ΠΠ½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΡΠ΅ Π±Π΅Π»ΠΊΠΈ β ΠΌΠΈΡΠ΅Π½ΠΈ Π΄Π»Ρ ΠΏΠΎΠΈΡΠΊΠ° Π½ΠΎΠ²ΡΡ Π°Π½ΡΠΈΡ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ²
ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ Π²Π΅Π³Π΅ΡΠ°ΡΠΈΠ²Π½ΡΠ΅, ΠΌΠ΅ΡΠ°Π±ΠΎΠ»ΠΈΡΠ΅ΡΠΊΠΈ Π°ΠΊΡΠΈΠ²Π½ΡΠ΅ ΡΠΎΡΠΌΡ Π‘. trachomatis Π½Π° ΡΡΠ΅Π΄Π½Π΅ΠΉ ΡΡΠ°Π΄ΠΈΠΈ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° ΡΠ°Π·Π²ΠΈΡΠΈΡ Π·Π°ΡΠΈΡΠ°ΡΡ ΡΡΠΊΠ°ΡΠΈΠΎΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΎΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°, ΠΈΠ½Π΄ΡΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΡΡΠ°ΡΡΠΎΡΠΏΠΎΡΠΈΠ½ΠΎΠΌ ΠΈ ΡΠ°Π·Π²ΠΈΠ²Π°ΡΡΠ΅Π³ΠΎΡΡ ΠΏΠΎ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠΌΡ ΠΏΡΡΠΈ. ΠΠ° ΡΠ°Π½Π½Π΅ΠΉ ΡΡΠ°Π΄ΠΈΠΈ ΠΆΠΈΠ·Π½Π΅Π½Π½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΡ ΠΈΠ½Π΄ΡΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Π½Π΅ Π½Π°Π±Π»ΡΠ΄Π°Π΅ΡΡΡ, ΡΡΠΎ ΠΏΡΠΈΠ²ΠΎΠ΄ΠΈΡ ΠΊ ΡΠ΅Π·ΠΊΠΎΠΌΡ ΡΠ½ΠΈΠΆΠ΅Π½ΠΈΡ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ … Π§ΠΈΡΠ°ΡΡ Π΅ΡΡ >
- Π‘ΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΠ΅
- ΠΡΠ΄Π΅ΡΠΆΠΊΠ°
- ΠΠΈΡΠ΅ΡΠ°ΡΡΡΠ°
- ΠΡΡΠ³ΠΈΠ΅ ΡΠ°Π±ΠΎΡΡ
- ΠΠΎΠΌΠΎΡΡ Π² Π½Π°ΠΏΠΈΡΠ°Π½ΠΈΠΈ
Π‘ΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΠ΅
- Π‘ΠΠΠ‘ΠΠ Π‘ΠΠΠ ΠΠ©ΠΠΠΠ
- ΠΠΠΠΠ 1. ΠΠΠΠΠ ΠΠΠ’ΠΠ ΠΠ’Π£Π Π«
- 1. 1. ΠΠΈΠΎΠ»ΠΎΠ³ΠΈΡ Ρ
Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 1. 1. ΠΠ΅Π½ΠΎΡΠΈΡΡΠ΅ΠΌΠ°ΡΠΈΠΊΠ° ΠΈ ΡΠ°ΠΊΡΠΎΠ½ΠΎΠΌΠΈΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 1. 2. Π‘ΡΡΠΎΠ΅Π½ΠΈΠ΅ ΠΈ ΠΆΠΈΠ·Π½Π΅Π΄Π΅ΡΡΠ΅Π»ΡΠ½ΠΎΡΡΡ Ρ
Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 1. 2. 1. Π‘ΡΡΠΎΠ΅Π½ΠΈΠ΅ ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΠΎΠ±ΠΎΠ»ΠΎΡΠΊΠΈ ΠΈ Π°Π½ΡΠΈΠ³Π΅Π½Π½ΡΠ΅ Π΄Π΅ΡΠ΅ΡΠΌΠΈΠ½Π°Π½ΡΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 1. 2. 2. Π‘Π΅ΠΊΡΠ΅ΡΠΈΡΡΠ΅ΠΌΡΠ΅ ΡΠ°ΠΊΡΠΎΡΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 1. 2. 2. 1. Π‘ΠΈΡΡΠ΅ΠΌΠ° ΡΠ΅ΠΊΡΠ΅ΡΠΈΠΈ III ΡΠΈΠΏΠ° Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 1. 2. 2. 2. Π‘Π΅ΠΊΡΠ΅ΡΠΈΡΡΠ΅ΠΌΡΠ΅ ΡΠ°ΠΊΡΠΎΡΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ Π²Π½Π΅ ΡΠΈΡΡΠ΅ΠΌΡ ΡΠ΅ΠΊΡΠ΅ΡΠΈΠΈ III ΡΠΈΠΏΠ°
- 1. 1. 3. ΠΠΈΠ·Π½Π΅Π½Π½ΡΠΉ ΡΠΈΠΊΠ» Ρ
Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 1. 3. 1. Π Π°Π½Π½ΠΈΠΉ ΡΡΠ°ΠΏ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΡΡΠ°Π΄ΠΈΠΈ ΠΆΠΈΠ·Π½Π΅Π½Π½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ ΡΡΠ°Π΄ΠΈΡ ΠΈΠ½Π²Π°Π·ΠΈΠΈ)
- 1. 113. 2. Π‘ΡΠ΅Π΄Π½ΠΈΠΉ ΡΡΠ°ΠΏ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΡΡΠ°Π΄ΠΈΠΈ ΠΆΠΈΠ·Π½Π΅Π½Π½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° Ρ
Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ (ΡΡΠ°Π΄ΠΈΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΠ³ΠΎ Π΄Π΅Π»Π΅Π½ΠΈΡ)
- 1. 1. 3. 3. ΠΠΎΠ·Π΄Π½ΠΈΠΉ ΡΡΠ°ΠΏ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΡΡΠ°Π΄ΠΈΠΈ ΠΆΠΈΠ·Π½Π΅Π½Π½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ (Π·Π°Π²Π΅ΡΡΠ΅Π½ΠΈΠ΅ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠ³ΠΎ ΡΡΠ°ΠΏΠ° ΡΠ°Π·Π²ΠΈΡΠΈΡ)
- 1. 1. ΠΠΈΠΎΠ»ΠΎΠ³ΠΈΡ Ρ
Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 2. ΠΠΏΠΎΠΏΡΠΎΠ· ΡΡΠΊΠ°ΡΠΈΠΎΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΊΠ»Π΅ΡΠΊΠΈ
- 1. ^.2.1. Π‘ΠΈΠ³Π½Π°Π»ΡΠ½ΡΠ΅ ΠΏΡΡΠΈ ΠΈΠ½Π΄ΡΠΊΡΠΈΠΈ ΠΈ ΡΠ΅Π°Π»ΠΈΠ·Π°ΡΠΈΠΈ-Π°ΠΏΠΎΠΏΡΠΎΠ·Π°
- 1. 2. 3. Π‘ΠΈΠ³Π½Π°Π»ΡΠ½ΡΠ΅ ΠΏΡΡΠΈ, Π½Π΅Π³Π°ΡΠΈΠ²Π½ΠΎ ΡΠ΅Π³ΡΠ»ΠΈΡΡΡΡΠΈΠ΅ ΠΏΡΠΎΡΠ΅ΡΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°
- 112. 3. 1. Π 13-Π/ΠΠΊ^ΡΠΈΠ³Π½Π°Π»ΡΠ½ΡΠΉ ΠΏΡΡΡ
- 1. 2. 3. 2. Π’ΡΠ°Π½ΡΠΊΡΠΈΠΏΡΠΈΠΎΠ½Π½ΡΠΉ ΡΠ°ΠΊΡΠΎΡ ΠΠ’-ΠΊΠ."
- 112. 3. 1. Π 13-Π/ΠΠΊ^ΡΠΈΠ³Π½Π°Π»ΡΠ½ΡΠΉ ΠΏΡΡΡ
- 1. 3. Π Π΅Π³ΡΠ»ΡΡΠΈΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Π±Π°ΠΊΡΠ΅ΡΠΈΡΠΌΠΈ
- 1. 3. 1. ΠΠ½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½Π°Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 3. 1. -Π. Π ΠΎΠ»Ρ 1ΠΏΡΠ² Π² Π°Π½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Ρ
Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 3. 1. 2. ΠΠΈΠ°ΡΠΈΠ»Π³Π»ΠΈΡΠ΅ΡΠΈΠ½, ΠΊΠ°ΠΊ ΡΠ°ΠΊΡΠΎΡ Π°Π½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 3. 131. ΠΠΊΡΠΈΠ²Π°ΡΠΈΡ ΠΠΠ Π- ΡΠΈΠ³Π½Π°Π»ΡΠ½ΠΎΠ³ΠΎ ΠΏΡΡΠΈ
- 1. 3. 1. 4. Π ΠΎΠ»Ρ Π‘Π ΠΠ Π² Π°Π½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 3. 1. 5. ΠΠ½Π°ΡΠ΅Π½ΠΈΠ΅ ΠΠ’-ΠΊΠ Π² Π°Π½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 1. 3. 2. ΠΡΠΎΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½Π°Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 2. 1. ΠΠ°ΡΠ΅ΡΠΈΠ°Π»Ρ
- 2. 14. 1. -ΠΠ»Π΅ΡΠΎΡΠ½ΡΠ΅ Π»ΠΈΠ½ΠΈΠΈ
- 2. 1. 2. Π¨ΡΠ°ΠΌΠΌΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ
- 2. 1. 3. ΠΠ°Π±ΠΎΡΠ°ΡΠΎΡΠ½ΡΠ΅ ΠΆΠΈΠ²ΠΎΡΠ½ΡΠ΅
- 2. 2. ΠΡΠ»ΡΡΡΡΠ°Π»ΡΠ½ΡΠ΅ ΠΌΠ΅ΡΠΎΠ΄Ρ
- 2. 211 ΠΡΠ»ΡΡΠΈΠ²ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΊΠ»Π΅ΡΠΎΠΊ
- 2. 2. 1. 1. ΠΡΠ»ΡΡΠΈΠ²ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΠΠ-293 ΠΈ ΠΠ‘Π’
- 2. 2. 112. ΠΡΠ»ΡΡΠΈΠ²ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΊΠ»Π΅ΡΠΎΠΊ McCoy
- 2. 2. 2. * ΠΠΎΠ»ΡΡΠ΅Π½ΠΈΠ΅ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΌΠ°ΡΠ΅ΡΠΈΠ°Π»Π°
- 2. 2. 2. 1. ΠΠΎΠ»ΡΡΠ΅Π½ΠΈΠ΅ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΌΠ°ΡΠ΅ΡΠΈΠ°Π»Π° C. trachomatis
- 2. 2. 2. 2. ΠΠΎΠ»ΡΡΠ΅Π½ΠΈΠ΅ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΌΠ°ΡΠ΅ΡΠΈΠ°Π»Π° C. muridarum
- 2. 3. ΠΠ΅ΡΠΎΠ΄Ρ ΠΎΡΠ΅Π½ΠΊΠΈ ΡΡΠΎΠ²Π½ΡΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ
- 2. 3. 1. Π€Π»ΡΠΎΡΠ΅ΡΡΠ΅Π½ΡΠ½Π°Ρ ΠΌΠΈΠΊΡΠΎΡΠΊΠΎΠΏΠΈΡ (ΠΎΡΠ΅Π½ΠΊΠ° ΠΏΡΠΎΡΠ΅Π½ΡΠ° ΠΈΠ½ΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΈ ΡΡΠΎΠ²Π΅Π½Ρ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°)
- 2. 3. 21. ΠΠΎΠ΄ΠΈΡΠΈΠΊΠ°ΡΠΈΡ ΠΌΠ΅ΡΠΎΠ΄Π° ΠΠ€Π Π΄Π»Ρ ΠΊΠΎΠ»ΠΈΡΠ΅ΡΡΠ²Π΅Π½Π½ΠΎΠ³ΠΎ ΡΡΠ΅ΡΠ° ΡΠ°Π·Π²ΠΈΡΠΈΡ* Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ^
- 2. 4. ΠΠ΅ΡΠΎΠ΄Ρ.ΠΎΡΠ΅Π½ΠΊΠΈ ΡΡΠΎΠ²Π½Ρ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° ΠΈ Π²ΡΠΆΠΈΠ²Π°Π΅ΠΌΠΎΡΡΠΈ
- 214. 1. ONPG ΡΠ΅ΡΡ (ΠΎΡΠ΅Π½ΠΊΠ° Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Π -Π³Π°Π»Π°ΠΊΡΠΎΠ·ΠΈΠ΄Π°Π·Ρ)
- 2. 4. 2. ΠΠ·ΠΌΠ΅ΡΠ΅Π½ΠΈΠ΅ ΡΡΠΎΠ²Π½Ρ ΠΊΠ°ΡΠΏΠ°Π· 3 ΠΈ
- 2. 4. 3. ΠΠ’Π’-ΡΠ΅ΡΡ
- 2. 4. 4. ΠΠΊΡΠ°ΡΠΊΠ° ΠΌΠ΅ΡΠΈΠ»Π΅Π½ΠΎΠ²ΡΠΌ ΡΠΈΠ½ΠΈΠΌ
- 2. 5. Π¦ΠΈΡΠΎΠΌΠ΅ΡΡΠΈΡΠ΅ΡΠΊΠ°Ρ.ΠΎΡΠ΅Π½ΠΊΠ° ΠΏΡΠΎΡΠ΅Π½ΡΠ° ΠΈΠ½ΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΡΠΌΠΈ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΈ, ΡΡΠΎΠ²Π½Ρ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°
- 2. 6. ΠΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΡin, vivo
- 2. 7. Π‘ΡΠ°ΡΠΈΡΡΠΈΡΠ΅ΡΠΊΠ°Ρ ΠΎΠ±ΡΠ°Π±ΠΎΡΠΊΠ° ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΠΎΠ²
- 3. 1. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ Ρ
Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ Π½Π° ΠΌΠΈΡΠΎΡ
ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΠΉ>ΠΏΡΡΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°
- 3. 1. 1. ΠΡΠ΅Π½ΠΊΠ° Π²Π»ΠΈΡΠ½ΠΈΡ C. trachomatis Π½Π° Π°ΠΏΠΎΠΏΡΠΎΠ· Π½Π° ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΡΡΠ°ΠΏΠ°Ρ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ Π² ΡΡΠ»ΠΎΠ²ΠΈΡΡ ΠΈΠ½Π΄ΡΠΊΡΠΈΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠ³ΠΎ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°
- 3. 1. 21. ΠΠΎΠ»Π½ΡΠ΅ΡΡΠ²Π΅Π½Π½Π°Ρ ΠΎΡΠ΅Π½ΠΊΠ° ΡΠ°Π·Π²ΠΈΡΠΈΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ ΠΈ ΡΡΠΎΠ²Π½Ρ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Π½Π° ΡΠΎΠ½Π΅ ΠΈΠ½Π΄ΡΠΊΡΠΈΠΈ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° ΡΡΠ°ΡΡΠΎΡΠΏΠΎΡΠΈΠ½ΠΎΠΌ
- 3. 13. ΠΡΠ΅Π½ΠΊΠ° ΡΡΠΎΠ²Π½Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΠΊΠ°ΡΠΏΠ°Π· Π² ΠΈΠ½ΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ Gtrachomatis ΠΊΠ»Π΅ΡΠΊΠ°Ρ Π½Π° ΡΠΎΠ½Π΅ ΠΈΠ½Π΄ΡΠΊΡΠΈΠΈ ΡΡΠ°ΡΡΠΎΡΠΏΠΎΡΠΈΠ½ΠΎΠΌ
- 3. 2. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ C. trachomatis Π½Π° ΡΡΠ°Π½ΡΠΊΡΠΈΠΏΡΠΈΠΎΠ½Π½ΡΠΉ ΡΠ°ΠΊΡΠΎΡ NF-kB
- 3. 2. 1. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ Π½Π° Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ NF-kB
- 3. 2. 2. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΡΡΡΡΠΊΡΡΡΠ½ΡΡ ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½ΡΠΎΠ² C. trachomatis Π½Π° Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ NF-kB ΡΠ΅ΡΠ΅Π· .Π’ΠΎΠ»Π»-ΠΏΠΎΠ΄ΠΎΠ±Π½ΡΠ΅ ΡΠ΅ΡΠ΅ΠΏΡΠΎΡΡ
- 3. 3. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ C. trachomatis Π½Π° Π±Π΅Π»ΠΎΠΊ Ρ
- 3. 3. 1. ΠΠ½Π΄ΡΠΊΡΠΈΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Π±Π΅Π»ΠΊΠ° Ρ53 Π² Π·Π°Π²ΠΈΡΠΈΠΌΠΎΡΡΠΈ ΠΎΡ Π΄ΠΎΠ·Ρ 5-ΡΡΠΎΡΡΡΠ°ΡΠΈΠ»Π° Π½Π° ΡΠΎΠ½Π΅ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ
- 3. 3. 2. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ C. trachomatis Π½Π° ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΡΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ Π±Π΅Π»ΠΊΠ° Ρ Π½Π° ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΡΡΠ°ΠΏΠ°Ρ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ
- 3. 3. 3. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ Π²ΡΡΠ°ΠΆΠ΅Π½Π½ΠΎΡΡΠΈ ΡΡΡΠ΅ΠΊΡΠ° ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΡ ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΠΎΠΉΠ°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Π±Π΅Π»ΠΊΠ° Ρ53"ΠΎΡ Π΄ΠΎΠ·Ρ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ, Π²ΡΠ·Π²Π°Π½Π½ΠΎΠΉ C. trachomatis
- 3. 3. 4. ΠΡΠ΅Π½ΠΊΠ° ΡΡΠΎΠ²Π½Ρ Π±Π΅Π»ΠΊΠ° Ρ53 Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ Π½Π° ΡΠΎΠ½Π΅ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ, Π²ΡΠ·Π²Π°Π½Π½ΠΎΠΉ
- 3. 3. 4. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Π±Π΅Π»ΠΊΠ° Ρ53 Π½Π° ΡΠ°Π·Π²ΠΈΡΠΈΠ΅ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ C. trachomatis Π²ΠΊΡΠ»ΡΡΡΡΠ΅ ΠΊΠ»Π΅ΡΠΎΠΊ
- 3. 3. 5. ΠΡΠ΅Π½ΠΊΠ° ΡΠ°Π·Π²ΠΈΡΠΈΡ ΡΠΏΠΎΠ½ΡΠ°Π½Π½ΠΎΠ³ΠΎ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Π² ΠΊΡΠ»ΡΡΡΡΠ΅ ΠΈΠ½ΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ
ΠΊΠ»Π΅ΡΠΎΠΊ ΠΠ‘Π’-116 Π΄ΠΈΠΊΠΎΠ³ΠΎ ΡΠΈΠΏΠ° (wt) ΠΈ Π½ΠΎΠΊΠ°ΡΡΠ½ΡΡ
ΠΏΠΎ Π³Π΅Π½Ρ Π±Π΅Π»ΠΊΠ° Ρ53 (-/-)
- 3. 3. 6. 0. ΡΠ΅Π½ΠΊΠ° Π²Π»ΠΈΡΠ½ΠΈΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Π±Π΅Π»ΠΊΠ° Ρ53 Π½Π° ΡΠ°Π·Π²ΠΈΡΠΈΠ΅ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΠΎΠΉ. ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ Π². ΡΡΠ»ΠΎΠ²ΠΈΡΡ in vivo
- 3. 4. ΠΠ·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ Ρ ΠΏΡΠΎΡΠ΅ΠΈΠ½ΠΊΠΈΠ½Π°Π·ΠΎΠΉ Π (Akt ΡΠΈΠ³Π½Π°Π»ΡΠ½ΡΠΌ-ΠΏΡΡΠ΅ΠΌ)
- 3. 4−1. ΠΠΊΡΠΈΠ²Π°ΡΠΈΡ Akt Π½Π° ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΡΡΠ°ΠΏΠ°Ρ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ
3.5. ΠΡΡΠ²Π»Π΅Π½ΠΈΠ΅ Π½ΠΎΠ²ΡΡ ΠΌΠΈΡΠ΅Π½Π΅ΠΉ Π΄Π»Ρ Π΄Π΅ΠΉΡΡΠ²ΠΈΡ Π»Π΅ΠΊΠ°ΡΡΡΠ²Π΅Π½Π½ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ², Π½Π°ΠΏΡΠ°Π²Π»Π΅Π½Π½ΡΡ Π½Π° Π±ΠΎΡΡΠ±Ρ Ρ Ρ ΡΠΎΠ½ΠΈΡΠ΅ΡΠΊΠΈΠΌΠΈ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΡΠΌΠΈ, Π½Π° ΠΎΡΠ½ΠΎΠ²Π΅ ΠΈΠ΄Π΅Π½ΡΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΡ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΠΎΠ² ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΡ. Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΡΠΌΠΈ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°.
3.5.1. ΠΡΠ±ΠΎΡ III ΡΡΠ°Π½ΡΠΏΠΎΡΡΠ½ΠΎΠΉ ΡΠΈΡΡΠ΅ΠΌΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ Π² ΠΊΠ°ΡΠ΅ΡΡΠ²Π΅ ΠΌΠΈΡΠ΅Π½ΠΈ Π΄Π»Ρ ΠΈΠ½Π°ΠΊΡΠΈΠ²Π°ΡΠΈΠΈ. Π°Π½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΠΏΠ°ΡΠΎΠ³Π΅Π½Π°.
3.5.1.1. ΠΡΠ΅Π½ΠΊΠ° Π²Π»ΠΈΡΠ½ΠΈΡ Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΡ LHC-709-Π½Π° Π°ΠΏΠΎΠΏΡΠΎΠ· ΠΈΠ½ΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ C. trachomatis ΠΊΠ»Π΅ΡΠΎΠΊ.
3.5.1.2.* ΠΡΠ΅Π½ΠΊΠ° Π²Π»ΠΈΡΠ½ΠΈΡ ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΡΠ° Π‘Π‘Π’Π’ Π½Π° Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΡΠΉ ΠΆΠΈΠ·Π½Π΅Π½Π½ΡΠΉ^ ΡΠΈΠΊΠ»-.
3.5.2. ΠΠΎΠ΄ΡΠ»ΡΡΠΈΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΡΠ½Π΄ΠΎΠ³Π΅Π½Π½ΡΡ ΡΠΈΠ³Π½Π°Π»ΡΠ½ΡΡ ΠΏΡΡΠ΅ΠΉ, ΠΎΡΠ²Π΅ΡΡΡΠ²Π΅Π½Π½ΡΡ Π·Π°, ΡΡΡΠΎΠΉΡΠΈΠ²ΠΎΡΡΡ ΠΊ Π°ΠΏΠΎΠΏΡΠΎΠ·Ρ, Ρ ΠΊΠΎΡΠΎΡΡΠΌΠΈ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΡΡΡ ΠΏΠ°ΡΠΎΠ³Π΅Π½Ρ.
3.5.2.1. ΠΡΠ΅Π½ΠΊΠ° ΡΠΎΠΊΡΠΈΡΠ½ΠΎΡΡΠΈ ΡΠ΅ΡΠ²Π΅ΡΠ°ΡΡΠΎΠ»Π° Π΄Π»Ρ ΠΊΠ»Π΅ΡΠΎΠΊ.
3.5.2.2 ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΡΠ΅ΡΠ²Π΅ΡΠ°ΡΡΠΎΠ»Π° Π½Π° Π°ΠΏΠΎΠΏΡΠΎΠ· ΠΊΠ»Π΅ΡΠΎΠΊ, ΠΈΠ½ΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ *
C.trachomatis.
3.5.2.2.1. ΠΡΠ΅Π½ΠΊΠ°, ΡΡΠΎΠ²Π½Ρ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ Π»ΡΠΌΠΈΠ½Π΅ΡΡΠ΅Π½ΡΠ½ΠΎΠΉ ΠΌΠΈΠΊΡΠΎΡΠΊΠΎΠΏΠΈΠΈ ΠΏΡΠΈ ΠΎΠΊΡΠ°ΡΠΊΠ΅ ΠΏΡΠΎΠΏΠΈΠ΄ΠΈΡΠΌΠΎΠΌ ΠΈΠΎΠ΄ΠΈΠ΄ΠΎΠΌ.
3.5.2.2.2.0ΡΠ΅Π½ΠΊΠ° ΡΡΠΎΠ²Π½Ρ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°- ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ ΠΏΡΠΎΡΠΎΡΠ½ΠΎΠΉ ΡΠΈΡΠΎΠΌΠ΅ΡΡΠΈΠΈ.
3.5.2.2.3. ΠΡΠ΅Π½ΠΊΠ° Π²Π»ΠΈΡΠ½ΠΈΡ ΡΠ΅ΡΠ²Π΅ΡΠ°ΡΡΠΎΠ»Π° Π½Π° Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΠΊΠ°ΡΠΏΠ°Π·Ρ-3.
3.5.2.3. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΡΠ΅ΡΠ²Π΅ΡΠ°ΡΡΠΎΠ»Π° Π½Π° ΠΈΠ½ΡΠ΅ΠΊΡΠΈΡ, Π²ΡΠ·Π²Π°Π½Π½ΡΡ Π‘. Π¬-Π°ΡΠΠΎΡΠ°Π¨.
3.5.2.3.1. ΠΠΎΠ»ΠΈΡΠ΅ΡΡΠ²Π΅Π½Π½Π°Ρ ΠΎΡΠ΅Π½ΠΊΠ° Π²Π»ΠΈΡΠ½ΠΈΡ ΡΠ΅ΡΠ²Π΅ΡΠ°ΡΡΠΎΠ»Π° Π½Π° ΡΠ°Π·Π²ΠΈΡΠΈΠ΅ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ Π² ΠΊΡΠ»ΡΡΡΡΠ΅ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ ΠΠ€Π.
3.5.2.3.2. Π¦ΠΈΡΠΎΠΌΠ΅ΡΡΠΈΡΠ΅ΡΠΊΠ°Ρ ΠΎΡΠ΅Π½ΠΊΠ° Π²Π»ΠΈΡΠ½ΠΈΡ ΡΠ΅ΡΠ²Π΅ΡΠ°ΡΡΠΎΠ»Π° Π½Π° ΡΠ°Π·Π²ΠΈΡΠΈΠ΅ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ Π² ΠΊΡΠ»ΡΡΡΡΠ΅ ΠΊΠ»Π΅ΡΠΎΠΊ.
3.5.2.4. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΡΠ΅ΡΠ²Π΅ΡΠ°ΡΡΠΎΠ»Π° Π½Π° ΡΠ°Π·Π½ΡΠ΅ ΡΡΠ°ΠΏΡ ΠΆΠΈΠ·Π½Π΅Π½Π½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° Π‘.&Π°ΡΠΊΠΎΡΠ°Π
3.5.2.5 ΠΠ·ΡΡΠ΅Π½ΠΈΠ΅ Π²Π»ΠΈΡΠ½ΠΈΡ ΡΠ΅ΡΠ²Π΅ΡΠ°ΡΡΠΎΠ»Π° Π½Π° ΠΈΠ½ΡΠ΅ΠΊΡΠΈΡ, Π²ΡΠ·Π²Π°Π½Π½ΡΡ Π‘. ΡΠΈΠΏ (1Π°Π³11Ρ Ρ Π»Π°Π±ΠΎΡΠ°ΡΠΎΡΠ½ΡΡ ΠΆΠΈΠ²ΠΎΡΠ½ΡΡ .
ΠΠ«ΠΠΠΠ«.
ΠΠ½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΡΠ΅ Π±Π΅Π»ΠΊΠΈ β ΠΌΠΈΡΠ΅Π½ΠΈ Π΄Π»Ρ ΠΏΠΎΠΈΡΠΊΠ° Π½ΠΎΠ²ΡΡ Π°Π½ΡΠΈΡ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ² (ΡΠ΅ΡΠ΅ΡΠ°Ρ, ΠΊΡΡΡΠΎΠ²Π°Ρ, Π΄ΠΈΠΏΠ»ΠΎΠΌ, ΠΊΠΎΠ½ΡΡΠΎΠ»ΡΠ½Π°Ρ)
ΠΠΊΡΡΠ°Π»ΡΠ½ΠΎΡΡΡ.
ΠΠ»Ρ Π²ΡΠΆΠΈΠ²Π°Π½ΠΈΡ ΠΈ ΡΠΎΡΡΡΠ΅ΡΡΠ²ΠΎΠ²Π°Π½ΠΈΡ Ρ ΠΊΠ»Π΅ΡΠΊΠΎΠΉ Ρ ΠΎΠ·ΡΠΈΠ½Π° Π±Π°ΠΊΡΠ΅ΡΠΈΡΠΌ, ΡΠ°ΠΊΠΆΠ΅ ΠΊΠ°ΠΊ ΠΈ Π²ΠΈΡΡΡΠ°ΠΌ, Π½Π΅ΠΎΠ±Ρ ΠΎΠ΄ΠΈΠΌΠΎ ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΠΎ ΠΈΠ½Π°ΠΊΡΠΈΠ²ΠΈΡΠΎΠ²Π°ΡΡ Π·Π°ΡΠΈΡΠ½ΡΠ΅ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΡ ΠΌΠ°ΠΊΡΠΎΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠ°. Π Π² ΠΏΠ΅ΡΠ²ΡΡ ΠΎΡΠ΅ΡΠ΅Π΄Ρ ΠΎΠ½ΠΈ Π΄ΠΎΠ»ΠΆΠ½Ρ Π±Π»ΠΎΠΊΠΈΡΠΎΠ²Π°ΡΡ Π½Π°ΠΈΠ±ΠΎΠ»Π΅Π΅ ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΡΡ ΠΈ ΠΊΠ°ΡΠ΄ΠΈΠ½Π°Π»ΡΠ½ΡΡ Π·Π°ΡΠΈΡΡ Ρ ΠΎΠ·ΡΠΈΠ½Π° — Π°ΠΏΠΎΠΏΡΠΎΠ·, Ρ.ΠΊ. Π³Π΅Π½Π΅ΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΏΡΠΎΠ³ΡΠ°ΠΌΠΌΠΎΠΉ ΡΡΠΊΠ°ΡΠΈΠΎΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΏΡΠ΅Π΄ΡΡΠΌΠΎΡΡΠ΅Π½ΠΎ, ΡΡΠΎ ΠΎΠ½Π° «ΡΠ°ΠΌΠΎΠ»ΠΈΠΊΠ²ΠΈΠ΄ΠΈΡΡΠ΅ΡΡΡ», Π΅ΡΠ»ΠΈ Π² Π½Π΅Π΅ ΠΏΠΎΠΏΠ°Π»Π° ΠΈΠ½ΡΠ΅ΠΊΡΠΈΡ. ΠΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΠ΅ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° ΠΏΡΠΈΠ²ΠΎΠ΄ΠΈΡ Π² Π΄ΠΈΡΡΠ΅ΠΌΠΈΠ½Π°ΡΠΈΠΈ Π²ΠΎΠ·Π±ΡΠ΄ΠΈΡΠ΅Π»Ρ Π² ΡΠ°Π·Π»ΠΈΡΠ½ΡΠ΅ ΡΠΊΠ°Π½ΠΈ ΠΈ ΠΎΡΠ³Π°Π½Ρ, ΡΠ°ΡΠΏΡΠΎΡΡΡΠ°Π½Π΅Π½ΠΈΡ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΏΡΠΎΡΠ΅ΡΡΠ°, Π²ΡΠΆΠΈΠ²Π°Π½ΠΈΡ ΠΏΠ°ΡΠΎΠ³Π΅Π½Π° ΠΈ Π΅Π³ΠΎ ΠΏΠ΅ΡΡΠΈΡΡΠ΅Π½ΡΠΈΠΈ. ΠΡΠ΅ ΡΡΠΎ ΠΎΠΏΡΠ΅Π΄Π΅Π»ΡΠ΅Ρ Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎΡΡΡ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΡΡΠΆΠ΅Π»ΡΡ Ρ ΡΠΎΠ½ΠΈΡΠ΅ΡΠΊΠΈΡ ΡΠΎΡΡΠΎΡΠ½ΠΈΠΉ.
ΠΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΠ΅ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ Π΄Π»Ρ ΡΠ΅Π»ΠΎΠ³ΠΎ ΡΡΠ΄Π° Π±Π°ΠΊΡΠ΅ΡΠΈΠΉ, Π½ΠΎ Π² Π±ΠΎΠ»ΡΡΠ΅ΠΉ ΡΡΠ΅ΠΏΠ΅Π½ΠΈ ΡΡΠ° Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΡΠ²ΡΠ·Π°Π½Π° Ρ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΡΠΌ ΡΠΈΠΏΠΎΠΌ ΠΏΠ°ΡΠ°Π·ΠΈΡΠΈΡΠΎΠ²Π°Π½ΠΈΡ. Π’Π°ΠΊΠΎΠ΅ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ ΡΠ΅Π°Π»ΠΈΠ·ΡΠ΅ΡΡΡ Π² ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΠ΅ Π΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΎΡΠ΄Π΅Π»ΡΠ½ΡΡ ΡΡΡΡΠΊΡΡΡΠ½ΡΡ ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½ΡΠΎΠ² Π±Π°ΠΊΡΠ΅ΡΠΈΠ°Π»ΡΠ½ΠΎΠΉ ΠΊΠ»Π΅ΡΠΊΠΈ, Π»ΠΈΠ±ΠΎ ΡΠ΅ΠΊΡΠ΅ΡΠΈΡΡΠ΅ΠΌΡΡ ΠΌΠΎΠ»Π΅ΠΊΡΠ» Ρ ΠΊΠΎΠ½ΠΊΡΠ΅ΡΠ½ΡΠΌΠΈ Π·Π²Π΅Π½ΡΡΠΌΠΈ ΡΠΈΠ³Π½Π°Π»ΡΠ½ΠΎΠ³ΠΎ ΠΏΡΡΠΈ, Π²Π΅Π΄ΡΡΠ΅Π³ΠΎ ΠΊ Π°ΠΏΠΎΠΏΡΠΎΠ·Ρ. Π Π½Π°ΡΡΠΎΡΡΠ΅ΠΌΡ Π²ΡΠ΅ΠΌΠ΅Π½ΠΈ ΠΈΠ·ΡΡΠ΅Π½ΠΈΠ΅ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΡ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΠΎΠ² ΡΠΏΡΠ°Π²Π»Π΅Π½ΠΈΡ ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ Π³ΠΈΠ±Π΅Π»ΡΡ ΠΏΠΎΠ·Π²ΠΎΠ»ΠΈΠ»ΠΎ Π²ΠΎ ΠΌΠ½ΠΎΠ³ΠΎΠΌ ΠΎΠΏΡΠ΅Π΄Π΅Π»ΠΈΡΡ ΡΠΎΠ»Ρ ΡΡΠ΄Π° Π½Π΅ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ΅ΡΠΊΠΈΡ Π±Π°ΠΊΡΠ΅ΡΠΈΠ°Π»ΡΠ½ΡΡ ΠΌΠΎΠ»Π΅ΠΊΡΠ» ΡΠ°ΠΊΠΈΡ , ΠΊΠ°ΠΊ ΠΠΠ‘, Π»ΠΈΠΏΠΎΡΠ΅ΠΉΡ ΠΎΠ΅Π²ΡΠ΅ ΠΊΠΈΡΠ»ΠΎΡΡ, ΠΠΠ Π² ΡΠ΅Π³ΡΠ»ΡΡΠΈΠΈ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°. ΠΠ΄Π½Π°ΠΊΠΎ Π½Π°ΠΈΠΌΠ΅Π½Π΅Π΅ ΠΈΠ·ΡΡΠ΅Π½Π½ΠΎΠΉ ΠΎΠ±Π»Π°ΡΡΡΡ ΡΠ²Π»ΡΠ΅ΡΡΡ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½Π°Ρ Ρ Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΡΡΠΈΠΊΠ° Π΄Π΅ΠΉΡΡΠ²ΠΈΡ ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ΅ΡΠΊΠΈΡ Π±Π°ΠΊΡΠ΅ΡΠΈΠ°Π»ΡΠ½ΡΡ ΡΠ°ΠΊΡΠΎΡΠΎΠ², ΠΈΠ½Π³ΠΈΠ±ΠΈΡΡΡΡΠΈΡ Π°ΠΏΠΎΠΏΡΠΎΠ·, Π° ΡΠ°ΠΊΠΆΠ΅ ΠΈΠ΄Π΅Π½ΡΠΈΡΠΈΠΊΠ°ΡΠΈΡ ΡΡΠΊΠ°ΡΠΈΠΎΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΌΠΈΡΠ΅Π½Π΅ΠΉ Π°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠ³ΠΎ ΡΠΈΠ³Π½Π°Π»ΡΠ½ΠΎΠ³ΠΎ ΠΏΡΡΠΈ, Ρ ΠΊΠΎΡΠΎΡΡΠΌΠΈ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΡΡΡ Π±Π°ΠΊΡΠ΅ΡΠΈΠΈ.
Π‘ΡΠ°Π½ΠΎΠ²ΠΈΡΡΡ ΠΎΡΠ΅Π²ΠΈΠ΄Π½ΡΠΌ, ΡΡΠΎ ΠΊΠΎΠ½ΡΡΠΎΠ»Ρ ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ Π³ΠΈΠ±Π΅Π»ΠΈ Π΄Π»Ρ Π²ΠΎΠ·Π±ΡΠ΄ΠΈΡΠ΅Π»Π΅ΠΉ ΡΠΈΡΠΎΠΊΠΎ ΡΠ°ΡΠΏΡΠΎΡΡΡΠ°Π½Π΅Π½Π½ΡΡ Π·Π°Π±ΠΎΠ»Π΅Π²Π°Π½ΠΈΠΉ ΡΠ΅Π»ΠΎΠ²Π΅ΠΊΠ°, Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΡΡ ΠΏΠ°ΡΠΎΠ³Π΅Π½ΠΎΠ², Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ ΡΠ²Π»ΡΠ΅ΡΡΡ ΠΎΠ΄Π½ΠΈΠΌ ΠΈΠ· Π²Π΅Π΄ΡΡΠΈΡ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΠΎΠ² ΠΈΠ½Π°ΠΊΡΠΈΠ²Π°ΡΠΈΠΈ Π·Π°ΡΠΈΡΠ½ΡΡ ΡΠ°ΠΊΡΠΎΡΠΎΠ² ΠΌΠ°ΠΊΡΠΎΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠ°, ΠΎΠΏΡΠ΅Π΄Π΅Π»ΡΡΡΠΈΡ ΠΏΠ°ΡΠΎΠ³Π΅Π½Π΅Π· Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ. ΠΠ½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½Π°Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ, ΠΏΠΎ-Π²ΠΈΠ΄ΠΈΠΌΠΎΠΌΡ, Π±ΡΠ»Π° Π·Π°ΠΊΡΠ΅ΠΏΠ»Π΅Π½Π° Π² ΠΏΡΠΎΡΠ΅ΡΡΠ΅ ΡΠ²ΠΎΠ»ΡΡΠΈΠΈ ΠΊΠ°ΠΊ ΡΠ°ΠΊΡΠΎΡ ΠΏΠ°ΡΠΎΠ³Π΅Π½Π½ΠΎΡΡΠΈ. ΠΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ ΠΏΠΎΡΠ»Π΅Π΄Π½Π΅Π³ΠΎ Π²ΡΠ΅ΠΌΠ΅Π½ΠΈ Π΄Π°ΡΡ ΠΎΡΠ½ΠΎΠ²Π°Π½ΠΈΡ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»Π°Π³Π°ΡΡ, ΡΡΠΎ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΈ ΠΈΡΠΏΠΎΠ»ΡΠ·ΡΡΡ ΡΠ°Π·Π»ΠΈΡΠ½ΡΠ΅ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΡ ΡΠΏΡΠ°Π²Π»Π΅Π½ΠΈΡ ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ Π³ΠΈΠ±Π΅Π»ΡΡ, ΠΊΠΎΡΠΎΡΡΠ΅ ΡΠ°Π±ΠΎΡΠ°ΡΡ Π½Π° Π½Π΅ΡΠΊΠΎΠ»ΡΠΊΠΈΡ ΡΡΠ°ΠΏΠ°Ρ ΠΏΡΠΎΠ²Π΅Π΄Π΅Π½ΠΈΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠ³ΠΎ ΡΠΈΠ³Π½Π°Π»Π°. Π ΡΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΠ°Ρ in vitro Π½Π° ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΠΊΠ»Π΅ΡΠΎΡΠ½ΡΡ ΠΌΠΎΠ΄Π΅Π»ΡΡ Π±ΡΠ»ΠΎ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΈ Π·Π°ΡΠΈΡΠ°ΡΡ ΡΠΏΠΈΡΠ΅Π»ΠΈΠ°Π»ΡΠ½ΡΠ΅ ΠΊΠ»Π΅ΡΠΊΠΈ, ΠΌΠΎΠ½ΠΎΡΠΈΡΡ/ΠΌΠ°ΠΊΡΠΎΡΠ°Π³Π° ΠΎΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°, ΠΈΠ½Π΄ΡΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΊΠ°ΠΊ Π²Π½Π΅ΡΠ½ΠΈΠΌΠΈ, ΡΠ°ΠΊ ΠΈ Π²Π½ΡΡΡΠ΅Π½Π½ΠΈΠΌΠΈ ΡΠΈΠ³Π½Π°Π»Π°ΠΌΠΈ, Π½Π°ΠΏΡΠΈΠΌΠ΅Ρ, Π€ΠΠ-Π°, ΡΡΠ°ΡΡΠΎΡΠΏΠΎΡΠΈΠ½ΠΎΠΌ, ΡΡΠΎΠΏΠΎΠ·ΠΈΠ΄ΠΎΠΌ, Π³ΡΠ°Π½Π·ΠΈΠΌΠΎΠΌ Π/ΠΏΠ΅ΡΡΠΎΡΠΈΠ½ΠΎΠΌ, Π£Π€-ΠΎΠ±Π»ΡΡΠ΅Π½ΠΈΠ΅ΠΌ. ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ Π±Π»ΠΎΠΊΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° ΠΏΡΠΎΠΈΡΡ ΠΎΠ΄ΠΈΡ ΠΊΠ°ΠΊ ΠΏΡΠΈ ΠΏΡΠΎΠ΄ΡΠΊΡΠΈΠ²Π½ΠΎΠΉ, ΡΠ°ΠΊ ΠΈ ΠΏΡΠΈ ΠΏΠ΅ΡΡΠΈΡΡΠ΅Π½ΡΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ, ΡΡΠΎ ΠΈ ΠΎΠΏΡΠ΅Π΄Π΅Π»ΡΠ΅Ρ Π²ΡΡΠΎΠΊΠΈΠΉ ΡΠΈΡΠΊ ΡΠ°Π·Π²ΠΈΡΠΈΡ Ρ ΡΠΎΠ½ΠΈΡΠ΅ΡΠΊΠΈΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΡΡ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΉ. ΠΠ΄Π½Π°ΠΊΠΎ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΠ΅ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΡ ΡΠ»ΠΎΠΆΠ½ΠΎΠ³ΠΎ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΏΠ°ΡΠΎΠ³Π΅Π½Π° Ρ ΡΠΈΠ³Π½Π°Π»ΡΠ½ΡΠΌΠΈ ΠΏΡΡΡΠΌΠΈ Ρ ΠΎΠ·ΡΠΉΡΠΊΠΎΠΉ ΠΊΠ»Π΅ΡΠΊΠΈ, Π²Π΅Π΄ΡΡΠΈΠΌΠΈ ΠΊ Π°ΠΏΠΎΠΏΡΠΎΠ·Ρ, ΠΎΡΡΠ°ΡΡΡΡ Π²ΠΎ ΠΌΠ½ΠΎΠ³ΠΎΠΌ Π½Π΅ ΠΈΠ·ΡΡΠ΅Π½Π½ΡΠΌΠΈ.
ΠΠ΄Π΅Π½ΡΠΈΡΠΈΠΊΠ°ΡΠΈΡ Π±Π°ΠΊΡΠ΅ΡΠΈΠ°Π»ΡΠ½ΡΡ ΡΠ°ΠΊΡΠΎΡΠΎΠ², ΠΎΡΠ²Π΅ΡΡΡΠ²Π΅Π½Π½ΡΡ Π·Π° ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΠ΅ ΠΏΠ°ΡΠΎΠ³Π΅Π½Π°ΠΌΠΈ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° ΠΊΠ»Π΅ΡΠΊΠΈ Ρ ΠΎΠ·ΡΠΈΠ½Π° ΠΈ Π²ΡΡΠ²Π»Π΅Π½ΠΈΠ΅ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΡΡ ΡΠΈΠ³Π½Π°Π»ΡΠ½ΡΡ ΠΏΡΡΠ΅ΠΉ, Π²Π΅Π΄ΡΡΠΈΡ ΠΊ Π°ΠΏΠΎΠΏΡΠΎΠ·Ρ, ΠΊΠΎΡΠΎΡΡΠ΅ ΠΈΡΠΏΠΎΠ»ΡΠ·ΡΠ΅Ρ ΠΏΠ°ΡΠΎΠ³Π΅Π½ Π΄Π»Ρ ΡΠ²ΠΎΠ΅Π³ΠΎ Π²ΡΠΆΠΈΠ²Π°Π½ΠΈΡ ΠΈ ΡΠ°Π·ΠΌΠ½ΠΎΠΆΠ΅Π½ΠΈΡ, Π½Π°ΠΏΡΠ°Π²Π»Π΅Π½ΠΎ Π½Π° ΡΠΎΠ·Π΄Π°Π½ΠΈΠ΅ Π°Π½ΡΠΈΠ±Π°ΠΊΡΠ΅ΡΠΈΠ°Π»ΡΠ½ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ². ΠΡΠΎ ΠΏΠΎΠ·Π²ΠΎΠ»ΠΈΡ ΡΠ°Π·ΡΠ°Π±ΠΎΡΠ°ΡΡ ΠΏΡΠΈΠ½ΡΠΈΠΏΠΈΠ°Π»ΡΠ½ΠΎ Π½ΠΎΠ²ΡΠΉ ΠΏΠΎΠ΄Ρ ΠΎΠ΄ ΠΊ ΡΠ΅ΡΠ°ΠΏΠΈΠΈ ΡΡΠΆΠ΅Π»ΡΡ Ρ ΡΠΎΠ½ΠΈΡΠ΅ΡΠΊΠΈΡ Π·Π°Π±ΠΎΠ»Π΅Π²Π°Π½ΠΈΠΉ ΠΈ ΡΠΎΠ·Π΄Π°ΡΡ Π½ΠΎΠ²ΠΎΠ΅ ΠΏΠΎΠΊΠΎΠ»Π΅Π½ΠΈΠ΅ Π»Π΅ΠΊΠ°ΡΡΡΠ²Π΅Π½Π½ΡΡ ΡΡΠ΅Π΄ΡΡΠ², Π²Π»ΠΈΡΡΡΠΈΡ Π½Π° ΠΎΡΠ½ΠΎΠ²Ρ ΠΏΠ΅ΡΡΠΈΡΡΠ΅Π½ΡΠΈΠΈ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΎΠ½Π½ΡΡ Π°Π³Π΅Π½ΡΠΎΠ² Π² ΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠ΅. ΠΠ°ΠΊΡΠ΅ΡΠΈΠ°Π»ΡΠ½ΡΠ΅ ΡΠ°ΠΊΡΠΎΡΡ Ρ Π°Π½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡΡ Π±ΡΠ΄ΡΡ ΠΈΡΠΏΠΎΠ»ΡΠ·ΠΎΠ²Π°Π½Ρ ΠΊΠ°ΠΊ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΠ΅ ΠΌΠΈΡΠ΅Π½ΠΈ Π΄Π»Ρ Π²ΡΠ±ΠΎΡΠ° ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ΅ΡΠΊΠΈΡ (ΠΌΠΈΡΠ΅Π½Ρ-Π½Π°ΠΏΡΠ°Π²Π»Π΅Π½Π½ΡΡ ) ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΡΠΎΠ² Ρ ΠΏΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΠ΅ΠΌ ΡΠΎΠ²ΡΠ΅ΠΌΠ΅Π½Π½ΠΎΠΉ ΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΠΈ ΡΠΊΡΠΈΠ½ΠΈΠ½Π³Π° Π½ΠΈΠ·ΠΊΠΎΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΡ Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΡ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΠΉ. Π‘ Π΄ΡΡΠ³ΠΎΠΉ ΡΡΠΎΡΠΎΠ½Ρ, Π²ΡΠ±ΠΎΡ ΡΡΠΊΠ°ΡΠΈΠΎΡΠΈΡΠ΅ΡΠΊΠΈΡ Π±Π΅Π»ΠΊΠΎΠ², ΡΠ²Π»ΡΡΡΠΈΡ ΡΡ ΠΌΠΈΡΠ΅Π½ΡΠΌΠΈ Π±Π°ΠΊΡΠ΅ΡΠΈΠ°Π»ΡΠ½ΡΡ Π°Π½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΡΡ ΡΠ°ΠΊΡΠΎΡΠΎΠ², Π΄Π°ΡΡ Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎΡΡΡ ΡΠ°Π·ΡΠ°Π±ΠΎΡΠ°ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΡ, ΠΌΠΎΠ΄ΡΠ»ΠΈΡΡΡΡΠΈΠ΅ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ Π΄Π°Π½Π½ΡΡ Π±Π΅Π»ΠΊΠΎΠ² Ρ ΡΠ΅Π»ΡΡ ΠΏΡΠ΅Π΄ΠΎΡΠ²ΡΠ°ΡΠ΅Π½ΠΈΡ ΠΈ/ΠΈΠ»ΠΈ ΠΏΡΠ΅ΠΊΡΠ°ΡΠ΅Π½ΠΈΡ Ρ ΡΠΎΠ½ΠΈΠ·Π°ΡΠΈΠΈ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΏΡΠΎΡΠ΅ΡΡΠ°. ΠΡΡΡΠ½Π΅Π½ΠΈΠ΅ ΡΠ½Π΄ΠΎΠ³Π΅Π½Π½ΡΡ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΠΎΠ², ΠΎΠΏΡΠ΅Π΄Π΅Π»ΡΡΡΠΈΡ ΡΡΠ²ΡΡΠ²ΠΈΡΠ΅Π»ΡΠ½ΠΎΡΡΡ ΠΊ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΎΠ½Π½ΠΎΠΌΡ Π°Π³Π΅Π½ΡΡ, ΠΏΠΎΠ·Π²ΠΎΠ»ΠΈΡ ΠΏΡΠΎΠ³Π½ΠΎΠ·ΠΈΡΠΎΠ²Π°ΡΡ Ρ Π°ΡΠ°ΠΊΡΠ΅Ρ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ, Π° ΡΠ°ΠΊΠΆΠ΅ ΠΎΠ±Π΅ΡΠΏΠ΅ΡΠΈΡ Π½Π°ΡΡΠ½ΠΎ ΠΎΠ±ΠΎΡΠ½ΠΎΠ²Π°Π½Π½ΡΠΉ ΠΏΠΎΠ΄Ρ ΠΎΠ΄ Π΄Π»Ρ Π²ΡΠ±ΠΎΡΠ° ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΠΎΠ³ΠΎ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠ° ΠΈΠ· ΡΠΏΠΈΡΠΊΠ° ΡΡΡΠ΅ΡΡΠ²ΡΡΡΠΈΡ Π»Π΅ΠΊΠ°ΡΡΡΠ²Π΅Π½Π½ΡΡ ΡΡΠ΅Π΄ΡΡΠ², ΠΌΠΎΠ΄ΡΠ»ΠΈΡΡΡΡΠΈΡ ΠΊΠ»Π΅ΡΠΎΡΠ½ΡΠ΅ ΡΠΈΠ³Π½Π°Π»ΡΠ½ΡΠ΅ ΠΏΡΡΠΈ.
Π¦Π΅Π»Ρ: ΠΈΠ·ΡΡΠΈΡΡ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΡ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΡ Ρ ΡΠΈΠ³Π½Π°Π»ΡΠ½ΡΠΌΠΈ ΠΏΡΡΡΠΌΠΈ, Π²Π΅Π΄ΡΡΠΈΠΌΠΈ ΠΊ Π°ΠΏΠΎΠΏΡΠΎΠ·Ρ, ΠΈ ΠΈΠ΄Π΅Π½ΡΠΈΡΠΈΡΠΈΡΠΎΠ²Π°ΡΡ ΠΏΠ΅ΡΡΠΏΠ΅ΠΊΡΠΈΠ²Π½ΡΠ΅ ΠΌΠΈΡΠ΅Π½ΠΈ Π΄Π»Ρ ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΡ Π°Π½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΠΏΠ°ΡΠΎΠ³Π΅Π½Π°.
ΠΠ°Π΄Π°ΡΠΈ:
1. ΠΡ Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΠ·ΠΎΠ²Π°ΡΡ Π²Π»ΠΈΡΠ½ΠΈΠ΅ Π‘. trachomatis Π½Π° Π°ΠΏΠΎΠΏΡΠΎΠ· ΠΊΠ»Π΅ΡΠΊΠΈ-Ρ ΠΎΠ·ΡΠΈΠ½Π° Π½Π° ΡΠ°Π·Π½ΡΡ ΡΡΠ°ΠΏΠ°Ρ ΠΆΠΈΠ·Π½Π΅Π½Π½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° ΠΏΠ°ΡΠΎΠ³Π΅Π½Π°.
2. ΠΠ·ΡΡΠΈΡΡ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΠ΅ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΡ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΡ Π‘. trachomatis Ρ ΠΎΡΠ½ΠΎΠ²Π½ΡΠΌΠΈ ΡΠ½Π΄ΠΎΠ³Π΅Π½Π½ΡΠΌΠΈ ΡΠΈΠ³Π½Π°Π»ΡΠ½ΡΠΌΠΈ ΠΏΡΡΡΠΌΠΈ, Π²Π΅Π΄ΡΡΠΈΠΌΠΈ ΠΊ Π°ΠΏΠΎΠΏΡΠΎΠ·Ρ.
3. ΠΠ·ΡΡΠΈΡΡ Π²Π»ΠΈΡΠ½ΠΈΠ΅ ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΡΠ° ΠΈΠ΄Π΅Π½ΡΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠΉ Π±Π°ΠΊΡΠ΅ΡΠΈΠ°Π»ΡΠ½ΠΎΠΉ ΠΌΠΈΡΠ΅Π½ΠΈ Π½Π° Π°ΠΏΠΎΠΏΡΠΎΠ· Π² ΠΈΠ½ΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ ΠΊΠ»Π΅ΡΠΊΠ°Ρ ΠΈ Π½Π° ΡΠ°Π·Π²ΠΈΡΠΈΠ΅ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ.
4. ΠΡΠ±ΡΠ°ΡΡ ΠΌΠΎΠ΄ΡΠ»ΡΡΠΎΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΡΡΠΊΠ°ΡΠΈΠΎΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΌΠΈΡΠ΅Π½Π΅ΠΉ ΠΈ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°ΡΡ Π΅Π³ΠΎ ΠΏΡΠΎΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠ΅ ΠΈ Π°Π½ΡΠΈΡ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΠΎΠ΅ Π΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ Π² ΡΡΠ»ΠΎΠ²ΠΈΡΡ in vitro ΠΈ in vivo .
ΠΠ°ΡΡΠ½Π°Ρ Π½ΠΎΠ²ΠΈΠ·Π½Π°.
ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ Π‘. trachomatis Ρ Ρ53 ΡΠΈΠ³Π½Π°Π»ΡΠ½ΡΠΌ ΠΏΡΡΠ΅ΠΌ. ΠΠ½ΡΠ΅ΠΊΡΠΈΡ Π² ΠΊΡΠ»ΡΡΡΡΠ΅ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΏΡΠΈΠ²ΠΎΠ΄ΠΈΠ»Π° ΠΊ ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΡ ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Π±Π΅Π»ΠΊΠ° Ρ53 ΠΈ ΠΏΠΎΠ²ΡΡΠ΅Π½ΠΈΡ ΡΠ΅Π·ΠΈΡΡΠ΅Π½ΡΠ½ΠΎΡΡΠΈ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΊ ΡΠΏΠΎΠ½ΡΠ°Π½Π½ΠΎΠΌΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Ρ, Π°ΠΊΡΠΈΠ²ΠΈΡΡΠ΅ΠΌΠΎΠΌΡ ΠΏΡΠΈ ΡΡΠ°ΡΡΠΈΠΈ ΡΡΠΎΠ³ΠΎ ΡΠ΅Π³ΡΠ»ΡΡΠΎΡΠ° ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ Π³ΠΈΠ±Π΅Π»ΠΈ. ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΎ, ΡΡΠΎ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ Π±Π΅Π»ΠΊΠ° Ρ53 Π½Π΅Π³Π°ΡΠΈΠ²Π½ΠΎ Π²Π»ΠΈΡΠ΅Ρ Π½Π° ΡΠ°Π·Π²ΠΈΡΠΈΠ΅ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ, ΠΎΠ±ΡΡΠ»ΠΎΠ²Π»Π΅Π½Π½ΠΎΠΉ Π‘.trachomatis.
ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΡΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΠ°Π»ΡΠ½ΠΎ ΠΏΡΠΎΠ΄Π΅ΠΌΠΎΠ½ΡΡΡΠΈΡΠΎΠ²Π°Π½ΠΎ, ΡΡΠΎ ΠΈΠ΄Π΅Π½ΡΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΠ΅ Π±ΠΈΠΎΠΌΠΎΠ»Π΅ΠΊΡΠ»Ρ, ΠΎΡΠ²Π΅ΡΡΡΠ²Π΅Π½Π½ΡΠ΅ Π·Π° ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΠ΅ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°, ΠΊΠ°ΠΊ Ρ ΡΠ°ΠΌΠΈΡ ΠΏΠ°ΡΠΎΠ³Π΅Π½ΠΎΠ², ΡΠ°ΠΊ ΠΈ Ρ Ρ ΠΎΠ·ΡΠΉΡΠΊΠΎΠΉ ΠΊΠ»Π΅ΡΠΊΠΈ, ΡΠ²Π»ΡΡΡΡΡ ΠΏΠ΅ΡΡΠΏΠ΅ΠΊΡΠΈΠ²Π½ΡΠΌΠΈ ΠΌΠΈΡΠ΅Π½ΡΠΌΠΈ Π΄Π»Ρ ΠΏΠΎΠΈΡΠΊΠ° Π½ΠΎΠ²ΡΡ Π°Π½ΡΠΈΠ±Π°ΠΊΡΠ΅ΡΠΈΠ°Π»ΡΠ½ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ².
ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΠΏΡΠΎΠ΄Π΅ΠΌΠΎΠ½ΡΡΡΠΈΡΠΎΠ²Π°Π½ΠΎ, ΡΡΠΎ ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΡΠΈΡΡΠ΅ΠΌΡ ΡΠ΅ΠΊΡΠ΅ΡΠΈΠΈ III ΡΠΈΠΏΠ° Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ Π½Π° ΡΠ°Π½Π½ΠΈΡ ΡΡΠ°ΠΏΠ°Ρ ΠΆΠΈΠ·Π½Π΅Π½Π½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° Π²ΠΎΠ·Π±ΡΠ΄ΠΈΡΠ΅Π»Ρ ΠΏΡΠΈΠ²ΠΎΠ΄ΠΈΡ ΠΊ ΠΈΠ½Π΄ΡΠΊΡΠΈΠΈ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Π² ΠΈΠ½ΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ ΠΊΠ»Π΅ΡΠΊΠ°Ρ Ρ ΠΏΡΠ΅ΠΊΡΠ°ΡΠ΅Π½ΠΈΠ΅ΠΌ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ.
ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ ΠΌΠΎΠ΄ΡΠ»ΡΡΠΎΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΡΠ½Π΄ΠΎΠ³Π΅Π½Π½ΡΡ ΡΠΈΠ³Π½Π°Π»ΡΠ½ΡΡ ΠΏΡΡΠ΅ΠΉ Π²ΡΠΆΠΈΠ²Π°Π½ΠΈΡ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΏΠΎΠ΄Π°Π²Π»ΡΠ΅Ρ ΡΠ°Π·Π²ΠΈΡΠΈΠ΅ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ Ρ ΠΌΡΡΠ΅ΠΉ, ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ ΠΎΠ±Π»Π°Π΄Π°Π΅Ρ ΠΏΡΠΎΡΠ΅ΠΊΡΠΈΠ²Π½ΡΠΌ ΡΡΡΠ΅ΠΊΡΠΎΠΌ ΠΎΡ Π»Π΅ΡΠ°Π»ΡΠ½ΠΎΠΉ Π΄ΠΎΠ·Ρ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ.
ΠΡΠ°ΠΊΡΠΈΡΠ΅ΡΠΊΠ°Ρ Π·Π½Π°ΡΠΈΠΌΠΎΡΡΡ.
Π Π°Π·ΡΠ°Π±ΠΎΡΠ°Π½Ρ ΠΎΡΠΈΠ³ΠΈΠ½Π°Π»ΡΠ½ΡΠ΅ ΡΠΊΡΠΈΠ½ΠΈΠ½Π³ΠΎΠ²ΡΠ΅ ΡΠΈΡΡΠ΅ΠΌΡ Π΄Π»Ρ ΠΊΠΎΠ»ΠΈΡΠ΅ΡΡΠ²Π΅Π½Π½ΠΎΠΉ ΠΎΡΠ΅Π½ΠΊΠΈ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ in vitro.
ΠΠΏΡΠΎΠ±ΠΈΡΠΎΠ²Π°Π½Ρ ΠΌΠ΅ΡΠΎΠ΄Ρ Π΄Π»Ρ Ρ Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΡΡΠΈΠΊΠΈ Π°Π½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ Π² ΠΊΡΠ»ΡΡΡΡΠ΅ ΠΊΠ»Π΅ΡΠΎΠΊ. ΠΡΠ΅Π΄Π»ΠΎΠΆΠ΅Π½Ρ ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΡΡ, ΠΌΠΎΠ΄ΡΠ»ΠΈΡΡΡΡΠΈΡ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ ΠΏΠ°ΡΠΎΠ³Π΅Π½Π° Ρ ΡΠΈΡΡΠ΅ΠΌΠΎΠΉ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Ρ ΠΎΠ·ΡΠΉΡΠΊΠΎΠΉ ΠΊΠ»Π΅ΡΠΊΠΈ Π΄Π»Ρ ΡΠΎΠ·Π΄Π°Π½ΠΈΡ ΠΌΠ΅ΡΠΎΠ΄ΠΈΡΠ΅ΡΠΊΠΎΠΉ Π±Π°Π·Ρ Π² ΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΠΈ ΡΠ°Π·ΡΠ°Π±ΠΎΡΠΊΠΈ ΠΌΠΈΡΠ΅Π½Ρ Π½Π°ΠΏΡΠ°Π²Π»Π΅Π½Π½ΠΎΠ³ΠΎ ΠΏΠΎΠΈΡΠΊΠ° Π»Π΅ΠΊΠ°ΡΡΡΠ²Π΅Π½Π½ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ² Π½ΠΎΠ²ΠΎΠ³ΠΎ ΠΏΠΎΠΊΠΎΠ»Π΅Π½ΠΈΡ, Π²Π»ΠΈΡΡΡΠΈΡ Π½Π° ΠΎΡΠ½ΠΎΠ²Ρ ΠΏΠ°ΡΠΎΠ³Π΅Π½Π½ΠΎΡΡΠΈ Π²ΠΎΠ·Π±ΡΠ΄ΠΈΡΠ΅Π»Ρ.
Π²ΡΠ²ΠΎΠ΄Ρ.
1. ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ Π²Π΅Π³Π΅ΡΠ°ΡΠΈΠ²Π½ΡΠ΅, ΠΌΠ΅ΡΠ°Π±ΠΎΠ»ΠΈΡΠ΅ΡΠΊΠΈ Π°ΠΊΡΠΈΠ²Π½ΡΠ΅ ΡΠΎΡΠΌΡ Π‘. trachomatis Π½Π° ΡΡΠ΅Π΄Π½Π΅ΠΉ ΡΡΠ°Π΄ΠΈΠΈ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° ΡΠ°Π·Π²ΠΈΡΠΈΡ Π·Π°ΡΠΈΡΠ°ΡΡ ΡΡΠΊΠ°ΡΠΈΠΎΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΎΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°, ΠΈΠ½Π΄ΡΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΡΡΠ°ΡΡΠΎΡΠΏΠΎΡΠΈΠ½ΠΎΠΌ ΠΈ ΡΠ°Π·Π²ΠΈΠ²Π°ΡΡΠ΅Π³ΠΎΡΡ ΠΏΠΎ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠΌΡ ΠΏΡΡΠΈ. ΠΠ° ΡΠ°Π½Π½Π΅ΠΉ ΡΡΠ°Π΄ΠΈΠΈ ΠΆΠΈΠ·Π½Π΅Π½Π½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΡ ΠΈΠ½Π΄ΡΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Π½Π΅ Π½Π°Π±Π»ΡΠ΄Π°Π΅ΡΡΡ, ΡΡΠΎ ΠΏΡΠΈΠ²ΠΎΠ΄ΠΈΡ ΠΊ ΡΠ΅Π·ΠΊΠΎΠΌΡ ΡΠ½ΠΈΠΆΠ΅Π½ΠΈΡ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ .
2. ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ C. trachomatis Π½Π° Π²Π½Π΅ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΡΡΠ°Π΄ΠΈΠΈ ΠΆΠΈΠ·Π½Π΅Π½Π½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° Π²ΡΠ·ΡΠ²Π°Π΅Ρ Π°ΠΊΡΠΈΠ²Π°ΡΠΈΡ ΡΡΠ°Π½ΡΠΊΡΠΈΠΏΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΡΠ°ΠΊΡΠΎΡΠ° NF-kB ΠΏΠΎΡΡΠ΅Π΄ΡΡΠ²ΠΎΠΌ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΡ ΡΠ»Π΅ΠΌΠ΅Π½ΡΠ°ΡΠ½ΡΡ ΡΠ΅Π»Π΅Ρ Ρ ΡΠ΅ΡΠ΅ΠΏΡΠΎΡΠ½ΡΠΌ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠΌ TLR4/MD2/CD14 Π½Π° ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Π΅ ΡΡΠΊΠ°ΡΠΈΠΎΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΊΠ»Π΅ΡΠΊΠΈ.
3. ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΎ, ΡΡΠΎ C. trachomatis ΠΏΠΎΠ΄Π°Π²Π»ΡΠ΅Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΠΎΠ΄Π½ΠΎΠ³ΠΎ ΠΈΠ· ΠΊΠ»ΡΡΠ΅Π²ΡΡ ΡΠ΅Π³ΡΠ»ΡΡΠΎΡΠΎΠ² Π°ΠΏΠΎΠΏΡΠΎΠ·Π°, Π±Π΅Π»ΠΊΠ° Ρ53, Π½Π° ΡΡΠ°ΠΏΠ΅ Π°ΠΊΡΠΈΠ²Π½ΠΎΠ³ΠΎ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠ³ΠΎ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΠΏΠ°ΡΠΎΠ³Π΅Π½Π°. ΠΡΠΎ ΠΏΡΠΈΠ²ΠΎΠ΄ΠΈΡ ΠΊ ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΠΏΠ°ΡΠΎΠ³Π΅Π½ΠΎΠΌ Ρ53- Π·Π°Π²ΠΈΡΠΈΠΌΠΎΠ³ΠΎ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°. Π ΡΠ²ΠΎΡ ΠΎΡΠ΅ΡΠ΅Π΄Ρ, Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ Π±Π΅Π»ΠΊΠ° Ρ53 Π½Π΅Π³Π°ΡΠΈΠ²Π½ΠΎ Π²Π»ΠΈΡΠ»Π° Π½Π° ΡΠ°Π·Π²ΠΈΡΠΈΠ΅ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ Π² ΠΊΡΠ»ΡΡΡΡΠ΅ ΠΊΠ»Π΅ΡΠΎΠΊ.
4. ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΡ, Π²ΡΠ·Π²Π°Π½Π½Π°Ρ C. trachomatis, Π½Π° ΡΠ°Π½Π½ΠΈΡ ΡΡΠ°ΠΏΠ°Ρ ΠΆΠΈΠ·Π½Π΅Π½Π½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° Π°ΠΊΡΠΈΠ²ΠΈΡΡΠ΅Ρ ΠΎΡΠ½ΠΎΠ²Π½ΠΎΠΉ' ΡΠ½Π΄ΠΎΠ³Π΅Π½Π½ΡΠΉ ΠΏΡΡΡ Π²ΡΠΆΠΈΠ²Π°Π½ΠΈΡ ΠΊΠ»Π΅ΡΠΊΠΈ, ΠΎΠΏΠΎΡΡΠ΅Π΄ΠΎΠ²Π°Π½Π½ΡΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡΡ ΠΏΡΠΎΡΠ΅ΠΈΠ½ΠΊΠΈΠ½Π°Π·Ρ-Π.
5. ΠΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΠ΅ ΡΠΈΡΡΠ΅ΠΌΡ ΡΠ΅ΠΊΡΠ΅ΡΠΈΠΈ III ΡΠΈΠΏΠ° Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ΅ΡΠΊΠΈΠΌ ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΡΠΎΠΌ ΠΏΡΠΈΠ²ΠΎΠ΄ΠΈΡ ΠΊ Π°ΠΊΡΠΈΠ²Π°ΡΠΈΠΈ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Π² ΠΈΠ½ΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ ΠΊΠ»Π΅ΡΠΊΠ°Ρ ΠΈ ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΡ ΡΠ°Π·Π²ΠΈΡΠΈΡ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ.
6. ΠΠΎΠ΄ΡΠ»ΡΡΠΎΡ ΠΏΡΠΎΡΠ΅ΡΡΠΎΠ² ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ Π³ΠΈΠ±Π΅Π»ΠΈ ΠΈ ΠΏΡΠΎΠ»ΠΈΡΠ΅ΡΠ°ΡΠΈΠΈ — ΠΏΡΠ΅ΠΏΠ°ΡΠ°Ρ ΡΠ΅ΡΠ²Π΅ΡΠ°ΡΡΠΎΠ»Π²ΡΠ·ΡΠ²Π°Π΅Ρ ΠΏΠΎΠ²ΡΡΠ΅Π½ΠΈΠ΅ ΡΡΠΎΠ²Π½Ρ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Π² ΠΊΡΠ»ΡΡΡΡΠ΅ ΠΈΠ½ΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ, ΡΡΠΎ ΠΏΡΠΈΠ²ΠΎΠ΄ΠΈΡ ΠΊ ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΡ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉΠ½ΠΎΠΉ ΠΈΠ½ΡΠ΅ΠΊΡΠΈΠΈ Π² ΡΡΠ»ΠΎΠ²ΠΈΡΡ in vitro.
7. ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ ΡΠ΅ΡΠ²Π΅ΡΠ°ΡΡΠΎΠ» ΠΏΠΎΠ΄Π°Π²Π»ΡΠ΅Ρ Π½Π°ΠΊΠΎΠΏΠ»Π΅Π½ΠΈΠ΅ C. muridarum Π² Π»Π΅Π³ΠΊΠΈΡ ΡΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΠ°Π»ΡΠ½ΠΎ ΠΈΠ½ΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ ΠΆΠΈΠ²ΠΎΡΠ½ΡΡ ΠΈ Π·Π°ΡΠΈΡΠ°Π΅Ρ ΠΎΡ ΡΠ°Π·Π²ΠΈΡΠΈΡ Π»Π΅ΡΠ°Π»ΡΠ½ΠΎΠΉ ΠΏΠ½Π΅Π²ΠΌΠΎΠ½ΠΈΠΈ Ρ ΠΌΡΡΠ΅ΠΉ.
Π‘ΠΏΠΈΡΠΎΠΊ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- Π£ΠΌΠ°Π½ΡΠΊΠΈΠΉ Π‘.Π . ΠΠΏΠΎΠΏΡΠΎΠ·: ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΠ΅ ΠΈ ΠΊΠ»Π΅ΡΠΎΡΠ½ΡΠ΅ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΡ // ΠΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½Π°Ρ Π±ΠΈΠΎΠ»ΠΎΠ³ΠΈΡ.- 1996.-Π’. 30.-β. 3.- Π‘. 487−502.
- ΠΠ΄Π΅Π»ΡΡΠΏΠ΅ΠΉΠ½ Π. Π. Π€ΡΠ½Π΄Π°ΠΌΠ΅Π½ΡΠ°Π»ΡΠ½ΡΠ΅ ΠΈΠ·ΠΌΠ΅Π½Π΅Π½ΠΈΡ Π² ΠΊΠ»Π°ΡΡΠΈΡΠΈΠΊΠ°ΡΠΈΠΈ Ρ Π»Π°ΠΌΠΈΠ΄ΠΈΠΉ ΠΈ ΡΠΎΠ΄ΡΡΠ²Π΅Π½Π½ΡΡ ΠΈΠΌ ΠΌΠΈΠΊΡΠΎΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠΎΠ² ΠΏΠΎΡΡΠ΄ΠΊΠ° Chlamydiales // ΠΠΠΠ₯ -1999.-Π’.1.-β.1.- Π‘.5−11.
- Π―ΡΠΈΠ»ΠΈΠ½ Π.Π. ΠΠΏΠΎΠΏΡΠΎΠ·: ΠΏΡΠΈΡΠΎΠ΄Π° ΡΠ΅Π½ΠΎΠΌΠ΅Π½Π° ΠΈ Π΅Π³ΠΎ ΡΠΎΠ»Ρ Π² Π½ΠΎΡΠΌΠ΅ ΠΈ ΠΏΡΠΈ ΠΏΠ°ΡΠΎΠ»ΠΎΠ³ΠΈΠΈ // ΠΠΊΡΡΠ°Π»ΡΠ½ΡΠ΅ ΠΏΡΠΎΠ±Π»Π΅ΠΌΡ ΠΏΠ°ΡΠΎΡΠΈΠ·ΠΈΠΎΠ»ΠΎΠ³ΠΈΠΈ. ΠΠΎΠ΄ ΡΠ΅Π΄. Π. Π. ΠΠΎΡΠΎΠ·Π°. Π.: ΠΠ΅Π΄ΠΈΡΠΈΠ½Π°, 2001.-Π‘. 13−56.
- Amoult D, Gaume Π, Karbowski Π, Sharpe JC Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization EMBO J. 2003 Sep l-22(17):4385−99
- Attardi L.D., Reczek E.E., Cosmas C. et al. PERP, an apoptosis-associated target of p53, is a novel member of the PMP-22/gas3 family // Genes & Dev.-200.-Vol. 14.-β.6.-P. 704−718
- Au J., Panchal N., Li D. Apoptosis: a new pharmacodynamic endpoint // Pharm.Res.-1997.-Vol.14.- β.12.-P. 1659−1671.
- Backert S., Selbach M. Tyrosine-phosphorylated bacterial effector proteins: the enemies within. Trends Microbiol. 2005, — Vol. 13, — β.10.- P. 476−484.
- Bai S., Liu H., Kun-Hung C. NF-ΠΊΠ-regulated expression of cellular FLIP protects rheumatoid arthritis synovial fibroblasts from tumor necrosis factor a-mediated apoptosis // Arthritis and rheumatism 2004.- Vol. 50.-β.12.- P. 3844−3855
- Balsara Z., Misaghi S., Lafave J. et al. Chlamydia trachomatis Infection Induces Cleavage of the Mitotic Cyclin B1 // Infect Immun. 2006, — Vol. 74.-β.10.-P. 56 025 608.
- Bannantine J. P., Rockey D.D., Hackstadt T. Tandem genes of Chlamydia psittaci that encode proteins localized to the inclusion membrane // Molecular Microbiology.-1998.-Vol. 28.-β.5,-P. 1017−1026
- Bao Q, Shi Y. Apoptosome: a platform for the activation of initiator caspases// Cell Death and Differentiation.-2007.- Vol.14.- P. 56−65
- Baron. S. Medical Microbiology // 4th ed.- U. of Texas, Galveston, 1996.- 348 p.
- Baumgartner H.K., Gerasimenko J.V., Thome C. et al. Caspase-8-mediated apoptosis induced by oxidative stress is independent of the intrinsic pathway and dependent on cathepsins // Am J Physiol Gastrointest Liver Physiol-2007. Vol. 293.- β.1.- P.296−307
- Bavoil P.M., Wyrick P. Chlamydia: genomics and pathogenesis // Horizon Bioscience, Norfolk, United Kingdom.- 2006.- 542 p.
- Beiland R.J., Zhong G., Crane D.D.et al. Genomic transcriptional profiling of the developmental cycle of Chlamydia trachomatis // PNAS- 2003.- Vol. 100.-β.1.-P.48 478−8483.
- Bender L, M., Morgan M. J., Thomas L. R. et al. The adaptor protein TRADD activates distinct mechanisms of apoptosis from the nucleus and the cytoplasm// Cell Death Differ -2005.- Vol. 12.- β.5, — P. 473−481.
- Bennett M., Macdonald K., Chan S.W. et al. Cell surface trafficking of Fas: a rapid mechanism of p53-mediated apoptosis.// Science.- 1998.- Vol.282.- β.5387.-P.290−293
- Bernal-Mizrachi L., Lovly C., Ratner L. The role of NF-kB-1 and NF-KB-2-mediated resistance to apoptosis in lymphomas // PNAS 2006.- Vol. 103.-β. 24.-P. 9220−9225
- Billen L.P., Kokoski C.L., Lovell J.F. et al. Bcl-XL inhibits membrane permeabilization by competing with Bax.// PLoS Biol. -2008.- Vol.6.-β.6.-1268−1280.
- Birbes H., Bawab S., Obeid L. et al. Mitochondria and ceramide: intertwined roles in regulation of apoptosis//Adv. Enzyme Regul 2002.- Vol.42.- P. 113−129
- Bonizzi G., Karin M. The two NF-kB activation pathways and their role in innate and adaptive immunity // Trends in Immunology.-2004.- Vol.25.- β.6.- P.280−288
- Boulares A.H., Yakovlev A.G., Ivanova V. et al. Role of Poly (ADP-ribose) Polymerase (PARP) cleavage in apoptosis: caspase 3-resistant PARP mutant rates of apoptosis in transfected cells // J Biol Chem.-1999.- Vol. 274.-β.33.- P. 22 932−22 940
- Brasier A.R. The NF-kB regulatory network // Cardiovasc. Toxicol. 2006. — Vol.6.-β.2.-P. 111−130.
- Brunet A., Bonni A., Zigmond M. et al. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor // Cell- 1999.- Vol. 96.- β.6.- P. 857−868
- Brutinel E.D., Yahr T.L. Control of gene expression by type III secretory activity //Curr Opin. Microbiol.-2008.-Vol.ll.-β.2.-P. 128−133.
- Cahill C. M, Tzivion G., Nasrin N. et al. Phosphatidylinositol 3-kinase signaling inhibits DAF-16 DNA binding and function via 14−3-3-dependent and 14−3-3-independent pathways //J Biol Chem. -2001.- Vol. 276.- β.16.- P. 13 402−13 410.
- Cande C, Cohen I, Daugas E et al. Apoptosis-indueing factor (AIF): a novel caspase-independent death effector released from mitochondria // Biochimie. 2002.- Vol.84.-β.2−3.-P.215−222
- Carabeo R., Grieshaber S., Hasenkrug A. Requirement for the Rae GTPase in Chlamydia trachomatis invasion of non-phagocytic cells// Traffic.- 2004.- Vol. 5.-β.6.-P. 418−425.
- Carabeo R.A., Grieshaber S.S., Fischer E. et al. Chlamydia trachomatis induces remodeling of the actin cytoskeleton during attachment and entry into HeLa cells // Infect.Immun.- 2002.-Vol.70.- β.7.-P. 3793−3803.
- Carlson J.H., Porcella S.F., McClarty G. et al. Comparative genomic analysis of Chlamydia trachomatis oculotropic and genitotropic strains //Infect.Immune.-2005.-Vol. 73.-β. 10.-P. 6407−6418.
- Chauhan D., Li G., Hideshima T. et al. JNK-dependent release of mitochondrial protein, Smac, during apoptosis in multiple myeloma // J Biol Chem.- 2003.- Vol.278.- β.20.-P.17 593−17 596.
- Chen D., Chai J., Hart P. Identifying catalytic residues in CPAF, a Chlamydia-secreted protease// Arch Biochem Biophys -2009.- Vol. 485.- β.1.-P. 16−23
- Cheng E. H, Wei M., Weiler S. et al. BCL-2, BCL-XL Sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis // Molecular Cell.-2001.- Vol. 8.- β.3.-P. 705−711
- Chowdhury I, Tharakan B, Bhat GK. Caspases an update // Comp Biochem Physiol B Biochem Mol Biol. — 2008, — Vol.151.- β.1.- P. 10−27.
- Clifton D.R., Fields K.A., Grieshaber S.S. A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin. Proc. Natl. Acad. Sci.USA.-2004.- Vol: 101, — β.27.- P.10 166−10 171.
- Cory S, Huang DC, Adams JM. The Bcl-2 family: roles in cell survival and oncogenesis // Oncogene.- 2003.-Vol.22.-β.53.-P.8590−8607.
- Creagh E.M., Conroy H., Martin S.J. Caspase-activation pathways in apoptosis and immunity.// Immunol Rev. -2003.- Vol.193.- P.10−21
- Culmsee C., Plesnila N. Targeting Bid to prevent programmed cell death in neurons/ZBiochemical Society Transactions 2006, — Vol.34.-β. 6.-P.1334−1340.
- Datta S.R., Dudek H., Tao X. et al. Akt phosphorylation of BAD couples survival signals to the cell-Intrinsic death machinery// Cell.- Vol. 91.- β. 2. -P. 231−241
- Daugas E, Susin SA, Zamzami N et al. Mitochondrio-nuclear translocation of AIF in apoptosis and necrosis// FASEB J.- 2000.- Vol. l4.-β.5.- P.729−739.
- Delevoye C., Nilges M., Dehoux P. et al. SNARE protein mimicry by an intracellular bacterium// PLoS Pathog.- 2008.- Vol. 4.- β.3.-P. 1−14.
- Dlugosz P., Billen L., Annis G. et al. Bcl-2 changes conformation to inhibit Bax oligomerization// The EMBO Journal 2006.- Vol. 25.-β.l 1.- P.2287−2296.
- Dremina E., Sharov V., Kumar K. Anti-apoptotic protein Bcl-2 interacts with and destabilizes the sarcoplasmic/endoplasmic reticulum Ca2±ATPase (SERCA)// Biochem. J. 2004, — Vol. 383- β.2.-P. 361−370.
- Dremina E.S., Sharov V.S., Schoneich C. Displacement of SERCA from SR lipid caveolae-related domains by Bcl-2: a possible mechanism for SERCA inactivation // Biochemistry. 2006, — Vol.45.-β. 1.- P. 175−84
- Dufour J.F., Clavien P., Trautwein C. et al. Signaling Pathways in Liver Diseases.// Springer, 2005.-442p.
- Dumrese C., Maurus C.F., Gygi D. Chlamydia pneumoniae induces aponecrosis in human aortic smooth muscle cells // BMC Microbiol. -2005 .- Vol.5.-β.2.-P.l-15.
- Earnshaw W., Martins L., Kaufmann S. Mammalian caspases: structure, activation, substrates, and functions during apoptosis.// Annu Rev Biochem .-1999. Vol. 68.-P. 383−424.
- Eley A., Hosseinzadeh S., Hakimi H. et al. Apoptosis of ejaculated human sperm is induced by co-incubation with Chlamydia trachomatis lipopolysaccharide // Hum Reprod.- 2005.- Vol.20.-β.9.-P.2601−267
- Elwell C.A., Ceesay A., Kim J.H. et al. RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry. // PLoS Pathog. 2008.- Vol.4.-β.3.-P. 1−15.
- Embree-Ku M., Venturini D., Boekelheide K. Fas Is Involved in the p53-Dependent Apoptotic Response to Ionizing Radiation in Mouse Testis // Biol Reprod.- 2002.-Vol.66.-β.5.- P.1456−1461
- Equils O., Lu D., Gatter M. et al. Chlamydia heat shock protein 60 induces trophoblast apoptosis through TLR4// J. Immunol. 2006.-Vol. 177.-№ 2.-P. 1257−1263.
- Evan D. Brutinel E.D., Yahr T.L. Control of gene expression by type III secretory activity // Curr Opin Microbiol. -2008.- Vol. 11.- β.2.-P. 128−133.
- Everett K.D., Andersen AA. The ribosomal intergenic spacer and domain I of the 23S rRNA gene are phylogenetic markers for Chlamydia spp.// Int J Syst Bacterid. -1997.-Vol.47.- β. 2.-P.461−473
- Fadel S., Eley A. Chlamydia trachomatis OmcB protein is a surface-exposed glycosaminoglycan-dependent adhesion // Med Microbiol.- 2007.- β. 56.- P. 15−22.
- Fadel S., Eley A. Differential glycosaminoglycan binding of Chlamydia trachomatis OmcB protein from serovars E and LGV // J Med Microbiol.-2008.- β.57.-P.1058−1061.
- Fan T.J., Han L.H., Cong R.S., Liang J. Caspase family proteases and apoptosis. // Acta Biochim Biophys Sin 2005.- Vol.37.-β.l 1.- P.719−727
- Fang X., Yu S., Eder A. et al. Regulation of BAD phosphorylation at serine 112 by the Ras-mitogen-activated protein kinase pathway// Oncogene.- 1999.- Vol.18.- № 48.-P. 6635−6640
- Fields K.A., Hackstadt T. Evidence for the secretion of Chlamydia trachomatis CopN by a type III secretion mechanism // Mol. Microbiol.-2000.-Vol. 38.-β.5.-P. 1048−1060
- Fields K.A., Fischer E., Hackstadt T. Inhibition of fusion of Chlamydia trachomatis inclusions at 32 Β°C correlates with restricted export of IncA //Infect.Immun.- 2000.- Vol. 68,-β. l.-P. 360−367.
- Fields K.A., Mead D.J., Dooley C.A. et al. Chlamydia trachomatis type III secretion: evidence for a functional apparatus during early-cycle development // Mol. Microbiol.-2003.-Vol.48.-β.3.-P. 671−683.
- Findlay HE, McClafferty H, Ashley RH. Surface expression, single-channel analysis and membrane topology of recombinant Chlamydia trachomatis Major Outer Membrane Protein // BMC Microbiol. 2005.-Vol. 26.-β.5.- P.5−20.
- Fujita E., Jinbo A., Matuzaki H. et al. Akt Phosphorylation site found in human Caspase-9 is absent in mouse Caspase-9 // Biochem Biophys Res Coramun.- 1999.-Vol.264.-β.2.-P.550−555.
- Galan JE, Collmer A. Type III Secretion machines: bacterial devices for protein delivery into host cells // Science. -1999.- Vol.284.-β.5418.-P.1322−1328
- Gerard H. C, Freise J., Wang Z. et al. Chlamydia trachomatis genes whose products are related to energy metabolism are expressed differentially in active vs. persistent infection.//Microb.Infect.- 2002.-Vol.4. β.1.-P. 13−22.
- Gerlach R.G., Hensel M. Protein secretion systems and adhesins: The molecular armory of Gram-negative pathogens // Int. J. Med. Microbiol. -2007.-Vol.297.-β.6.-P.401−415.
- Ghosh P. Process of protein transport by the type III secretion system // Microbiol. Mol. Biol. Rev.- 2004. Vol. 68.- β. 4, — P. 771−795
- Gilmore T.D. Introduction to NF-kB: players, pathways, perspectives // Oncogene-2006.-Vol. 25.-β.51.-P. 6680−6684
- Gnesutta N., Minden A. Death receptor-induced activation of initiator Caspase 8 is antagonized by serine/threonine kinase PAK4 // Mol. Cel. Biol.- 2003.- Vol. 23.-β. 21,-P. 7838−7848
- Gottlieb T., Leal J., Seger R. et al. Cross-talk between Akt, p53 and Mdm2: possible implications for the regulation of apoptosis // Oncogene 2002.-Vol.21.-β.8.- P. 12 991 303
- Grieshaber N.A., Sager J.B., Dooley C.A. et al. Regulation of the Chlamydia trachomatis histone HI-like protein Hc2 is IspE dependent and IhtA independent // J. Bacteriol.-2006.- Vol. 188.- β. 14.- P. 5289−5292
- Grinberg M., Sarig R., Zaltsman Y. et al. tBID homooligomerizes in the mitochondrial membrane to induce apoptosis // J.Biol.Chem.-2002.- Vol. 277.-β.14.- P. 12 237−12 245.
- Habelhah H., Takahashi S., Cho S. et al. Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kB//EMBO J. 2004, — Vol. 23.2.- Π .322—332.
- Hackstadt Π’., Scidmore-Carlson M.A., Shaw E.I., Fischer E.R. The Chlamydia trachomatis IncA protein is required for homotypic vesicle fusion.// Cell Microbiol. -1999.-Vol.L- β.2.-P.l 19−130.
- Haimovitz-Friedman A., Kolesnick R.N., Fuks Z. Ceramide signaling in apoptosis //British Medical Bulletin.- 1997.-Vol.53.-β.3.- P. 539−553
- Ho T.D.,. Stambach M.N. The Salmonella enterica serovar Typhimurium-encoded type III secretion systems can translocate Chlamydia trachomatis proteins into the cytosol of host cells //Infect.Immun.-2005.- Vol. 73.- β. 2, — P.905−911
- Holohan C., Szegezdi E., Ritter Π’. et al. Cytokine-induced ?-cell apoptosis is N0-dependent, mitochondria-mediated and inhibited by BCL-XL // J Cell Mol Med.-2007.-Vol.l2.-β.2.~ P. 591 -606
- Hsu H, Shu HB, Pan MG et al. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduc // Cell.- 1996.- Vol.84.-β.2.-P.299−308.
- Huang Z., Feng Y., Chen D. et al, Structural basis for activation and inhibition of the secreted Chlamydia protease CPAF// Cell Host & Microbe.-2008.- Vol.4.-β.6.-P. 529 542
- Hybiske K., Stephens R. Mechanisms of host cell exit by the intracellular bacterium Chlamydia // Proc Natl Acad Sei U S A.- 2007.- Vol.104.- β.27.-P. 11 430−11 435.
- Iliffe-Lee ER, McClarty G. Glucose metabolism in Chlamydia trachomatis: the «energy parasite» hypothesis revisited.// Mol Microbiol. -1999.- Vol.33.- β.1.- P.177−187.
- Isao Miyairi I., Byrne G.I.Chlamydia and programmed cell death Curr Opin Microbiol -2006.- Vol. 9.-β.l.-P. 102−108
- Jewett Π’., Fischer E.R., Mead D.J., Hackstadt Π’. Chlamydial TARP is a bacterial nucleator of actin //PNAS.- 2006.-Vol. 103, — β. 42 P. 15 599−15 604.
- Kandel, E.S., Hay, N., The regulation and activities of the multifunctional serine/threonine kinase Akt/PKB.// Exp Cell Res. -1999.- Vol. 253.- β.1.- P. 210−229
- Kelekar A., Chang B., Harlan J. et al. Bad Is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-xL// Mol. Cel.Biol.- 1997.- Vol. 17.- β. 12.- P. 7040−7046
- Kepp O., Gottschalk K., Churin Y. Bim and Bmf synergize to induce apoptosis in Neisseria gonorrhoeae infection//PLoS Pathogens 2009. — Vol. 5.- β. 3.-1−10.
- Kim D., Kim S., Lee J. et al. Sphingosine-1 -phosphate-induced ERK activation protects human melanocytes from UVB-induced apoptosis// Arch Pharm Res.-2003.- Vol. 26.-β.9.- P.739−746
- Kim J., Kim K, Leeb E. Up-regulation of Bfl-l/Al via NF-kB activation in cisplatin-resistant human bladder cancer cell line // Cancer Letters 2004. -Vol. 212.-β.1.- P. 61−70
- Klee M., Pallauf K., Alcala S. et al. Mitochondrial apoptosis induced by BH3-only molecules in the exclusive presence of endoplasmic reticular Bak // The EMBO Journal -2009.-Vol. 28.-P. 1757 1768
- Kohout S., Corbalan-Garcia S., Torrecillas A. et al. C2 domains of protein kinase C isoforms alpha, beta, and gamma: activation parameters and calcium stoichiometrics of the membrane-bound state.//Biochemistry 2002.- Vol.41 .-β.38.-P.l 1411−11 424.
- Kubo A, Stephens RS. Characterization and functional analysis of PorB, a Chlamydia porin and neutralizing target // Mol Microbiol.- 2000.- Vol.38.-β.4.-P.772−780.
- Kubo A, Stephens RS. Substrate-specific diffusion of select dicarboxylates through Chlamydia trachomatis PorB // Microbiology. 2001.- Vol.147.- β.11.-P.3135−3140.
- Kumar Y., Valdivia R.H. Actin and intermediate filaments stabilize the Chlamydia trachomatis vacuole by forming dynamic structural scaffolds // Cell Host Microbe.-2008.- Vol.4.- β.2, — P. 159−69
- Kuribara R., Honda H., Matsui H. et al. Roles of Bim in apoptosis of normal and Bcr-Abl-expressing hematopoietic progenitors // Mol. Cel. Biol.- 2004.- Vol. 24.- β. 14. -P. 6172−6183
- Kwon D.S., Kwon C.H., Kim J.H. et al. Signal transduction of MEK/ERK and PI3K/Akt activation by hypoxia/reoxygenation in renal epithelial cells.// Eur J Cell Biol. 2006.- Vol.85.-β. 11.- P. 1189−1199.
- Landshamer S., Hoehn M., Barth N. et al. Bid-induced release of AIF from mitochondria causes immediate neuronal cell death// Cell Death Differ. 2008.- Vol. l5.-β.10.-P.1553−1563
- Lane B.J., Mutchler C., Khodor S. et al Chlamydial entry involves TARP binding ofiguanine nucleotide exchange factors // PLoS Pathog. 2008 Vol. 4.-β.3.- P. l-11
- Le Negrate G., Krieg A., Faustin B. et al. ChlaDubl of Chlamydia trachomatis suppresses NF-kappaB activation and inhibits IkappaBalpha ubiquitination and degradation. // Cell Microbiol. -2008.-Vol.10.-β.9.-P. 1879−1892
- LeBlanc HN, Ashkenazi A. Apo2L/TRAIL and its death and decoy receptors // Cell Death Differ 2003.-Vol. 10.- β.l.-P.66−75
- Li H, Zhu H, Xu CJ, Yuan J Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis.// Cell 1998.- Vol.94.-β.4.-P.491−501.
- Li J, Lee B, Lee AS. Endoplasmic reticulum stress-induced apoptosis: multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53.//J Biol Chem.- 2006.-Vol.281.-β.11.-P.7260−7270.
- Li Z., Chen C., Chen D. et al. Characterization of fifty putative inclusion membrane proteins encoded in the Chlamydia trachomatis genome.// Infect Immun. 2008.-Vol. 76.-β.6.- P. 2746−2757.
- Liu J., Lin A. Role of JNK activation in apoptosis: A double-edged sword // Cell Research- 2005.-Vol. 15.-β.1.-P. 36−42.
- Los M., Gibson S.B. Apoptotic pathways as targets for novel therapies in cancer and other diseases.- Business Media, 2005.-P.395.
- Los M., Mozoluk M., Ferrari D. et al. Activation and caspase-mediated inhibition of PARP: A molecular switch between fibroblast necrosis and apoptosis in death receptor signaling//MBC.- 2002.-Vol. 13.-β.3.-P. 978−988.
- Lu B., Wang L., Stehlik C. Phosphatidylinositol 3-Kinase/Akt positively regulates Fas (CD95)-mediated apoptosis in epidermal C141 cells// J Immunol. 2006 .- Vol. 176.-β.11.-P. 6785−6793
- Lu M. L, Sato M, Cao B. UV irradiation-induced apoptosis leads to activation of a 36-kDa myelin basic protein kinase in HL-60 cells// Proc Natl Acad Sci U S A 1996.-Vol. 93.-β.17.-P. 8977−8982
- Lukacova M, Baumann M, Brade L, et al. Lipopolysaccharide smooth-rough phase variation in bacteria of the genus Chlamydia//Infect Immun.- 1994.-Vol.62.- № 6,-P.2270−2276.
- MacLachlan T., El-Deiry W. Apoptotic threshold is lowered by p53 transactivation of caspase-6 // Proc Natl Acad Sci USA- 2002.-Vol. 99.-β.14.-P. 9492−9497.
- Majeed M., Kihlstrom E. Mobilization of F-actin and clathrin during redistribution of Chlamydia trachomatis to an intracellular site in eucaryotic cells // Infect Immun. -1991. -Vol. 59.- β.12.- P. 4465−4472.
- Marani M., Tenev T., Hancock D. et al. Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis// Mol.Cel. Biol.2002.- Vol. 22, — β. 11.- P. 3577−3589
- Marek L., Henning W. Caspases: their role in cell death and cell survival.- Hardcover, 2003.- 260p.
- Marek L., Henning W. Caspases: their role in cell death and cell survival.- Hardcover, 2003.- 260p.
- Marra F, Delogu W, Petrai I et al. Differential requirement of members of the MAPK family for CCL2 expression by hepatic stellate cells // Am J Physiol Gastrointest Liver Physiol. -2004.- Vol.287.-β. 1 .-P. 18−26
- Marsters S., Sheridan J.P., Pitti R. et al. Identification of a ligand for the death-domain-containing receptor Apo3 //Current Biology.-1998.- Vol. 8.-β.9.-P. 525−562.
- Martins M., Iaccarino I., Tenev T. The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif// J Biol Chem 2002.-Vol. 277.-β.l.- P. 439−444
- Masters S.C., Yang H., Datta S.R. et al. 14−3-3 inhibits Bad-induced cell death through interaction with serine-136 // Mol Pharmacol.- 2001.- Vol.60.- β.6.- P.1325−1331.
- Mayer B., Oberbauer R. Mitochondrial regulation of apoptosis// News Physiol Sci.-2003.-Vol. 18.-β.3.-P. 89−94.
- McCoy A.J., Maurelli A.T. Building the invisible wall: updating the chlamydial peptidoglycan anomaly // Trends in Microbiology 2006,-Vol. 14.- β.2.- P. 70−77
- Mignotte B, Vayssiere JL. Mitochondria and apoptosis // Eur J Biochem. -1998.-Vol.252.-β.l.- P. 1−15
- Misaghi S., Balsara Z.R., Catic A. et al. Chlamydia trachomatis-derived deubiquitinating enzymes in mammalian cells during infection. // Mol Microbiol. 2006.-Vol.61.-β.1.-P. 142−50i
- Mochizuki T., Asai A., Saito N. Akt protein kinase inhibits non-apoptotic programmed cell death induced by ceramide // J. Biol. Chem.-2002.- Vol. 277.-β.4.- P.2790−2797
- Moelleken K., Hegemann J.H. The Chlamydia outer membrane protein OmcB is required for adhesion and exhibits biovar-specific differences in glycosaminoglycan binding // Mol Microbiol.- 2008.- Vol.67.-β.2.- P. 40319.
- Molestina R., Miller R. Requirement for NF-kB in Transcriptional Activation of Monocyte Chemotactic Protein 1 by Chlamydia pneumoniae in Human Endothelial Cells //Infect.Immun.- 2000.- Vol. 68.- β. 7.- P. 4282−4288.
- Moraes T.F., Spreter T., Strynadka N. Piecing together the Type III injectisome of bacterial pathogens // Curr. Opin. Struct. Biol.- 2008.-Vol.l8.-N.2.- P.258−266.
- Morgan M., Thorburn J., Pandolfi P. P et al. Nuclear and cytoplasmic shuttling of TRADD induces apoptosis via different mechanisms// JCB.-2002.-Vol.-157.-β. 6.- P. 975−984
- Moroni M.C., Hickman E.S., Denchi E. et al. Apaf-1 is a transcriptional target for E2 °F and p53//Nature cell biology.-2001.-Vol. 3.-β.6.-P.552−558.
- Mukhopadhyay S., Good D., Miller R. Identification of Chlamydia pneumoniae Proteins in the Transition from Reticulate to Elementary Body Formation // Molecular & Cellular Proteomics -2006.- Vol.5.-β.12.- P.2311−2318.
- Muraoka R.S., Dumont N., Ritter C. Blockade of TGF-P inhibits mammary tumor cell viability, migration, and metastases // J. Clin. Invest. 2002.- Vol.109.- β.12.- P. 1551−1559
- Nakajima W, Tanaka N. Synergistic induction of apoptosis by p53-inducible Bcl-2 family proteins Noxa and Puma // J Nippon Med Sch. 2007.-Vol.74.-β.2.- P.148−157
- Neff L., Daher S., Muzzin P. Molecular characterization and subcellular localization of Macrophage infectivity potentiator, a Chlamydia trachomatis lipoprotein // J. Bacteriol.-2007.- Vol. 189.- № 13.- P. 4739−4748.
- Nguyen J.T., Wells J.A.Direct activation of the apoptosis machinery as a mechanism to target cancer cells // PNAS.- 2003, — Vol. 100.- β. 13.- P. 7533−7538
- Ni H., Chen X., Shi Y. et al. Genetic delineation of the pathways mediated by Bid and JNK in Tumor Necrosis Factor-a-induced liver injury in adult and embryonic mice // J. Biol. Chem.-2009.- Vol. 284.- β.7.-P. 4373−4382
- Nicholson K.M., Anderson N.G. The protein kinase B/Akt signalling pathway in human malignancy. Cell Signal. 2002.- Vol.14.- β.5.- P.381−395
- Ninomiya E., Ito Y., Shibata M. et al. The activation of caspase-3 and DNA fragmentation in B cells phagocytosed by macrophages // Med Electron Microsc. -2003.- Vol. 36.- β.2, — P. 87−93
- Obsilova V., Silhan J., Boura E. et al. 14−3-3 proteins: a family of versatile molecular regulators // Physiol Res. 2008.- Vol.57.-β.3.- P. l 1−21.
- Oda E., Ohki R., Murasawa H. et al. Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis.// Science. 2000.- Vol. 288.-β.5468.-P.1053−1058
- Ogawara Y., Kishishita S., Obata T. et al. Akt enhances Mdm2-mediated ubiquitination and degradation of p53.// J Biol Chem. 2002.- Vol.277.-β.24.-P.21 843−21 850.
- Ooij C., Apodaca G., Engel J. Characterization of the Chlamydia trachomatis vacuole and its interaction with the host endocytic pathway in HeLa cells // Infect. Immun.-1997.-Vol.65.-β.2.-P.758−766.
- Ouellette S.P., Rahman Y.M., Belland R.J.et al. The Chlamydia pneumoniae type III secretion-related lcrH gene clusters are developmentally expressed operons // J. Bacterid. 2005.- Vol. 187.- β. 22.- P. 7853−7856
- Pallen M.J., Bailey C.M., Beatson S.A. Evolutionary links between FliH/YscL-like proteins from bacterial type III secretion systems and second-stalk components of the FoFl and vacuolar ATPases.//Protein Sei. -2006.-Vol.l5.-β.4.-P.935−941.
- Park H.H., Wu H. Crystal Structure of RAIDD Death Domain Implicates Potential Mechanism of PIDDosome Assembly// J Mol Biol.-2006.- Vol.357.-β.2.- P.358−364
- Paschen S.A., Christian J.G., Vier J. et al. Cytopathicity of Chlamydia is largely reproduced by expression of a single chlamydial protease //J Cell Biol. 2008.-Vol.l82.-β.l.-P. 117−127
- Pearson G., Robinson F., Beers G. T, et al. Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions // Endocr. Rev.2001.-Vol. 22.-β.2.-P.153−183.
- Peeling R. W, Peeling J, Brunham R.C. High-resolution 31P nuclear magnetic resonance study of Chlamydia trachomatis: induction of ATPase activity in elementary bodies.// Infect Immun. -1989.- Vol.57.-β.l 1.- P.3338−3344.
- Peng J., Tan C., Roberts GJ. et al. tBid elicits a conformational alteration in membrane-bound Bcl-2 such that it inhibits Bax pore formation //J Biol Chem. 2006 Vol.281.-β.47.-P.35 802−35 811.
- Perfettini J. L, Ojcius D. M, Andrews C. W et al. Role of proapoptotic BAX in propagation of Chlamydia muridarum (the mouse pneumonitis strain of Chlamydia trachomatis) and the host inflammatory response.// J Biol Chem.- 2003.-Vol. 278.-β.ll.-P.9496−502
- Perkins N.D. Integrating cell-signalling pathways with NF-kB and IKK function. Nat. Rev. Mol. Cell Biol. -2007. -Vol.8.-β.l.-P. 49−62.
- PesoL., Gonzalez-Garcia M., Page C. et al. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt// Science.-1997.-Vol. 278.-β. 5338.- P. 687−689.
- Peters J.M., Wilson D.P., Myers G. et al. Type III Secretion a la Chlamydia // Trends In Microbiology.-2007.-Vol.l5.-β.6.-P. 241−251.
- Pirbhai M., Dong F., Zhong Y. et al. The secreted protease factor CPAF is responsible for degrading proapoptotic BH3-only proteins in C. trachomatis-infected cells // J. Biol. Chem.-2006.- Vol. 281.-β.42.-P. 31 495−31 501.
- Prebeck S., Kirschning C., Durr S. et al. Predominant role of Toll-Like Receptor 2 versus 4 in Chlamydia pneumoniae-induced activation of dendritic cells // J. Immunol.-2001.-Vol. 167.-β. 6.- P. 3316−3323.
- Rajalingam K., Sharma M., Lohmann C. Mcl-1 is key regulator of apoptosis resistance in Chlamydia trachomatis-infected cells//PlosOne 2008.-Vol.3.-β.9.-P.l-l 1.
- Rakesh Srivastava Apoptosis, cell signaling, and human diseases: molecular mechanisms -Humana Press, 2007. 402 p.
- Ravagnan L., Gurbuxani S., Susin S. et al. Heat-shock protein 70 antagonizes apoptosis-inducing factor//Nature Cell Biology-2001.-β. 3.- P. 839 843
- Reed J., Cardone M. Caspase phosphorylation, cell death, and species variability // Science 2000.- Vol. 287.- β. 5457. — P. 1363
- Robles A.I., Bemmels N.A., Foraker A.B.et al. APAF-1 Is a transcriptional target of p53 in DNA damage-induced apoptosis cancer res.-2001.- Vol.61.-β.18.-P. 6660−6664.
- Rockey D.D., Heizen R.A., Hackstadt T. Cloning and characterization of a Chlamydia psittaci gene encoding for a protein localized in the inclusion membrane of infected cells.//Mol Microbiol. 1995.- Vol. 15.-β.4.- P.617−626
- Rockey D.D., Scidmore M.A., Bannantine J.P., Brown W.J. Proteins in the chlamydial inclusion membrane // Microbes and Infection .-2002.-Vol.4.-β.3.- P. 333−340.
- Roy S., Nicholson D.W. Cross-talk in cell death signaling // J Exp Med.-2000.- Vol. 192.-β. 8.-P.21−26
- Rytkonen A, Holden D.W. Bacterial interference of ubiquitination and deubiquitination.//Cell Host Microbe. -2007.- Vol.l.-β.l- P. 13−22.
- Rytomaa M., Martins L.M., Downward J. Involvement of FADD and caspase-8 signalling in detachment-induced apoptosis //Current Biology.-1999.-Vol. 9.- β.18.-P.1043−1052
- Rzomp K. A., Moorhead A. R., Scidmore M. A. The GTPase Rab4 Interacts with Chlamydia trachomatis Inclusion Membrane Protein CT229 // Infect. Immun.- 2006.-Vol. 74.-β. 9.- P. 5362−5373.
- Salari SH, Ward ME. Polypeptide composition of Chlamydia trachomatis.//J.Gen Microbiol.-1981.- Vol.-123 .-β.2.-P. 197−207
- Sandu C, Morisawa G, Wegorzewska I. FADD self-association is required for stable interaction with an activated death receptor // Cell Death and Differentiation.- 2006.-Vol. 13.- P.2052−2061
- Saraste A, Pulkki K. Morphologic and biochemical hallmarks of apoptosis.//Cardiovasc Res.-2000.- Vol.45.-β.3.-P.528−537
- Saraste A. Morphologic criteria and detection of apoptosis.// Herz.-1999.- Vol.24.-β.3.-P.189−195
- Sattler M., Liang H., Nettesheim D. et al. Structure of Bcl-xL-Bak Peptide Complex: Recognition Between Regulators of Apoptosis // Science -1997.- Vol. 275.-β. 5302. -P. 983−986
- Savill J, Fadok V, Henson P, Haslett C. Phagocyte recognition of cells undergoing apoptosis // Immunol Today. 1993, — Vol. 14.-β.3.-P.131−136.
- Schmitz-Esser S., Linka N., Collingro A. et al. ATP/ADP translocases: a common feature of obligate intracellular amoebal symbionts related to Chlamydiae and Rickettsiae // J. Bacteriol.- 2004.- Vol. 186.- β. 3.- P. 683−691
- Schuler M, Green DR. Mechanisms of p53-dependent apoptosis.// Biochem Soc Trans. 2001 Nov-29(Pt 6):684−8.
- Scidmore M.A., Fischer E.R., Hackstadt T. Restricted fusion of Chlamydia trachomatis vesicles with endocytic compartments during the initial stages of infection // Infect. Immun.- 2003.- Vol. 71.- β. 2.- P. 973−984.
- Scidmore M.A., Fischer E.R., Hackstadt T. Sphingolipids and Glycoproteins Are Differentially Trafficked to the Chlamydia trachomatis Inclusion// J Cell Biol. 1996.-Vol. 134.-β.2,-P. 363−374.
- Scidmore M.A., Hackstadt T. Mammalian 14−3-3beta associates with the Chlamydia trachomatis inclusion membrane via its interaction with IncG// Mol Microbiol.- 2001.-Vol.39.-β.6.-P. 1638−1650.
- Seger R, Krebs EG. The MAPK signaling cascade. // FASEB J. -1995.-Vol.9.-β.9.-P.726−735
- Shankar S, Srivastava RK. Involvement of Bcl-2 family members, phosphatidylinositol 3-kinase/AKT and mitochondrial p53 in curcumin (diferulolylmethane)-induced apoptosis in prostate cancer // Int J Oncol.- 2007.- Vol.30.-β.4.-P.905−918.
- Sharma M., Rudel T. Apoptosis resistance in Chlamydia-infected cells: a fate worse than death?// FEMS Immunol Med Microbiol. 2009.- Vol.55.-β.2.-P.154−61
- Shen Y, White E. p53-dependent apoptosis pathways. //Adv Cancer Res. 2001−82:55−84.
- Sianna Castillo S.S., Teegarden D. Sphingosine-1-Phosphate Inhibition of Apoptosis Requires Mitogen-Activated Protein Kinase Phosphatase-1 in Mouse Fibroblast C3H10T ½ Cells //J. Nutr. -2003.- Vol.133.-P.3343−3349
- Singh R., Pervin S., Chaudhuri G. Caspase-8-mediated BID cleavage and release of mitochondrial cytochrome c during N-Hydroxy-L-arginine-induced apoptosis in MDA-MB-468 cells //J. Biol. Chem. -2002. -Vol. 277.-β.40.-P. 37 630−37 636
- Slepenkin A., Maza L.M., Peterson E.M. Interaction between components of the type III secretion system of Chlamydiaceae // J.Bacteriol.-2005.- Vol. 187.- β. 2.- P. 473−479
- Slepenkin A., Motin V., Maza L. et al. Temporal expression of type III secretion genes of Chlamydia pneumoniae// Infect.Immun. 2003.- Vol. 71, — β. 5.- P. 2555−2562
- Song G, Ouyang G, Bao S. The activation of Akt/PKB signaling pathway and cellsurvival.// J Cell Mol Med.- 2005.- Vol. 9.- β. 1.- P. 59−71
- Stenner-Liewen F., Liewen H., Zapata J. et al. CADD, a Chlamydia Protein That Interacts with Death Receptors //J. Biol. Chem.- 2002.- Vol. 277.-β.12.- P. 9633−9636
- Stephens R.S. Chlamydia: Intracellular biology, pathogenesis, and immunity // Washington: ASM Press 1999, 321 p.
- Su H., Watkins N.G., Zhang Y X et al. Chlamydia trachomatis-host cell interactions: role of the chlamydial major outer membrane protein as an adhesion // Infect Immun. -1990.-Vol.58.- β.4.-P. 1017−1025.
- Su H., Raymond L., Rockey D.D. et al. A recombinant Chlamydia trachomatis major outer membrane protein binds to heparan sulfate receptors on epithelial cells // Proc. Nat. Acad. Sci.-1996.-Vol. 93.-β.20.-P. 11 143−11 148
- Suchland R.J., Rockey D.D., Weeks R.K. et al. Development of secondary inclusions in cells infected by Chlamydia trachomatis // Infect. Immune.- 2005: — Vol. 73.-β. 7.-P.3954−3962.
- Suchland R.J., Rockey D.D., Bannantine J.P. et al. Isolates of Chlamydia trachomatis that occupy nonfusogenic inclusions lack IncA, a protein localized to the inclusion membrane. // Infect. Immun. 2000.- Vol.68.-β.l .-P.360−367.
- Takimoto R., El-Deiry S. Wild-type p53 transactivates the KILLER/DR5 gene through an intronic sequence-specific DNA-binding site // Oncogene- 2000.- Vol. l9.-β. M.P.I 735−1743
- Tan K.O., Tan K.M., Yu V.C.A novel BH3-like domain in BID is required for intramolecular interaction and autoinhibition of pro-apoptotic activity.// J Biol Chem. -1999.- Vol.274.-β.34.- P.23 687−23 690.
- Tang D., Kidd V.J. Cleavage of DFF-45/ICAD by multiple caspases is essential for its function during apoptosis // J Biol Chem. -1998.- Vol. 273.- β. 44.-P. 28 549−28 552.
- Tang G., Minemoto Y., Dibling B. et al. Inhibition of JNK activation through NF-kappaB target genes//Nature -2001.-Vol. 414.-P. 313−317.
- Tenzer A., Zingg D., Rocha S. et al. The phosphatidylinositide 3'-kinase/Akt survival pathway is a target for the anticancer and radiosensitizing agent PKC412, an inhibitor of protein kinase C. // Cancer Res. 2001.- Vol.61.-β.22.- P.8203−8210.
- Thorburn A. Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand (TRAIL) Pathway Signaling// Journal of Thoracic 0ncology.-2007.- Vol.2.-β.6.-P.461−465
- Touny L., Baneijee P. Akt-GSK-3 pathway as a target in genistein-induced inhibition of TRAMP prostate cancer progression toward a poorly differentiated phenotype // Carcinogenesis -2007,-Vol. 28, — β.8.- P.1710−1717
- Tse S., Mason D., Botelho R. Accumulation of Diacylglycerol in the Chlamydia Inclusion Vacuole Possible role in the inhibition ot host apoptosis //J. Biol. Chem.-2005.- Vol. 280.-β.26.-P. 25 210−25 215
- Tsujimoto Y, Shimizu S. Bcl-2 family: life-or-death switch // FEBS Lett. 2000.-Vol.466.-β.l.-P. 6−10
- Tsujimoto Y. Role of Bcl-2 family proteins in apoptosis: apoptosomes or mitochondria?//Genes Cells. 1998.- Vol.3.-β. 11.-P. 697−707
- Tsujimoto Y., Shimizu S. VDAC regulation by the Bcl-2 family of proteins// Cell Death Differ.-2000.-Vol.7.-β.12.- P. l 174−1181
- Vander Heiden M., Xian X., Gottlieb Y. et al. Bcl-xL promotes the open configuration of VDAC and metabolite passage through the outer mitochondrial membrane // J. Biol. Chem.- 2001. Vol.276.-β.22.-P. 19 414−19 419.
- Verbeke P., Welter-Stahl L., Ying S. et al. Recruitment of BAD by the Chlamydia trachomatis vacuole correlates with host-cell survival// PLoS Pathog. 2006.-Vol.2.-β.5.-0408−0417.
- Verma A., Maurelli A.T. 2003. Identification of two eukaryote-like serine/threonine kinases encoded by Chlamydia trachomatis serovar L2 and characterization of interacting partners of Pknl.// Infect Immun. -2003.- Vol.71.- β.10.-P. 5772−5784.
- Wahl C., Mailer S., Marre R. et al. Chlamydia pneumoniae induces the expression of inhibitor of apoptosis 2 (c-IAP2) in a human monocytic cell line by an NF-kappaB-dependent pathway // Int. J. Med. Microbiol 2003.- Vol. 293.-β.5.- P. 377−381
- Wan Q., Kuang E., Dong W. et al. Reticulon 3 mediates Bcl-2 accumulation in mitochondria in response to endoplasmic reticulum stress. // Apoptosis. 2007,-Vol. 12.-β.2.-P. 319−328
- Wang X. The expanding role of mitochondria in apoptosis// Genes Dev.- 2001.- β. 15.-P.2922—2933
- Wang CY, Mayo MW, Korneluk RG et al. NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAPl and c-IAP2 to suppress caspase-8 activation // Science 1998.-Vol. 281 .-β.5383.-P. 1680−1683
- Wang J., Chun H., Wong W. et al Caspase-10 is an initiator caspase in death receptor signaling//PNAS -2001.- Vol. 98.-β.24.- P.13 884−13 888
- Wang K., Yin X., Chao D.T. et al. BID: a novel BH3 domain-only death agonist // Genes Dev. 1996.- Vol. l0.-β.22.-P.2859−2869.'
- Wang P., Yu J., Zhang L. The nuclear function of p53 is required for PUMA-mediated apoptosis induced by DNA damage // PNAS 2007.- Vol. 104.-β.10.-P. 4054−4059
- Wang X, Zhang J, Kim HP et al. disrupts death-inducing signal complex formation in plasma membrane induced by hypoxia/reoxygenation // FASEB J.- 2004.- Vol. 18.-β. 15.-P. 1826−1833
- Wang Z, Cao N, Nantajit D et al. Mitogen-activated protein kinase phosphatase-1 represses c-Jun NH2-terminal kinase-mediated apoptosis via NF-kappaB regulation. // J Biol Chem. -2008, — Vol.283.-β.30.- P.21 011−21 023.
- Wehrl W, Brinkmann V, Jungblut PR. From the inside out-processing of the Chlamydial autotransporter PmpD and its role in bacterial adhesion and activation of human host cells.// Mol Microbiol. 2004.- Vol.51.-β.2.- P.319−334.
- Wiman K.G., Hainaut P. 25 Years of p53 research.-Springer, 2007.- 446 p.
- Woo H.N., Seo Y. W, Moon A.R. et al. Effects of the BH3-only protein human Noxa on mitochondrial dynamics. // FEBS Lett. 2009.
- Wright M. M ., McMaster C.R. Phospholipid synthesis, diacylglycerol compartmentation, and apoptosis.// Biol. Res. -2002.-Vol.35.-β.2.-P.223−229
- Wright M. M ., McMaster C.R. Phospholipid synthesis, diacylglycerol compartmentation, and apoptosis.// Biol. Res. -2002.-Vol.35.-β.2.-P.223−229
- Wu M.X. Roles of the stress-induced gene IEX-1 in regulation of cell death and oncogenesis // Apoptosis 2003.- Vol.8.-β.l.-P.l 1−18
- Wu M.X., Ao*Z., Prasad K.V. et al. IEX-1 L, an apoptosis inhibitor involved in NF-kappaB-mediated cell survival // Science 1998.-Vol.281.-β.5379.-P.998−1001
- Wullaert A, Heyninck K, Beyaert R. Mechanisms of crosstalk between TNF-induced NF-kappaB and JNK activation in hepatocytes.// Biochem Pharmacol. 2006, — Vol.72.-β.9.- P.1090−1101
- Wyrick P.B. Intracellular survival by Chlamydia // Cell Microbiol.- 2000.- Vol.2.-β.4.-P.275−282.
- Wyttenbach A., Tolkovsky A.M. The BH3-only protein Puma is both necessary and sufficient for neuronal apoptosis induced by DNA damage in sympathetic neurons.// J Neurochem. -2006.- Vol.96.- β.5.-P.1213−1226.
- Xiao Y., Zhong Y., Greene W. et al. Chlamydia trachomatis infection inhibits both Bax and Bak activation induced by staurosporine // Infect. Immun. 2004.- Vol. 72.-β. 9.-P.5470−5474
- Xiao Y., Zhong Y., Su H. et al. NF-kB activation is not required for Chlamydia trachomatis inhibition of host epithelial cell apoptosis// J. Immunol.- 2005, — Vol.-174.-β.3.-P. 1701−1708.
- Yamaguchi Y., Shirai Y., Matsubara T. et al. Phosphorylation and up-regulation of diacylglycerol kinase gamma via its interaction with protein kinase C gamma.// J Biol Chem. -2006.- Vol.28l.-β.42.-P.31 627−31 637
- Yang X., Fraser M., Moll U.M. et al. Akt-mediated cisplatin resistance in ovarian cancer: modulation of p53 action on caspase-dependent mitochondrial death pathway// Cancer Res. -2006, — Vol.66.-β.6.-P.3126−3136
- Yasuda M., Chinnadurai G. Functional identification of the apoptosis e. ector BH3 domain in cellular protein BNIP1// Oncogene 2000.- Vol.19.- β. 19.- P.2363−2367.
- Ying S., Pettengill M., Ojcius D. et al. Host-cell survival and death during Chlamydia infection // Current Immunology Reviews.- 2007.- Vol.3.- β.1.-P. 31−40
- Zambetti G. The p53 tumor suppressor pathway and cancer.- Science, 2005.- 246 p.
- Zermati Y., Garrido C., Amsellem S. et al. Caspase activation is required for terminal erythroid differentiation // J. Exp. Med.-2001. Vol. 193. -β. 2. -P. 247−254
- Zhao T., Zhang H., Guo H. Granzyme K Directly processes Bid to release cytochrome c and endonuclease G leading to mitochondria-dependent cell death // J. Biol. Chem.-2007.- Vol. 282.-β.16.- P. 12 104−12 111.
- Zhivotovsky B., Orrenius S. Caspase-2 function in response to DNA damage.// Biochem. Biophys. Res. Commun. -2005.-Vol. 331.-β.3.-P.859−867
- Zhong G., Fan P., Ji H., Dong F., Huang Y. 2001. Identification of a chlamydial protease-like activity factor responsible for the degradation of host transcription factors. // J Exp Med. 2001.- Vol.193.- β.8.- P.935−942.
- Zhong G., Fan T., Liu L. Chlamydia inhibits interferon gamma-inducible major histocompatibility complex class II expression by degradation of upstream stimulatory factor 1 // J Exp Med. 1999.-Vol.l89.-β.12.- P.1931−1938.
- Zhou H., Li X., Meinkoth J et al. Akt regulates cell survival and apoptosis at a postmitochondrial level// J. Cell Biol. -2000,-Vol. 151, — β.3.- P. 483−494
- Zhu L., Xiang R., Dong W. et al. Anti-apoptotic activity of Bcl-2 is enhanced by its interaction with RTN3 // Cell Biol Int. 2007.- Vol.31.- β.8, — P. 825−830.
- Zhuang S., Yan Y., Daubert R.A. et al. ERK promotes hydrogen peroxide-induced apoptosis through caspase-3 activation and inhibition of Akt in renal epithelial cells // Am J Physiol Renal Physiol. 2007. — Vol. 292.-β.l.- P.440−447
- Zilfou J.T., Spector M.S., Low S. Slugging it out: fine tuning the p53-PUMA // Death Connection Cell.-2005.- Vol.123.- β.4.-P. 545−548
- Zong W., Edelstein L., Chen C. et al. The prosurvival Bcl-2 homolog Bfl-l/Al is a direct transcriptional target of NF-kB that blocks TNFa-induced apoptosis// Genes Dev.-1999.- Vol. 13.-β.4.-P. 382−387.