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Aminopeptidase activity in human nasal mucosa
K Ohkubo1, J N Baraniuk, R Hohman
1Department of Otolaryngology, Nippon Medical School, Tokyo, Japan.
The Journal of Allergy and Clinical Immunology
|November 18, 1998
Summary
This study identified aminopeptidase activities in human nasal mucosa, finding that membrane-bound, puromycin-resistant aminopeptidases are predominant in epithelial and gland cells.
Area of Science:
- Biochemistry
- Immunology
- Rhinology
Background:
- Aminopeptidases play a role in activating bradykinin and degrading inflammatory peptides.
- Understanding aminopeptidase activity in the nasal mucosa is crucial for respiratory health research.
Purpose of the Study:
- To identify and characterize aminopeptidase activities within human nasal mucosa.
- To investigate the localization and regulation of these enzymes in vivo.
Main Methods:
- Fractionation of human nasal mucosa into cytoplasmic (S2) and membrane-rich (P2) components.
- Enzyme assays using specific substrates (leucine-enkephalin, alanine-nitroanilide) and inhibitors (puromycin, bestatin).
- Histochemical (zymography, immunohistochemistry) and biochemical (gel electrophoresis) analyses, alongside in vivo nasal provocation tests.
Main Results:
- The membrane-rich fraction (P2) showed the highest puromycin-resistant aminopeptidase activity.
- Soluble puromycin-resistant aminopeptidase and lower levels of soluble puromycin-sensitive aminopeptidase (PS-Ap) were detected.
- Aminopeptidase activity was localized to epithelial and gland cells, with leucine-AP correlating with glandular exocytosis.
Conclusions:
- The primary aminopeptidase in human nasal epithelium and submucosal glands is membrane-bound and puromycin-resistant.
- A novel soluble puromycin-resistant aminopeptidase was identified.
- These findings contribute to understanding the enzymatic landscape of the nasal mucosa.
