3.4.22.65: peptidase 1 (mite)
This is an abbreviated version!
For detailed information about peptidase 1 (mite), go to the full flat file.
Word Map on EC 3.4.22.65
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3.4.22.65
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allergic
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asthma
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ige
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dermatophagoides
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pteronyssinus
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children
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home
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asthmatic
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atopic
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farinae
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airway
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indoor
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immunotherapy
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mattress
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bronchial
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rhinitis
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inhale
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prick
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allergen-specific
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floor
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carpet
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bedroom
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dermatitis
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humid
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hyperresponsiveness
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airborne
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household
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houses
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cockroach
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aeroallergens
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vacuum
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wheeze
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house-dust
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ige-binding
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cleaner
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ras
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blomia
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anti-der
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allergen-induced
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rhinoconjunctivitis
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component-resolved
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mite-induced
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radioallergosorbent
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diagnostics
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hdm-induced
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hypoallergenic
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pharmacology
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nonatopic
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medicine
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wheal
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immunocap
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dander
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skin-prick
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drug development
- 3.4.22.65
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allergic
- asthma
- ige
- dermatophagoides
- pteronyssinus
- children
-
home
-
asthmatic
-
atopic
- farinae
- airway
-
indoor
-
immunotherapy
-
mattress
- bronchial
- rhinitis
-
inhale
-
prick
-
allergen-specific
-
floor
-
carpet
-
bedroom
- dermatitis
-
humid
-
hyperresponsiveness
-
airborne
-
household
-
houses
- cockroach
-
aeroallergens
-
vacuum
-
wheeze
-
house-dust
-
ige-binding
-
cleaner
- ras
- blomia
-
anti-der
-
allergen-induced
-
rhinoconjunctivitis
-
component-resolved
-
mite-induced
-
radioallergosorbent
- diagnostics
-
hdm-induced
-
hypoallergenic
- pharmacology
-
nonatopic
- medicine
-
wheal
-
immunocap
-
dander
-
skin-prick
- drug development
Reaction
broad endopeptidase specificity =
Synonyms
allergen Der f 1, allergen Der f1, allergen Der p, allergen Der p 1, allergen Der p1, CO1.073, Der f 1, Der f1, Der p 1, Der p 7, Der p1, dust mite allergen Der p 7, dust mite peptidase allergen Der p 1, house dust mite allergen, house dust mite allergens, major house dust mite allergen, mite allergen, mite major group 1 allergens, pro-Der f1, ProDer f 1, ProDer p 1
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General Information
General Information on EC 3.4.22.65 - peptidase 1 (mite)
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evolution
physiological function
additional information
enzyme Der p 1 is a cysteine protease from the papain family
evolution
mannosylation is a unique feature of the allergens within the cysteine protease family of enzymes, e.g. Der 1 p, papain, and bromelain, while non-allergens of the family, e.g. calpain, and cysteine protease B do not show mannosylation in their carbohydrate patterns, staphopain B is also a cysteine protease protein, like Der p 1, but is an amannosylated antigen
Der p 7 elicits strong IgE antibody and T-cell responses in mite allergic patients. Sensitization to house dust mite allergens is strongly correlated with asthma. The allergen function may contribute to allergenicity, e.g. the protease activity of Group 1 mite allergens, and the interaction with the innate immune system by Group 2 mite allergens
physiological function
the isozymes have allergenic potential in humans
physiological function
high enzyme concentration in mites faecal pellets can be airborne and, when inhaled, can cause perennial rhinitis and bronchial asthma in humans
physiological function
sinonasal epithelial exposure to house dust mite antigen enzyme Der p 1 decreases expression of tight junction proteins, representing a potential mechanism for increased permeability and presentation of antigens across the sinonasal epithelial layer. Enzyme Der p 1-exposed human sinonasal cells show a marked decrease in transepithelial resistance when compared to control cells, with decreased expression of tight junction proteins claudin-1 and junction adhesion molecule-A (JAM-A). Epithelial permeability is highly dependent upon the integrity of tight junctions, cell-cell adhesion complexes located at the apical aspect of the lateral membrane of polarized epithelial cells. Importance of Der p 1 cysteine protease activity directed against airway epithelia
physiological function
stimulation with natural Der p 1 causes an increase in thymic stromal lymphopoietin, TSLP, cytokine secretion by human lung epithelia in a carbohydrate-dependent manner. TSLP may drive denditic cell maturation in support of allergic hypersensitivity reactions
physiological function
the enzyme is is the primary activator of Der p 3, Der p 6 and Der p 9 the proteolytic allergens produced by the house dust mite Dermatophagoides pteronyssinus. Der p 1 in either its recombinant formor in the natural context of house dustmite extracts specifically cleaves all zymogens, thus establishing its role as a major activator of both mite cysteine and serine proteases
physiological function
Der p1 activates the human receptor mas-related G-protein-coupled receptor X1 and the mouse homolog mas-related G-protein-coupled receptor C11. Der p1 also induces the release of IL-6 from heterologous cells expressing mas-related G-protein-coupled receptor X1
the Group 7 as well as the Group 2 mite allergens are structurally similar to different proteins in the TLR pathway
additional information
activation mechanism analysis of the two other serine proteases, Der p 6 (chymotrypsin-like) and Der p 9 (collagenase)zymogen by mite protease Der p 1, overview
additional information
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activation mechanism analysis of the two other serine proteases, Der p 6 (chymotrypsin-like) and Der p 9 (collagenase)zymogen by mite protease Der p 1, overview
additional information
binding properties of in tobacco plant-produced I-rDer p 1 versus the IgE of patients sera are comparable to those obtained on Der p 1 preparation immobilized on a microarray
additional information
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binding properties of in tobacco plant-produced I-rDer p 1 versus the IgE of patients sera are comparable to those obtained on Der p 1 preparation immobilized on a microarray
additional information
Dermatophagoides farinae allergen Der f1 is one of the most important indoor allergens associated with allergic diseases in humans
additional information
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Dermatophagoides farinae allergen Der f1 is one of the most important indoor allergens associated with allergic diseases in humans
additional information
the enzyme is a group 1 mite allergen
additional information
the enzyme is bound by the mannose receptor of dendritic cells, the recombinant enzyme binds stronger due to its higher degree of mannans compared to the native enzyme