). Higher chitinase activity levels at baseline were associated with improved asthma control following surgery (p< 0.01). Conclusions In children with high pre-operative circulating chitinase activity levels, asthma control and healthcare utilization were significantly improved after adenotonsillecotmy. Chitinase activity decreased after surgery in children with improved control. This suggests that adenotonsillectomy modulates chitinase activity, affecting airway inflammation and improving airway disease.

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Expression of Chitinases in Hypertrophied Adenoids of Children

Abstract: The findings suggest that chitin-containing pathogens or dysregulated immune responses to them in the hypertrophied adenoids of children could be factors contributing to CRS, OME, and AR via AMCase or ChT overexpression.

Cited by 7 publications

References 20 publications

Loss and Gain of Human Acidic Mammalian Chitinase Activity by Nonsynonymous SNPs

Loss and Gain of Human Acidic Mammalian Chitinase Activity by Nonsynonymous SNPs

Role of pepsin and pepsinogen: Linking laryngopharyngeal reflux with otitis media with effusion in children

Improvement in asthma control and inflammation in children undergoing adenotonsillectomy

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