Search results
Results from the WOW.Com Content Network
IgE may have evolved as a defense to protect against venoms. [6] [7] [8] IgE also has an essential role in type I hypersensitivity, [9] which manifests in various allergic diseases, such as allergic asthma, most types of sinusitis, allergic rhinitis, food allergies, and specific types of chronic urticaria and atopic dermatitis.
The high-affinity IgE receptor, also known as FcεRI, or Fc epsilon RI, is the high-affinity receptor for the Fc region of immunoglobulin E (IgE), an antibody isotype involved in allergy disorders and parasite immunity. FcεRI is a tetrameric receptor complex that binds Fc portion of the ε heavy chain of IgE. [1]
CD23 is known to have a role of transportation in antibody feedback regulation. Antigens which enter the blood stream can be captured by antigen specific IgE antibodies. The IgE immune complexes that are formed bind to CD23 molecules on B cells, and are transported to the B cell follicles of the spleen.
In IgG, IgA and IgD antibody isotypes, the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains; IgM and IgE Fc regions contain three heavy chain constant domains (C H domains 2–4) in each polypeptide chain.
2205 14125 Ensembl ENSG00000179639 ENSMUSG00000005339 UniProt P12319 P20489 RefSeq (mRNA) NM_002001 NM_010184 RefSeq (protein) NP_001992 NP_034314 Location (UCSC) Chr 1: 159.29 – 159.31 Mb Chr 1: 173.05 – 173.05 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide, also known as FCER1A, is a protein which in humans ...
Mechanism of class-switch recombination that allows isotype switching in activated B cells. Immunoglobulin class switching, also known as isotype switching, isotypic commutation or class-switch recombination (CSR), is a biological mechanism that changes a B cell's production of immunoglobulin from one type to another, such as from the isotype IgM to the isotype IgG. [1]
In 2013, the Temporal Model of human IgE and IgG function was proposed. [15] This model suggests that IgG3 (and IgE) appear early in a response. The IgG3, though of relatively low affinity, allows IgG-mediated defences to join IgM-mediated defences in clearing foreign antigens. Subsequently, higher affinity IgG1 and IgG2 are produced.
Each heavy chain has two regions: a constant region (which is the same for all immunoglobulins of the same class but differs between classes).. Heavy chains γ, α and δ have a constant region composed of three tandem (in a line next to each other) immunoglobulin domains but also have a hinge region for added flexibility.