EC Number   |
Natural Substrates |
|---|
   3.4.22.65 | CD23 + H2O |
Der p 1 in addition to being highly immunogenic may up-regulate IgE synthesis by virtue of its ability to cleave CD23 |
| 3.4.22.65 | lung surfactant protein A + H2O |
degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen |
| 3.4.22.65 | lung surfactant protein D + H2O |
degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen |
| 3.4.22.65 | mas-related G-protein-coupled receptor C11 + H2O |
mouse protein |
| 3.4.22.65 | mas-related G-protein-coupled receptor X1 + H2O |
human protein |
| 3.4.22.65 | more |
allergen from Dermatophagoides farinae |
| 3.4.22.65 | more |
Der p 1 is the most immunodominant allergen involved in the expression of dust mite-specific immunoglobulin (Ig)E-mediated hypersensitivity. The proteolytic activity of Der p 1 is a major contributor to its allergenicity. Cysteine protease activity of Der p 1 enhances total IgE production |
| 3.4.22.65 | more |
cysteine protease activity of Der p 1 enhances total IgE production, apart from increasing Der p 1-specific IgE. This allergen may play a central role in destabilizing the micro-environment within target tissues to one that is pro-allergic, and thus aid in the initiation and propagation of the allergic cascade |
| 3.4.22.65 | more |
recombinant Der f 1 activated with L-cysteine reduces the barrier function of the skin in dose- and time-dependent manners. The reduction is dependent on its proteolytic activity |
| 3.4.22.65 | more |
the efficient in vivo responses, including production of IgE and IgG against the highly purified rDer p 1, are dependent on the cysteine protease activity in mice. The three types of rDer p 1 differing in function or structure elicit distinctly different immune responses |
