Abstract |
Allergic responses at the level of the respiratory system are mostly mediated by IgE-dependent mechanisms. The first selective anti-IgE therapy, a recombinant humanized monoclonal anti-IgE antibody(rhuMAb-E25), binds with high affinity to the Fc epsilon RI receptor binding site on IgE, thereby reducing the amount of free IgE available to bind to Fc epsilon RI receptors on mast cells and basophils. In addition, administration of rhuMAb-E25 indirectly reduces Fc epsilon RI receptor density on cells involved in allergic responses. rhuMAb-E25 has been shown to reduce allergic responses in atopic individuals and to improve symptoms and reduce rescue medication and corticosteroid use in patient with allergic asthma. The clinical effectiveness of rhuMAb-E25 supports the central role of IgE in allergic reaction and the viability of anti-IgE therapy as an effective immunological intervention for allergic asthma.
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Authors | Masanori Nishikawa, Takeshi Matsuse |
Journal | Nihon rinsho. Japanese journal of clinical medicine
(Nihon Rinsho)
Vol. 60
Issue 3
Pg. 591-7
(Mar 2002)
ISSN: 0047-1852 [Print] Japan |
PMID | 11904978
(Publication Type: English Abstract, Journal Article, Review)
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Chemical References |
- Anti-Asthmatic Agents
- Antibodies, Monoclonal
- Receptors, IgE
- rhuMAb-E25
- Immunoglobulin E
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Topics |
- Animals
- Anti-Asthmatic Agents
(administration & dosage)
- Antibodies, Monoclonal
(administration & dosage)
- Asthma
(immunology, therapy)
- Humans
- Immunoglobulin E
(immunology)
- Mice
- Randomized Controlled Trials as Topic
- Receptors, IgE
(immunology)
- Treatment Outcome
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