Novel inhibitors of histamine-releasing factor suppress food allergy in a murine model

• Published in: Allergology International Vol. 71; no. 1; pp. 147 - 149
• Main Authors: Kawakami, Yu, Kurosawa, Yasunori, Oltean, Daniela, Espinosa, Lisa Yuko, Kim, Hwan Soo, Lemersal, Ian, Kawakami, Yuko, Okumura, Shigeru, Maruyama, Toshiaki, Kawakami, Toshiaki
• Format: Journal Article
• Language: English; Japanese
• Published: England Elsevier B.V 01.01.2022; JAPANESE SOCIETY OF ALLERGOLOGY; Elsevier
• Subjects: Animals; Anti-Allergic Agents - pharmacology; Antibodies, Monoclonal - pharmacology; Disease Models, Animal; Food Hypersensitivity - immunology; Food Hypersensitivity - metabolism; Food Hypersensitivity - prevention & control; Histamine Release - drug effects; Mice; Mice, Inbred BALB C; Ovalbumin; Peptides - pharmacology; Rabbits; Tumor Protein, Translationally-Controlled 1 - antagonists & inhibitors; Tumor Protein, Translationally-Controlled 1 - immunology; Tumor Protein, Translationally-Controlled 1 - metabolism
• ISSN: 1323-8930; 1440-1592
• DOI: 10.1016/j.alit.2021.07.005

Dear Editor, Histamine-releasing factor (HRF), also known as translationally controlled tumor protein and fortilin, is a highly conserved protein required for fundamental intracellular functions such as proliferation and survival. Since it is secreted during allergic reactions, it is implicated in allergic diseases. Recent studies demonstrated that HRF amplifies allergic inflammation by promoting immunoglobulin (Ig) E-dependent activation of mast cells and basophils in animal models of anaphylaxis, asthma and food allergy. HRF can be present as a monomer and disulfide-linked oligomers. HRF directly binds to a subset of IgE and IgG molecules by interactions between the Fab portion of IgE/IgG and two Ig-binding sites within HRF, i.e., the amino-terminal 19 residues (N19) and the helical domain H3.