Нуклеозиддифосфаткиназа: особенности взаимодействия с наружной мембраной митохондрий и системой окислительного фосфорилирования тема диссертации и автореферата по ВАК РФ 03.00.04, кандидат биологических наук Воинова, Вера Владимировна

• Воинова, Вера Владимировна
• кандидат биологических наук
• 2009

Оглавление диссертации кандидат биологических наук Воинова, Вера Владимировна

1. Список сокращений.

2. Введение.

3. Обзор литературы.

3.1. Кинетические характеристики и механизм нуклеозиддифосфаткиназной реакции.

3.1.1. Кинетические характеристики нуклеозиддифосфаткиназной реакции.

3.1.2. Роль ионов двухвалентных металлов.Л.

3.1.3. Роль 3' гидроксильной группы рибозы.

3.1.4. Фосфорилированный интермедиат.

3.1.5. Природа переходного состояния нуклеозиддифосфаткиназной реакции.

3.1.6. Альтернативные субстраты и ингибиторы НДФК.

3.2. Физико-химические свойства изоформ НДФК.

3.2.1. Гены, кодирующие НДФК.

3.2.2. Структура НДФК.

3.2.3. Локализация, молекулярная масса и изоэлектрические точки изоформ НДФК.

3.2.4. Локализация НДФК в митохондриях.

3.3. Роль продуктов нуклеозиддифосфаткиназной реакции в метаболизме.

3.4. Вторичные активности НДФК.

3.5. Роль НДФК в регуляции внутриклеточных процессов.

3.5.1. Участие НДФК в регуляции клеточного цикла.

3.5.2. Участие НДФК1пт23 в регуляции процессов дифференциации.

3.5.3. Движение и форма клеток.

3.5.4. Роль НДФК/пт23 в регуляции метастазирования опухолей.

3.5.5. Ген - мутатор Escherichia coli.

3.5.6. Участие НДФК в регуляции программируемой клеточной смерти.

3.5.7. НДФК/и/7225, как фактор регуляции экспрессии генов на уровне транскрипции.

3.5.8. НДФК и сигнальные каскады.

3.6. Регуляция проницаемости наружной мембраны митохондрий.

3.7. Представление о функциональных компартмснтах и роли киназ наружного компартмента митохондрий во внутриклеточном транспорте энергии.

3.7.1. Компартментация метаболитов и функциональное сопряжение, определение понятий.

3.7.2. Компартментация адениловых нуклеотидов в межмембранном пространстве митохондрий во время активности митохондриальной аденилаткиназы.

3.7.3. Функциональное сопряжение между активностью митохондриальной креатинкиназы и системой окислительного фосфорилирования.

3.7.4. Функциональное сопряжение активности киназ, локализованных на внешней поверхности наружной мембраны митохондрий, с окислительным фосфорилированием.

4. Цели и задачи I шел едования.

5. Методы исследования.

5.1. Материалы.

5.2. Выделение митохондрий печени крысы методом дифференциального центрифугирования.

5.3. Полярографический метод регистрации дыхания митохондрий.

5.4. Определение скорости окислительного фосфорилирования, коэффициента дыхательного контроля и активностей НДФК. гсксокиназы и аденилаткиназы полярографическим методом.

5.5. Выделение митохондрий по методу Ноушб и соавт.

5.6. Удаление цитохрома с из митохондрий.

• 5.7. Исследование локализации нмНДФК в наружном компартменте митохондрий.

5.8. Влияние различных веществ на солюбилизацию нмНДФК.

5.9. Определение доли связанной с мембранами активности нмНДФК в ходе хранения препарата митохондрий.

5.10.Получение препарата митохондрий с низким содержанием нмНДФК.

5.11.Полярографические эксперименты в присутствии креатинкиназы.

5.12. Обработка проб после полярографического эксперимента.

5.13.Определение скорости взаимодействия креатинкиназы с CDP.

5.14. Определение времени инкубации проб с хлорной кислотой, необходимого для полной инактивации ферментов.

5.15.Определение степени гидролиза креатинфосфата и ЛТР при обработке проб хлорной кислотой.

5.16.Определение концентрации креатина.

5.17. Определение концентраций нуклеотидов, глюкозо-6-фосфата и креатинфосфата.

5.17.1. . Определение концентрации ADP и CDP.

5.17.2. Определение концентрации глюкозо-6-фосфата, ATP, СТР и креатинфосфата.

5.17.3. Определение концентрации ATP, ADP. AMP, СТР, CDP и UDP на основании коэффициентов их молярного поглощения.

5.17.4. Определение чистоты препаратов ATP, ADP и CDP.

5.18. Исследование взаимодействия дрожжевой НДФК с мембранами митохоидрий.

5.19. Исследование взаимодействия дрожжевой ГК с мембранами митохондрий.

5.20.Обращение солюбилизации нмНДФК добавлением Mg

5.21.Сравнение взаимодействия протеиназ с пмНДФК, перешедшей в раствор, и с компонентами мембран в местах её связывания.

5.22.Влияние рН на прочность взаимодействия нмНДФК с мембранами митохондрий.

5.23. Обращение солюбилизации нмНДФК изменением рН среды хранения.

5.24.Влияние пальмитиновой кислоты на прочность взаимодействия нмНДФК с мембранами митохондрий.

5.2 5. По лучение экстракта белков с поверхности митохондрий для электрофоретических исследований.

5.26.Спектрофотометрическое определение активности гексокиназы и НДФК в сопряженной ферментной системе.

5.27.Электрофорез белков, солюбшгазированных с поверхности митохондрий.

5.27.1. Деионизация растворов.

5.27.2. Изоэ л ектро ф оку сир ов ание.

5.27.3. Нативный электрофорез.

5.27.4. Градиентный электрофорез.

5.27.5. Окрашивание гелей.

5.28.Определение концентрации Mg2+ методом комплексонометрического титрования.

5.29.Определение белка митохондрий.

5.30. Статистическая обработка результатов.

6. Результаты исследования.

6.1. Полярографический метод регистрации скорости дыхания митохондрий.

6.2. Сравнение двух методов выделения митохондрий.

6.3. Исследование локализации нмНДФК в наружном компартменте митохондрий.

6.4. Природа сил взаимодействия нмНДФК с мембранами митохондрий.

6.5. Изучение функционального сопряжения между активностью нмНДФК наружного компартмента митохондрий и окислительным фосфорилированием.

6.5.1. Пригодность КК на роль внешней ADP-потребляющей системы.

6.5.2. Солюбилизация нмНДФК из митохондрий, хранившихся в разных средах.

6.5.3. Определение времени инактивации ферментов.

6.5.4. Определение степени гидролиза КФ и АТР в ходе инкубации проб полярографического опыта с НСЮ4.

6.5.5. Оптимизация метода определения креатина.

6.5.6. Исследование взаимодействия дрожжевой НДФК и дрожжевой ГК с мембранами митохондрий.:.

6.5.7. Полярографические эксперименты в присутствии креатинкиназы.

6.6. Доля активности нмНДФК, функционально сопряженной с окислительным фосфорилированием.

6.7. Влияние 10%-ного декстрана на функциональное сопряжение нмНДФК и митохондриальной аденилаткиназы с окислительным фосфорилированием.

6.8. Обращение солюбилизации нмНДФК в среде с низкой ионной силой добавлением MgCl2.

6.9. Сравнение взаимодействия протеиназ с нмНДФК, перешедшей в раствор, и с компонентами мембраны в местах её связывания.

6.10.Поиск физиологических регуляторов солюбилизации нмНДФК.

6.10.1. Влияние рН на прочность взаимодействия нмНДФК с мембранами митохондрий.

6.10.2. Обратное связывание нмНДФК, солюбилизировавшейся при кислом значении рН.

6.10.3. Влияние различных веществ на прочность связи нмНДФК с мембранами.

6.10.4. Влияние голодания и углеводной диеты на солюбилизацию нмНДФК.

6.11. Исследование однородности нмНДФК наружного компартмента митохондрий.

6.11.1. Оптимизация метода окрашивания геля по активности НДФК.

6.11.2. Нативньтй электрофорез экстракта белков с поверхности митохондрий.

7. Обсуждение результатов.

8. Выводы.

Заключение диссертации по теме «Биохимия», Воинова, Вера Владимировна

8. Выводы

1. Получены доказательства того, что вся НДФК наружного компартмента митохондрий локализована на внешней поверхности наружной митохондриалыюй мембраны.

2. Установлено, что прочность связи нмНДФК с мембранами митохондрий повышается с увеличением ионной силы и рН среды хранения митохондрий, а также в присутствии ионов ]У^2+ и не зависит от присутствия ЭДТА.

3. При изучении функционального сопряжения активности нмНДФК с системой окислительного фосфорилирования установлено, что в присутствии избытка активности мышечной ЮС нмНДФК более эффективно поставляет А1ЭР для системы окислительного фосфорилирования, чем дНДФК и дГК.

4. Установлено, что в функциональном сопряжении с системой окислительного фосфорилирования участвует 22 - 24% активности нмНДФК.

5. Установлено, что солюбилизация из митохондрий нмНДФК, не участвующей в функциональном сопряжении, обратима. В зависимости от условий хранения митохондрий, солюбилизация может быть обращена добавлением ]У^2+ или повышением рН среды хранения.

6. В экстракте белков с поверхности митохондрий присутствуют две фракции, обладающие нуклеозиддифосфаткиназной активностью и различающиеся кажущимися величинами молекулярных масс (132 и 204 кДа) и изоэлектрическими точками (5,1 и 5,5), соответственно.

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