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Интенсивно гликозилированные экстрацеллюлярные участки гликофоринов содержат большое количество сиаловых кислот, придающих мембране эритро-цитов отрицательный заряд. Это обеспечивает взаимное отталкивание эритро-цитов, препятствует их агрегации, повышает их текучесть в кровеносных сосу-дах и капиллярах.
Гликофорины связаны с другими структурами эритроцитной мембраны: про-теином полосы 3, Rh-ассоциированным гликопротеином и др. Доказательством тому является отсутствие на гликофориндефицитных эритроцитах антиге-нов Wr b системы Diego и Duclos (Issitt и соавт. [116], Reid [198], Schmidt и со-авт. [225]). Антиген Duclos был включен в систему Rh (и получил обозначение Rh38), однако позднее был выведен из нее (Daniels [56], Habibi и соавт. [89]).
Гликофорины присутствуют исключительно на клетках эритроидного ряда, начиная с ранних предшественников эритроцитов (Bony и соавт. [30], Daniels
К соавт. [59]). Полагают, что они предохраняют эритроциты от лизиса эндоген-ным комплементом, поскольку препятствуют связыванию компонентов С5b −7.
Установлено, что определенные типы гликофорина могут служить биологи-ческим мостом, по которому в силу химического сродства возбудитель малярии Plasmodium falciparum проникает в эритроцит (Hadley и соавт. [90], Mitchell и соавт. [164], Pasvol и соавт. [183], Sim и соавт. [228]). Другие типы гликофорина недоступны для этого паразита, что обеспечивает невосприимчивость к малярии.
экспериментах in vitro показано, что клетки с пониженным содержани-ем гликофорина А и В (En a −, S −s −U −), а также обработанные трипсином по-ражаются малярийным плазмодием значительно реже (Hadley и соавт. [90]). Полагают, что повышенная частота фенотипа S −s −U − среди жителей энде-мичных по малярии зон является следствием естественного отбора: индивиды S −s −U − имели преимущество, поскольку оказались более устойчивыми к инва-зии, чем лица, имеющие другой фенотип.
Описаны уропатогенные штаммы Escherichia coli, вызывающие агглютина-
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цию эритроцитов М +. Таким образом, М-несущие гликофорины адсорбируют (I этап нейтрализации) продукты жизнедеятельности указанного штама кишеч-ной палочки.
Отмечена способность гликофоринов взаимодействовать с бактериальны-ми токсинами, гемолизирующими эритроциты (гемолизирующие штаммы Escherichia coli, Vibrio cholerae).
Гены GYPA, GYPB и GYPE имеют высокую степень гомологии, тем не менее некоторые особенности их строения позволили сформулировать гипотезу их филогенеза. Высказано предположение (Daniels [56]), что первым в эволюции человека сформировался ген GYPA. Второй ген, GYPB, возник позднее в резуль-тате дупликации GYPA, а локус GYPE произошел вследствие удвоения GYPB.
Интересная деталь: ген GYPA обнаружен у всех без исключения приматов, GYPB – только у некоторых высших обезьян: шимпанзе и горилл. У орангутан-гов и гиббонов ген GYPB отсутствует (Rearden и соавт. [196]). Таким образом, имеются некоторые основания полагать, что GYPB и GYPE в эволюционном аспекте являются более поздней субстанцией.
Эритроциты некоторых человекообразных обезьян несут антигены, облада-ющие N-подобной серологической активностью. Эритроциты шимпанзе содер-жат N-подобные антигены.
с целом совокупность полиморфных признаков системы MNS представляет собой уникальную модель, позволяющую глубже понять механизм формирова-ния антигенного многообразия тканей человека.
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