Юго-восточноазиатский овалоцитоз
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Разновидность наследственного овалоцитоза, известная как Юго-восточноазиатский овалоцитоз, встречается среди населения южной части Тихого океана. Эту патологию рассматривают как эволюционно сложившую-ся форму защиты от малярии. Овалоцитоз развивается в результате делеции 27 пар нуклеотидов в гене протеина полосы 3. При этом синтезируется особый ва-риант протеина с выпадением аминокислот в позиции 400–408 в участке свя-зывания N-терминального и первого трансмембранного доменов. Такой вари-ант протеина полосы 3 (вариант Мемфис I) неактивен в отношении транспор-та анионов. Несмотря на высокую частоту указанной делеции среди жителей Океании, не было найдено ни одного индивида, гомозиготного по этой делеции. Есть основания полагать, что гомозиготность по любой из мутаций, инактиви-рующей протеин полосы 3, является летальной.

 

Booth и соавт. [15], Daniels и соавт. [39], Smythe и соавт. [154] установили, что у жителей Меланезии снижена экспрессия многих эритроцитарных антиге-нов: Di b, Wr b (системы Diegо); S, s, U, En a (системы MN); D, C, e (системы Rh); Kp b (системы Kell); Jk a, Jk b (системы Кидд); Xg a (системы XG); Sc1 (системы Scianna); LW (системы Landsteiner – Wiener); Ge2, Ge3, Ge4 (системы Gerbich); I T, I F (системы Ii).

 

Супрессия перечисленных антигенов может быть результатом поломок в трансмембранных доменах протеина полосы 3, сказывающихся на интеграции различных мембранных структур. Уменьшение количества вещества D, C, c, E, LW, S, s и U происходит в связи с замедлением транспорта этих веществ

 

с поверхности мембраны (Beckmann и соавт. [12]). Могут иметь место боко-вые разрывы белковых комплексов внутри мембраны и другие дефекты, обу-словленные неполноценным белком полосы 3 (Daniels и соавт. [39], Smythe и

 

соавт. [154]).


 

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Глава 13.

 

Система Cartwright

 

 


Система Cartwright (Картрайт) интересна тем, что носителями составляю-щих ее антигенов являются молекулы ацетилхолинэстеразы (АХЭ). Этот фер-мент участвует в передаче нервного импульса. Импульс передается на воспри-нимающие рецепторы очередного нейрона или мускульной клетки через синапс посредством образования ацетилхолина (АХ), который после проведения им-пульса разлагается АХЭ на холин и уксусную кислоту. Таким образом АХЭ вы-полняет роль биохимического реле, разделяющего нервные импульсы и одно-временно контролирующего состояние системы связи. Острая токсичность фос-форорганических соединений является прямым следствием того, что они явля-ются сильными ингибиторами АХЭ.

 

Ассоциационно-диссоциационная система АХ – АХЭ – АХ является осно-вой иннервации всего организма, включая периферическую (проводниковую) и центральную нервную систему. Благодаря ей нервные импульсы поступают во все ткани организма.

 

275. связи с этим можно высказать предположение о своеобразной иннервации циркулирующих клеток как в норме, так и в состоянии стресса. Стресс охваты-вает весь организм: и стационарные ткани, к которым подходят нервные окон-чания, и циркулирующие в кровотоке клетки, которых нервные окончания не достигают. Наличие АХЭ на эритроцитах, по-видимому, обеспечивает подведе-ние к ним нервного импульса (доведение до эритроцитов стрессового сигнала). Организм как целостная система таким образом доводит сигнал стресса и моби-лизационный импульс до всех тканей, стационарных и подвижных, обеспечивая ответную реакцию всего организма.

 

276. литературе имеются указания на то, что ген ACHE (acetylcholinester-ase) играет определенную роль в гемопоэзе. Аномалии хромосомы 7, где располагается этот ген, часто обнаруживают у пациентов с острым не-лимфоцитарным лейкозом и миелодисплазией, и наиболее частые хромо-сомные нарушения при этих состояниях происходят в 7q22, участке гена

 

ACHE (Kere и соавт., 1989).

 

Lapidot-Lifson и соавт. (1989) связывали аномальный мегакариоцитопо-эз с нарушениями в локусе ACHE, вызванными химиотерапией, облучением или отравлением фосфорорганическими соединениями. Факт влияния АХЭ на мегакариоцитопоэз подтверждают результаты экспериментов на мышах

 

(Patinkin и соавт., 1989).


 

688





Антигены Yt a и Yt b

 

Система Cartwright представлена двумя антигенами: Yt a и Yt b (табл. 13.1). Антитела анти-Yt a, открывающие часто встречающийся антиген Yt a, обнаруже-ны в 1956 г. Eaton и соавт. [12] при проведении пробы на индивидуальную со-вместимость. Через 8 лет Giles и Metaxas [16] описали антитетичный антиген Yt b, встречающийся относительно редко (с частотой ≈ 8 %).

 

       

Таблица 13.1

   

Антигены системы Yt

               

Обозначение

 

Характеристика

              традиционное   ISBT Частота, % Молекулярная основа   Yt a [Yt(a +b −)]   YT1 91,8 His353   Yt ab [Yt(a +b + )]   нет 7,8     Yt b [Yt(a −b + )]   YT2 0,3 Asn353   Yt(a −b −)   нет 0    

 

Нулевой фенотип Yt(a −b −), как и молчащий ген, передаваемый по наслед-ству, в системе Yt неизвестен.

 

Антигенные различия Yt a / Yt b обусловлены заменой гистидина на аспарагин в по-зиции 353 (рис. 13.1). Локусы YT и ACHE (рис. 13.2) не зависят от генов других групп крови. Они расположены на хромосоме 7 в позиции 7q22.1 (Reid, Lomas-Francis [40]).

171989–1991 гг. группа исследователей (Coghlan и соавт., Zelinski и соавт.) опублико-вала данные о возможной сцепленности локусов YT и KEL. Последний, как вскоре выяснилось, так же как и YT, расположен на хромосоме 7. Однако последующие ис-следования не подтвердили существование указанной сцепленности.

 

 

Рис. 13.1. Строение гликопро-

 

теина, несущего антигены Yt.


 

689


 

Рис. 13.2. Организация гена YT (ACHE).

 



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