mimmunМедицинская иммунологияMedical Immunology (Russia)1563-06252313-741XSPb RAACI10.15789/1563-0625-2006-4-483-500mimmun-463Research ArticleОБЗОРЫREVIEWSИММУНОГЛОБУЛИН А (IgA) И ЕГО РЕЦЕПТОРЫIMMUNOGLOBULIN A (IgA) AND ITS RECEPTORSКлимовичВ. Б.KlimovichV. B.

лаборатория гибридомной технологии

197758, СПетербург, Песочный, д.2, Ленинградская ул., д. 70/4

vklim@sertolovo.ruСамойловичМ. П.SamoilovichM. P.vklim@sertolovo.ruЦентральный научно-исследовательский рентгено-радиологический институт МЗ РФ, Санкт-ПетербургRussian Federation20062207201484483500Copyright © Климович В.Б., Самойлович М.П., 20142014Климович В.Б., Самойлович М.П.Klimovich V.B., Samoilovich M.P.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://www.mimmun.ru/mimmun/article/view/463

Резюме. Общий объем продукции IgA в организме человека составляет 3-5 г в сутки и превышает выработку Ig остальных классов, вместе взятых. IgA представлен в организме девятью структурными вариантами. Его молекулы относятся к двум подклассам, IgA1 и IgA2, второй имеет два аллотипа. В сыворотке крови человека преобладают мономеры IgA1, синтезируемые клетками костного мозга. Лимфоидные ткани, ассоциированные со слизистыми, продуцируют димерные молекулы IgA1 и IgA2. В состав их входит дополнительная полипептидная J-цепь. При переносе через слой эпителия на поверхность слизистой к димерному IgA ковалентно присоединяется внеклеточный участок рецептора полимерных Ig (pIgR), который становится секреторным компонентом, частью молекулы секреторного IgA (sIgA). Основной функцией sIgA является связывание бактерий и вирусов на поверхности слизистых оболочек, препятствующее попаданию патогенов во внутреннюю среду организма (иммунное исключение). При переносе через эпителий IgA может нейтрализовать проникшие в клетки вирусы, а также связывать и выносить на поверхность слизистых, т. е. экскретировать белки и иные антигены. Лейкоцитарный рецептор IgA (FcαRI, CD89) экспрессирован на нейтрофилах, эозинофилах, моноцитах-макрофагах, дендритных и купферовских клетках. Цитоплазматический домен FcαRI лишен активационного ITAM-мотива. Для передачи сигнала используется ассоциированная с FcαRI γ-цепь Fcγ-рецептора, благодаря которой связывание IgA приводит к активации фагоцитоза, эндоцитоза, презентации антигена, синтеза провоспалительных медиаторов и других функций. Рецептор Fcα/μR структурно гомологичен pIgR, способен связывать IgA и IgM, но экспрессируется только на мембране зрелых В-лимфоцитов и макрофагов. Описано взаимодействие IgA с рецепторами асиалогликопротеинов, трансферрина (CD71) и некоторыми другими молекулами, роль которых в иммунной защите и в развитии патологических процессов пока не определена. Работа выполнена при поддержке РФФИ (грант № 05-04-48860).

Abstract. Daily IgA production in human organism comprises 3 to 5 g, thus exceeding total synthesis of other Ig classes. IgA in human body is presented by 9 structural variants. Its molecules belong to two subclasses, IgA1 and IgA2, the latter represented by two allotypes. In human serum, IgA1 monomers predominate, that are produced by the bone marrow cells. Mucosa-associated lymphoid tissues produce dimeric IgA1 and IgA2 molecules containing an accessory polypeptide J-chain. When transported across epithelial layer to the mucosal surface, an extracellular segment of polymeric IgA receptor (pIgAR) is joining the dimeric IgA1, which becomes a ‘secretory’ component being a part cesretory IgA (sIgA) molecule. The main function of sIgA is to bind bacteria and viruses at the mucosal surfaces, thus preventing pathogens to invade the internal spaces of the organism (immune exclusion). If transferred across epithelium, IgA may neutralize the viruses penetrating the cells, like as bind and deliver proteins and other antigens to the mucosal surface. The leukocyte IgA receptor (FcαRI, CD89) is expressed on the neutrophils, eosinophiles, monocytes/macrophages, as well as dendritic and Kupffer cells. The cytoplasmic domain FcαRI is devoid of an activation ITAM motif. To transduce signal, an FcαRI-associated chain of Fcγ receptor is used. Due to this mechanism, IgA binding leads to activation of phagocytosis, endocytosis, antigen presentation, synthesis of proinflammatory mediator and other immune functions. Fcα/μR receptor is a structural homologue of pIgR, and it is able to bind IgA and IgM, being, however, expressed only at the surface of mature B lymphocytes and macrophages. Interaction of IgA with asialoglycoprotein and transferrin (CD71) receptors, like as with some other molecules, that have yet undetermined role in immune defense and development of pathological events.

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The authors declare that there are no conflicts of interest present.