Π ΠΎΠ»Ρ ΡΠ°ΠΏΠ΅ΡΠΎΠ½Π° Hsp70 Π² ΡΠ΅Π°ΠΊΡΠΈΠΈ ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ Ρ ΠΏΠΎΠ²ΡΡΠ΅Π½Π½ΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠ΅ΠΉ ΠΏΡΠΎΡΠΎΠΎΠ½ΠΊΠΎΠ³Π΅Π½Π° ΠΡΡ Π½Π° Π΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ²
![ΠΠΈΡΡΠ΅ΡΡΠ°ΡΠΈΡ: Π ΠΎΠ»Ρ ΡΠ°ΠΏΠ΅ΡΠΎΠ½Π° Hsp70 Π² ΡΠ΅Π°ΠΊΡΠΈΠΈ ΠΎΠΏΡΡ
ΠΎΠ»Π΅Π²ΡΡ
ΠΊΠ»Π΅ΡΠΎΠΊ Ρ ΠΏΠΎΠ²ΡΡΠ΅Π½Π½ΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠ΅ΠΉ ΠΏΡΠΎΡΠΎΠΎΠ½ΠΊΠΎΠ³Π΅Π½Π° ΠΡΡ Π½Π° Π΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ
ΠΎΠ»Π΅Π²ΡΡ
ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ²](https://niscu.ru/work/5266766/cover.png)
Π¦Π΅Π»ΡΡ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΠΎΠΉ ΡΠ΅ΡΠ°ΠΏΠΈΠΈ ΡΠ²Π»ΡΠ΅ΡΡΡ ΡΠ½ΠΈΡΡΠΎΠΆΠ΅Π½ΠΈΠ΅ ΡΠ°ΠΊΠΎΠ²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ Π±Π΅Π· ΡΡΠ΅ΡΠ±Π° Π΄Π»Ρ ΠΎΠΊΡΡΠΆΠ°ΡΡΠΈΡ Π½ΠΎΡΠΌΠ°Π»ΡΠ½ΡΡ ΡΠΊΠ°Π½Π΅ΠΉΠΏΠΎΡΡΠΎΠΌΡ Π±ΠΎΠ»ΡΡΠΈΠ½ΡΡΠ²ΠΎ Ρ ΠΈΠΌΠΈΠΎΡΠ΅ΡΠ°ΠΏΠ΅Π²ΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ² Π·Π°Π΄ΡΠΌΠ°Π½ΠΎ ΡΠ°ΠΊ, ΡΡΠΎΠ±Ρ ΠΎΡΡΠ°Π½ΠΎΠ²ΠΈΡΡ ΠΏΡΠΎΠ»ΠΈΡΠ΅ΡΠ°ΡΠΈΡ ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΈ Π·Π°ΠΏΡΡΡΠΈΡΡ ΠΏΡΠΎΡΠ΅ΡΡ ΠΏΡΠΎΠ³ΡΠ°ΠΌΠΌΠΈΡΡΠ΅ΠΌΠΎΠΉ ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΡΠΌΠ΅ΡΡΠΈ (Π°ΠΏΠΎΠΏΡΠΎΠ·). Π ΠΊΠ»Π΅ΡΠΊΠ°Ρ U-937 Ρ ΠΏΠΎΡΡΠΎΡΠ½Π½ΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠ΅ΠΉ ΠΡΡ Π°ΠΏΠΎΠΏΡΠΎΠ· ΠΏΡΠΎΡΠ΅ΠΊΠ°Π΅Ρ ΠΏΡΠ΅ΠΈΠΌΡΡΠ΅ΡΡΠ²Π΅Π½Π½ΠΎ ΠΏΠΎ ΠΏΡΡΠΌΠΎΠΌΡ ΠΏΡΡΠΈ ΠΎΡ ΠΊΠ°ΡΠΏΠ°Π·Ρ 8… 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΅
- 1. ΠΠΠΠΠΠΠΠ
- 2. ΠΠΠΠΠ ΠΠΠ’ΠΠ ΠΠ’Π£Π Π«. 8 2.1. ΠΠΏΠΎΠΏΡΠΎΠ·
- 2. 1. 1. ΠΡΠ½ΠΎΠ²Π½ΡΠ΅ ΠΌΠΎΡΡΠΎΠ»ΠΎΠ³ΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΡΠ΅ΡΡΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°
- 2. 1. 2. ΠΠΈΠΎΡ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΡ Π°ΠΏΠΎΠΏΡΠΎΡΠΈΡΠ΅ΡΠΊΠΎΠΉ Π³ΠΈΠ±Π΅Π»ΠΈ
- 2. 1. 3. ΠΠΊΡΠΈΠ²Π°ΡΠΈΡ ΠΈ ΡΠ΅Π³ΡΠ»ΡΡΠΈΡ ΠΊΠ°ΡΠΏΠ°Π·Π½ΠΎΠ³ΠΎ ΠΊΠ°ΡΠΊΠ°Π΄Π°. 17 2.2 Π£ΡΠ°ΡΡΠΈΠ΅ ΠΎΠ½ΠΊΠΎΠ±Π΅Π»ΠΊΠ° ΠΡΡ Π² ΡΠ΅Π³ΡΠ»ΡΡΠΈΠΈ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°
- 2. 3. ΠΠ°ΡΠΈΡΠ½ΡΠ΅ ΡΠΈΡΡΠ΅ΠΌΡ ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ
- 2. 4. ΠΠ΅Π»ΠΊΠΈ ΡΠ΅ΠΏΠ»ΠΎΠ²ΠΎΠ³ΠΎ ΡΠΎΠΊΠ°
- 2. 4. 1. ΠΠ΅Π»ΠΊΠΈ ΡΠ΅ΠΏΠ»ΠΎΠ²ΠΎΠ³ΠΎ ΡΠΎΠΊΠ° ΠΈ ΠΈΡ ΠΊΠ»Π°ΡΡΠΈΡΠΈΠΊΠ°ΡΠΈΡ
- 2. 4. 2. Π‘Π΅ΠΌΠ΅ΠΉΡΡΠ²ΠΎ Π±Π΅Π»ΠΊΠΎΠ² Hsp70 ΠΈ Π΅Π³ΠΎ ΡΡΠ½ΠΊΡΠΈΠΈ
- 2. 4. 3. Π ΠΎΠ»Ρ Hsp70 Π² ΠΏΡΠΎΡΠ΅ΡΡΠ΅ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°
- 3. ΠΠΠ’ΠΠ ΠΠΠΠ« Π ΠΠΠ’ΠΠΠ«
- 3. 1. ΠΠ»Π΅ΡΠΎΡΠ½ΡΠ΅ Π»ΠΈΠ½ΠΈΠΈ ΠΈ ΠΈΡ ΠΊΡΠ»ΡΡΠΈΠ²ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅
- 3. 2. Π’Π΅ΠΏΠ»ΠΎΠ²ΠΎΠ΅ Π²ΠΎΠ·Π΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ ΠΈ ΠΈΠ½Π΄ΡΠΊΡΠΈΡ ΡΠΈΠ½ΡΠ΅Π·Π° Hsp
- 3. 3. Π’ΡΠ°Π½ΡΡΠ΅ΠΊΡΠΈΡ ΠΊΠ»Π΅ΡΠΎΠΊ
- 3. 4. ΠΠ½Π°Π»ΠΈΠ· ΡΠ΄Π΅ΡΠ½ΠΎΠΉ Π»ΠΎΠΊΠ°Π»ΠΈΠ·Π°ΡΠΈΠΈ MycER ΠΏΠΎΡΠ»Π΅ ΠΈΠ½Π΄ΡΠΊΡΠΈΠΈ ΠΠΠ’
- 3. 5. ΠΠ½Π΄ΡΠΊΡΠΈΡ ΠΈ ΠΎΡΠ΅Π½ΠΊΠ° Π°ΠΏΠΎΠΏΡΠΎΠ·Π°
- 3. 6. ΠΠ½Π°Π»ΠΈΠ· ΠΊΠΈΠ½Π΅ΡΠΈΠΊΠΈ ΠΊΠ°ΡΠΏΠ°Π·Π½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ
- 3. 7. ΠΠ½ΡΠΈΡΠ΅Π»Π°
- 3. 8. ΠΠ½Π°Π»ΠΈΠ· ΡΡΠ°Π³ΠΌΠ΅Π½ΡΠ°ΡΠΈΠΈ ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΠΠΠ
- 3. 9. ΠΠ½Π°Π»ΠΈΠ· ΡΡΠ°Π½ΡΠ»ΠΎΠΊΠ°ΡΠΈΠΈ ΡΠΈΡΠΎΡ ΡΠΎΠΌΠ°
- 3. 10. ΠΠΎΠΈΠΌΠΌΡΠ½ΠΎΠΏΡΠ΅ΡΠΈΠΏΠΈΡΠ°ΡΠΈΡ ΠΈ Π»ΠΈΠ³Π°Π½Π΄-Π±Π»ΠΎΡΡΠΈΠ½Π³
- 3. 11. ΠΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΈ ΠΎΡΠΈΡΡΠΊΠ° Π±Π΅Π»ΠΊΠΎΠ² ΡΠ΅ΠΏΠ»ΠΎΠ²ΠΎΠ³ΠΎ ΡΠΎΠΊΠ° ΡΠ΅ΠΌΠ΅ΠΉΡΡΠ²Π° 70 ΠΊΠΠ°
- 3. 12. Π‘ΡΠ°ΡΠΈΡΡΠΈΡΠ΅ΡΠΊΠ°Ρ ΠΎΠ±ΡΠ°Π±ΠΎΡΠΊΠ°
- 4. Π ΠΠΠ£ΠΠ¬Π’ΠΠ’Π«. 57 4.1. Π’Π΅ΠΏΠ»ΠΎΠ²ΠΎΠΉ ΡΠΎΠΊ ΡΠ½ΠΈΠΆΠ°Π΅Ρ ΡΡΠ²ΡΡΠ²ΠΈΡΠ΅Π»ΡΠ½ΠΎΡΡΡ ΠΎΠΏΡΡ
ΠΎΠ»Π΅Π²ΡΡ
ΠΊΠ»Π΅ΡΠΎΠΊ Ρ Π²ΡΡΠΎΠΊΠΈΠΌ ΡΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΠ΅ΠΌ ΠΡΡ ΠΊ Π΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ
ΠΎΠ»Π΅Π²ΡΡ
ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ²
- 4. 2. Hsp70 ΠΏΠΎΠ²ΡΡΠ°Π΅Ρ ΡΡΡΠΎΠΉΡΠΈΠ²ΠΎΡΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ Ρ Π²ΡΡΠΎΠΊΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠ΅ΠΉ
- ΠΡΡ ΠΊ Π΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ
ΠΎΠ»Π΅Π²ΡΡ
ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ²
- 4. 3. ΠΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΠ΅ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΡ ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΡ ΠΡΡ-ΠΎΠΏΠΎΡΡΠ΅Π΄ΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°
- 4. 4. ΠΡΠΎΡΠ΅ΡΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°, ΠΈΠ½ΠΈΡΠΈΠΈΡΠΎΠ²Π°Π½Π½ΡΠΉ v-Myc, ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ΅ΡΠΊΠΈ ΠΏΠΎΠ΄Π°Π²Π»ΡΠ΅ΡΡΡ ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΡΠΎΠΌ ΠΊΠ°ΡΠΏΠ°Π·Ρ
- 4. 5. Hsp70 ΡΠ΅Π³ΡΠ»ΠΈΡΡΠ΅Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΡΡΡΠ΅ΠΊΡΠΎΡΠ½ΡΡ ΠΊΠ°ΡΠΏΠ°Π·, Π½ΠΎ Π½Π΅ Π²Π»ΠΈΡΠ΅Ρ Π½Π° Π²ΡΡΠ²ΠΎΠ±ΠΎΠΆΠ΄Π΅Π½ΠΈΠ΅ ΡΠΈΡΠΎΡ ΡΠΎΠΌΠ° Ρ ΠΈΠ· ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ
- 4. 6. Hsp70 ΡΠΈΠ·ΠΈΡΠ΅ΡΠΊΠΈ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΡΠ΅Ρ Ρ ΠΊΠ°ΡΠΏΠ°Π·ΠΎΠΉ 3 ΠΈ ΠΊΠ°ΡΠΏΠ°Π·ΠΎΠΉ
- 5. ΠΠΠ‘Π£ΠΠΠΠΠΠ
- 6. ΠΠ«ΠΠΠΠ«
Π ΠΎΠ»Ρ ΡΠ°ΠΏΠ΅ΡΠΎΠ½Π° Hsp70 Π² ΡΠ΅Π°ΠΊΡΠΈΠΈ ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ Ρ ΠΏΠΎΠ²ΡΡΠ΅Π½Π½ΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠ΅ΠΉ ΠΏΡΠΎΡΠΎΠΎΠ½ΠΊΠΎΠ³Π΅Π½Π° ΠΡΡ Π½Π° Π΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ² (ΡΠ΅ΡΠ΅ΡΠ°Ρ, ΠΊΡΡΡΠΎΠ²Π°Ρ, Π΄ΠΈΠΏΠ»ΠΎΠΌ, ΠΊΠΎΠ½ΡΡΠΎΠ»ΡΠ½Π°Ρ)
ΠΠ·ΡΡΠ΅Π½ΠΈΠ΅ ΠΏΡΠΎΡΠ΅ΡΡΠΎΠ² ΠΈΠ½ΠΈΡΠΈΠ°ΡΠΈΠΈ ΠΈ ΠΏΡΠΎΠ³ΡΠ΅ΡΡΠΈΠΈ Π·Π»ΠΎΠΊΠ°ΡΠ΅ΡΡΠ²Π΅Π½Π½ΡΡ Π½ΠΎΠ²ΠΎΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΠΉ ΡΠ²Π»ΡΠ΅ΡΡΡ ΠΎΠ΄Π½ΠΎΠΉ ΠΈΠ· Π²Π°ΠΆΠ½Π΅ΠΉΡΠΈΡ Π·Π°Π΄Π°Ρ ΡΠΎΠ²ΡΠ΅ΠΌΠ΅Π½Π½ΠΎΠΉ ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ Π±ΠΈΠΎΠ»ΠΎΠ³ΠΈΠΈ ΠΈ ΠΌΠ΅Π΄ΠΈΡΠΈΠ½Ρ. ΠΠ·Π²Π΅ΡΡΠ½ΠΎ, ΡΡΠΎ ΠΎΠ³ΡΠΎΠΌΠ½ΠΎΠ΅ ΡΠ°Π·Π½ΠΎΠΎΠ±ΡΠ°Π·ΠΈΠ΅ ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΎΠ±ΡΠ΅Π΄ΠΈΠ½ΡΠ΅Ρ ΠΈΡ ΠΏΠΎΠ²ΡΡΠ΅Π½Π½Π°Ρ ΡΠΏΠΎΡΠΎΠ±Π½ΠΎΡΡΡ ΠΊ ΠΏΡΠΎΠ»ΠΈΡΠ΅ΡΠ°ΡΠΈΠΈ. ΠΡΠ° ΡΠΏΠΎΡΠΎΠ±Π½ΠΎΡΡΡ ΠΎΠ±ΡΡΠ½ΠΎ ΡΠΊΠ»Π°Π΄ΡΠ²Π°Π΅ΡΡΡ ΠΈΠ· Π΄Π²ΡΡ ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½ΡΠΎΠ²: ΠΈΠ· ΡΠ²Π΅Π»ΠΈΡΠ΅Π½Π½ΠΎΠΉ ΡΠΏΠΎΡΠΎΠ±Π½ΠΎΡΡΠΈ ΠΊ ΡΠΎΡΡΡ Π² ΠΊΠΎΠ½ΠΊΡΠ΅ΡΠ½ΡΡ ΡΡΠ»ΠΎΠ²ΠΈΡΡ (ΡΠΌΠ΅Π½ΡΡΠ΅Π½Π½ΠΎΠΉ ΠΏΠΎΡΡΠ΅Π±Π½ΠΎΡΡΠΈ Π² ΡΠΎΡΡΠΎΠ²ΡΡ ΡΠ°ΠΊΡΠΎΡΠ°Ρ , ΡΠ½ΠΈΠΆΠ΅Π½Π½ΠΎΠΉ Π·Π°Π²ΠΈΡΠΈΠΌΠΎΡΡΠΈ ΠΎΡ ΠΏΡΠΈΠΊΡΠ΅ΠΏΠ»Π΅Π½ΠΈΡ ΠΈ Ρ. ΠΏ.) ΠΈ ΠΈΠ· ΡΠΏΠΎΡΠΎΠ±Π½ΠΎΡΡΠΈ ΡΠ°ΡΡΠΈ Π½Π΅ΠΎΠΏΡΠ΅Π΄Π΅Π»Π΅Π½Π½ΠΎ Π΄ΠΎΠ»Π³ΠΎΠ΅ Π²ΡΠ΅ΠΌΡ (ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠ΅ Π±Π΅ΡΡΠΌΠ΅ΡΡΠΈΠ΅, ΠΈΠΌΠΌΠΎΡΡΠ°Π»ΠΈΠ·Π°ΡΠΈΡ, ΡΠΏΠΎΡΠΎΠ±Π½ΠΎΡΡΡ ΠΊ Π±Π΅ΡΠΊΠΎΠ½Π΅ΡΠ½ΠΎ Π΄ΠΎΠ»Π³ΠΎΠΉ ΠΏΡΠΎΠ»ΠΈΡΠ΅ΡΠ°ΡΠΈΠΈ).
Π Π½Π°ΡΡΠΎΡΡΠ΅Π΅ Π²ΡΠ΅ΠΌΡ ΠΎΠ½ΠΊΠΎΠ»ΠΎΠ³ΠΈ ΠΏΡΠΈΠΌΠ΅Π½ΡΡΡ ΡΡΠΈ ΠΎΡΠ½ΠΎΠ²Π½ΡΡ , ΠΊΠ»Π°ΡΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΈΠ»ΠΈ ΡΡΠ°Π΄ΠΈΡΠΈΠΎΠ½Π½ΡΡ ΠΌΠ΅ΡΠΎΠ΄Π° Π»Π΅ΡΠ΅Π½ΠΈΡ ΠΎΠ½ΠΊΠΎΠ»ΠΎΠ³ΠΈΡΠ΅ΡΠΊΠΈΡ Π·Π°Π±ΠΎΠ»Π΅Π²Π°Π½ΠΈΠΉ: Ρ ΠΈΡΡΡΠ³ΠΈΡΠ΅ΡΠΊΠΈΠΉ, Π»ΡΡΠ΅Π²ΠΎΠΉ ΠΈ Π»Π΅ΠΊΠ°ΡΡΡΠ²Π΅Π½Π½ΡΠΉ (Ρ ΠΈΠΌΠΈΠΎΡΠ΅ΡΠ°ΠΏΠΈΡ, Π³ΠΎΡΠΌΠΎΠ½ΠΎΡΠ΅ΡΠ°ΠΏΠΈΡ). Π‘ΠΎΠ²ΡΠ΅ΠΌΠ΅Π½Π½Π°Ρ ΠΌΠ΅Π΄ΠΈΡΠΈΠ½Π°, ΠΈΡΠΏΠΎΠ»ΡΠ·ΡΡ ΠΏΠΎΡΠ»Π΅Π΄Π½ΠΈΠ΅ Π΄ΠΎΡΡΠΈΠΆΠ΅Π½ΠΈΡ Π½Π°ΡΠΊΠΈ, ΠΏΡΠΎΠ΄ΠΎΠ»ΠΆΠ°Π΅Ρ ΡΠ°Π·Π²ΠΈΠ²Π°ΡΡ Π½Π°ΠΈΠ±ΠΎΠ»Π΅Π΅ Π·Π½Π°ΡΠΈΠΌΡΠ΅ Π½Π°ΠΏΡΠ°Π²Π»Π΅Π½ΠΈΡ Π² Π»Π΅ΡΠ΅Π½ΠΈΠΈ: Π³ΠΈΠΏΠ΅ΡΡΠ΅ΡΠΌΠΈΡ, Π³ΠΈΠΏΠ΅ΡΠ³Π»ΠΈΠΊΠ΅ΠΌΠΈΡ, ΡΠΎΡΠΌΠΎΠΆΠ΅Π½ΠΈΠ΅ ΡΠΎΡΡΠ° ΠΎΠΏΡΡ ΠΎΠ»ΠΈ, ΠΎΠ±Π»Π΅Π³ΡΠ΅Π½ΠΈΠ΅ Π΄ΠΎΡΡΠ°Π²ΠΊΠΈ Π»Π΅ΠΊΠ°ΡΡΡΠ², Π²ΠΎΠ·Π΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ Π½Π° ΠΌΠ΅ΠΌΠ±ΡΠ°Π½Ρ ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ. Π‘ΡΡΠ΅ΡΡΠ²ΡΡΡ ΡΠ°ΠΊΠΆΠ΅ ΡΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΠ°Π»ΡΠ½ΡΠ΅ ΠΌΠ΅ΡΠΎΠ΄Ρ, ΠΊΠΎΡΠΎΡΡΠ΅ ΠΏΠΎΠΊΠ°Π·Π°Π»ΠΈ ΡΠ²ΠΎΡ Π΄ΠΎΡΡΠ°ΡΠΎΡΠ½ΡΡ ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΠΈ Π³ΠΎΡΠΎΠ²Ρ Π²ΡΠΉΡΠΈ ΠΈΠ· ΠΎΠ±Π»Π°ΡΡΠΈ Π½Π°ΡΡΠ½ΡΡ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠΉ Π² ΡΠΈΡΠΎΠΊΡΡ ΠΊΠ»ΠΈΠ½ΠΈΡΠ΅ΡΠΊΡΡ ΠΏΡΠ°ΠΊΡΠΈΠΊΡ: Π°ΡΡΠΎΠΏΠ΅ΡΠ΅ΡΠ°Π΄ΠΊΠ° ΠΊΡΠ°ΡΠ½ΠΎΠ³ΠΎ ΠΊΠΎΡΡΠ½ΠΎΠ³ΠΎ ΠΌΠΎΠ·Π³Π° Π² ΡΠΎΡΠ΅ΡΠ°Π½ΠΈΠΈ Ρ Π±ΠΎΠ»ΡΡΠΈΠΌΠΈ Π΄ΠΎΠ·Π°ΠΌΠΈ ΡΠΈΡΠΎΡΡΠ°ΡΠΈΠΊΠΎΠ², Π³Π΅Π½Π½Π°Ρ ΡΠ΅ΡΠ°ΠΏΠΈΡ, ΡΠ»Π΅ΠΊΡΡΠΎΡ ΠΈΠΌΠΈΠΎΡΠ΅ΡΠ°ΠΏΠΈΡ, ΡΠΎΠΊΡΡΠΈΡΠΎΠ²Π°Π½Π½ΡΠΉ ΡΠ»ΡΡΡΠ°Π·Π²ΡΠΊ Π²ΡΡΠΎΠΊΠΈΡ ΡΠ½Π΅ΡΠ³ΠΈΠΉ (Π²ΡΠΆΠΈΠ³Π°ΡΡΠ°Ρ ΡΠ΅ΡΠ°ΠΏΠΈΡ ΠΎΠΏΡΡ ΠΎΠ»Π΅ΠΉ), ΠΏΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΠ΅ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ Π²Π°ΠΊΡΠΈΠ½. Π Π°Π·ΡΠ°Π±Π°ΡΡΠ²Π°ΡΡΡΡ ΠΈ Π΄ΡΡΠ³ΠΈΠ΅ ΠΌΠ΅ΡΠΎΠ΄Ρ, ΠΊΠΎΡΠΎΡΡΠ΅ Π½Π°Ρ ΠΎΠ΄ΡΡΡΡ Π»ΠΈΠ±ΠΎ Π² Π½Π°ΡΠ°Π»ΡΠ½ΠΎΠΉ ΡΡΠ°Π΄ΠΈΠΈ ΠΈΠ·ΡΡΠ΅Π½ΠΈΡ, Π»ΠΈΠ±ΠΎ ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½Ρ Π»ΠΈΡΡ ΠΏΡΠΈ Π»Π΅ΡΠ΅Π½ΠΈΠΈ ΠΎΡΠ΄Π΅Π»ΡΠ½ΡΡ Π²ΠΈΠ΄ΠΎΠ² ΠΎΠΏΡΡ ΠΎΠ»Π΅ΠΉ.
Π¦Π΅Π»ΡΡ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΠΎΠΉ ΡΠ΅ΡΠ°ΠΏΠΈΠΈ ΡΠ²Π»ΡΠ΅ΡΡΡ ΡΠ½ΠΈΡΡΠΎΠΆΠ΅Π½ΠΈΠ΅ ΡΠ°ΠΊΠΎΠ²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ Π±Π΅Π· ΡΡΠ΅ΡΠ±Π° Π΄Π»Ρ ΠΎΠΊΡΡΠΆΠ°ΡΡΠΈΡ Π½ΠΎΡΠΌΠ°Π»ΡΠ½ΡΡ ΡΠΊΠ°Π½Π΅ΠΉΠΏΠΎΡΡΠΎΠΌΡ Π±ΠΎΠ»ΡΡΠΈΠ½ΡΡΠ²ΠΎ Ρ ΠΈΠΌΠΈΠΎΡΠ΅ΡΠ°ΠΏΠ΅Π²ΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ² Π·Π°Π΄ΡΠΌΠ°Π½ΠΎ ΡΠ°ΠΊ, ΡΡΠΎΠ±Ρ ΠΎΡΡΠ°Π½ΠΎΠ²ΠΈΡΡ ΠΏΡΠΎΠ»ΠΈΡΠ΅ΡΠ°ΡΠΈΡ ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΈ Π·Π°ΠΏΡΡΡΠΈΡΡ ΠΏΡΠΎΡΠ΅ΡΡ ΠΏΡΠΎΠ³ΡΠ°ΠΌΠΌΠΈΡΡΠ΅ΠΌΠΎΠΉ ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΡΠΌΠ΅ΡΡΠΈ (Π°ΠΏΠΎΠΏΡΠΎΠ·).
ΠΠ»Ρ ΠΌΠ½ΠΎΠ³ΠΈΡ ΡΠΏΠΎΠ½ΡΠ°Π½Π½ΡΡ ΠΎΠΏΡΡ ΠΎΠ»Π΅ΠΉ ΠΈΠΌΠ΅ΡΡΡΡ ΡΠ΅ΡΡΠ΅Π·Π½ΡΠ΅ Π΄ΠΎΠΊΠ°Π·Π°ΡΠ΅Π»ΡΡΡΠ²Π° Π²ΠΎΠ²Π»Π΅ΡΠ΅Π½Π½ΠΎΡΡΠΈ ΠΎΠΏΡΠ΅Π΄Π΅Π»Π΅Π½Π½ΡΡ ΠΊΠ»Π΅ΡΠΎΡΠ½ΡΡ Π³Π΅Π½ΠΎΠ², ΠΈ, ΠΏΡΠ΅ΠΆΠ΄Π΅ Π²ΡΠ΅Π³ΠΎ ΠΎΠ½ΠΊΠΎΠ³Π΅Π½ΠΎΠ², Π³Π΅Π½ΠΎΠ²-ΡΡΠΏΡΠ΅ΡΡΠΎΡΠΎΠ² ΠΈ Π³Π΅Π½ΠΎΠ²-ΡΠ΅Π³ΡΠ»ΡΡΠΎΡΠΎΠ² ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠ³ΠΎ ΡΠΈΠΊΠ»Π° Π² ΠΏΡΠΎΡΠ΅ΡΡ ΠΊΠ°Π½ΡΠ΅ΡΠΎΠ³Π΅Π½Π΅Π·Π°, Π½ΠΎ Π΄Π»Ρ ΠΏΠΎΠ΄Π°Π²Π»ΡΡΡΠ΅Π³ΠΎ Π±ΠΎΠ»ΡΡΠΈΠ½ΡΡΠ²Π° ΠΎΠΏΡΡ ΠΎΠ»Π΅ΠΉ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΠ΅ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΡ Π·Π°ΠΏΡΡΠΊΠ° «ΠΎΠ½ΠΊΠΎΠ³Π΅Π½Π½ΠΎΠΉ» ΠΏΡΠΎΠ³ΡΠ°ΠΌΠΌΡ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΎΡΡΠ°ΡΡΡΡ Π½Π΅ΠΈΠ·Π²Π΅ΡΡΠ½ΡΠΌΠΈ. ΠΠ½ΡΠ΅ΡΠ΅ΡΠ½ΠΎ, ΡΡΠΎ ΠΌΠ½ΠΎΠ³ΠΈΠ΅ ΠΏΡΠΎΡΠΎΠΎΠ½ΠΊΠΎΠ³Π΅Π½Ρ, Π² ΡΠ°ΡΡΠ½ΠΎΡΡΠΈ ΠΏΡΠΎΡΠΎΠΎΠ½ΠΊΠΎΠ³Π΅Π½Ρ ΡΠ΅ΠΌΠ΅ΠΉΡΡΠ²Π° ΠΡΡ, Π·Π°ΠΏΡΡΠΊΠ°ΡΡΠΈΠ΅ ΠΊΠ»Π΅ΡΠΎΡΠ½ΡΡ ΠΏΡΠΎΠ»ΠΈΡΠ΅ΡΠ°ΡΠΈΡ, ΠΎΠ΄Π½ΠΎΠ²ΡΠ΅ΠΌΠ΅Π½Π½ΠΎ ΠΏΡΠ΅Π΄ΡΠ°ΡΠΏΠΎΠ»Π°Π³Π°ΡΡ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΊ Π°ΠΏΠΎΠΏΡΠΎΠ·Ρ (Reed, 2003). ΠΠ΅Π½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΈΠ·ΠΌΠ΅Π½Π΅Π½ΠΈΡ ΠΏΡΠΎΡΠΎΠΎΠ½ΠΊΠΎΠ³Π΅Π½Π° ΠΡΡ, Π²Π΅Π΄ΡΡΠΈΠ΅ ΠΊ Π΅Π³ΠΎ Π½Π΅ΡΠ΅Π³ΡΠ»ΠΈΡΡΠ΅ΠΌΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠΈ, Ρ Π°ΡΠ°ΠΊΡΠ΅ΡΠ½Ρ Π΄Π»Ρ ΠΌΠ½ΠΎΠΆΠ΅ΡΡΠ²Π° ΠΎΠΏΡΡ ΠΎΠ»Π΅ΠΉ ΡΠ°Π·Π»ΠΈΡΠ½ΠΎΠ³ΠΎ ΠΏΡΠΎΠΈΡΡ ΠΎΠΆΠ΄Π΅Π½ΠΈΡ — Π»ΠΈΠΌΡΠΎΠΌΡ ΠΠ΅ΡΠΊΠΈΡΡΠ°, ΡΠ°ΠΊΠ° Π»Π΅Π³ΠΊΠΎΠ³ΠΎ ΠΈ ΡΠ°ΠΊΠ° ΠΌΠΎΠ»ΠΎΡΠ½ΠΎΠΉ ΠΆΠ΅Π»Π΅Π·Ρ (Amati et al., 2001). ΠΠ΅Π»ΠΊΠΈ ΡΠ΅ΠΌΠ΅ΠΉΡΡΠ²Π° ΠΡΡ ΡΠ²Π»ΡΡΡΡΡ ΡΡΠ°Π½ΡΠΊΡΠΈΠΏΡΠΈΠΎΠ½Π½ΡΠΌΠΈ ΡΠ°ΠΊΡΠΎΡΠ°ΠΌΠΈ, ΠΈ Π½Π΅ΠΈΠ·Π²Π΅ΡΡΠ½Π° Π½ΠΈ ΠΎΠ΄Π½Π° ΠΌΡΡΠ°ΡΠΈΡ ΠΎΠ½ΠΊΠΎΠ³Π΅Π½Π½ΡΡ ΠΏΡΠ΅Π΄ΡΡΠ°Π²ΠΈΡΠ΅Π»Π΅ΠΉ ΡΡΠΎΠ³ΠΎ ΡΠ΅ΠΌΠ΅ΠΉΡΡΠ²Π° (v-myc, c-myc, N-myc ΠΈ L-myc), ΠΊΠΎΡΠΎΡΠ°Ρ Π±Ρ ΠΈΠ½Π°ΠΊΡΠΈΠ²ΠΈΡΠΎΠ²Π°Π»Π° ΠΏΡΠΎΠ°ΠΏΠΎΠΏΡΠΎΡΠΈΡΠ΅ΡΠΊΡΡ ΡΡΠ½ΠΊΡΠΈΡ, Π½Π΅ Π·Π°ΡΡΠΎΠ½ΡΠ² ΠΈΡ ΡΠΏΠΎΡΠΎΠ±Π½ΠΎΡΡΡ ΡΡΠΈΠΌΡΠ»ΠΈΡΠΎΠ²Π°ΡΡ ΠΏΡΠΎΠ»ΠΈΡΠ΅ΡΠ°ΡΠΈΡ. ΠΡΠ»ΠΎ ΡΠ΄Π΅Π»Π°Π½ΠΎ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»ΠΎΠΆΠ΅Π½ΠΈΠ΅, ΡΡΠΎ ΠΡΡ Π²Π»ΠΈΡΠ΅Ρ Π½Π° Π²ΡΡΠ²ΠΎΠ±ΠΎΠΆΠ΄Π΅Π½ΠΈΠ΅ ΡΠΈΡΠΎΡ ΡΠΎΠΌΠ° Ρ ΠΈΠ· ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ, ΡΠ΅ΠΌ ΡΠ°ΠΌΡΠΌ, ΠΏΡΠ΅Π΄ΡΠ°ΡΠΏΠΎΠ»Π°Π³Π°Ρ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΊ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠΌΡ ΠΏΡΡΠΈ ΡΠ΅Π°Π»ΠΈΠ·Π°ΡΠΈΠΈ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° (Juin et al., 1999).
Π ΠΏΡΠΎΡΠ΅ΡΡΠ΅ ΠΊΠ°Π½ΡΠ΅ΡΠΎΠ³Π΅Π½Π΅Π·Π° ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΠ΅ ΠΊΠ»Π΅ΡΠΊΠΈ Π²ΡΡΠ°Π±Π°ΡΡΠ²Π°ΡΡ ΡΠΎΠ±ΡΡΠ²Π΅Π½Π½ΡΠ΅ Π·Π°ΡΠΈΡΠ½ΡΠ΅ ΡΠΈΡΡΠ΅ΠΌΡ, Π²ΡΠ»Π΅Π΄ΡΡΠ²ΠΈΠ΅ ΡΠ΅Π³ΠΎ ΠΎΠ½ΠΈ Π·Π½Π°ΡΠΈΡΠ΅Π»ΡΠ½ΠΎ ΠΎΡΠ»ΠΈΡΠ°ΡΡΡΡ ΠΎΡ Π½ΠΎΡΠΌΠ°Π»ΡΠ½ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠ°, Π² ΡΠΎΠΌ ΡΠΈΡΠ»Π΅ ΠΈ ΠΏΠΎ ΡΠΏΠΎΡΠΎΠ±Π½ΠΎΡΡΠΈ Π²ΡΡΡΠΏΠ°ΡΡ Π² Π°ΠΏΠΎΠΏΡΠΎΠ·. ΠΠ΄Π½Π° ΠΈΠ· Π·Π°ΡΠΈΡΠ½ΡΡ ΡΠΈΡΡΠ΅ΠΌ ΠΎΡΠ½ΠΎΠ²Π°Π½Π° Π½Π° ΡΠ°ΠΏΠ΅ΡΠΎΠ½Π΅ Hsp70. ΠΡΠΎΡ Π±Π΅Π»ΠΎΠΊ ΠΎΠ±Π»Π°Π΄Π°Π΅Ρ Π΄Π²ΡΠΌΡ ΠΎΡΠ΅Π½Ρ Π²Π°ΠΆΠ½ΡΠΌΠΈ ΡΠ²ΠΎΠΉΡΡΠ²Π°ΠΌΠΈ: ΡΠ°ΠΏΠ΅ΡΠΎΠ½Π½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡΡ ΠΈ ΡΠΏΠΎΡΠΎΠ±Π½ΠΎΡΡΡΡ Π·Π°ΡΠΈΡΠ°ΡΡ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΎΡ ΡΠ°Π·Π½ΠΎΠΎΠ±ΡΠ°Π·Π½ΡΡ Π½Π΅Π±Π»Π°Π³ΠΎΠΏΡΠΈΡΡΠ½ΡΡ ΡΠ°ΠΊΡΠΎΡΠΎΠ². Π¨Π°ΠΏΠ΅ΡΠΎΠ½Π½Π°Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ — ΡΡΠΎ ΡΠΏΠΎΡΠΎΠ±Π½ΠΎΡΡΡ Π±Π΅Π»ΠΊΠ° ΡΠ²ΡΠ·ΡΠ²Π°ΡΡΡΡ Ρ ΠΏΠΎΠ²ΡΠ΅ΠΆΠ΄Π΅Π½Π½ΡΠΌΠΈ ΠΈΠ»ΠΈ Π²Π½ΠΎΠ²Ρ ΡΠΈΠ½ΡΠ΅Π·ΠΈΡΠΎΠ²Π°Π½Π½ΡΠΌΠΈ ΠΏΠΎΠ»ΠΈΠΏΠ΅ΠΏΡΠΈΠ΄Π°ΠΌΠΈ, ΡΡΠ°Π½ΡΠΏΠΎΡΡΠΈΡΠΎΠ²Π°ΡΡ ΠΈΡ ΡΠ΅ΡΠ΅Π· ΡΠ΅ΡΡ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΡΡ ΠΌΠ΅ΠΌΠ±ΡΠ°Π½ ΠΈ ΡΠΊΡΠΏΠΎΠ½ΠΈΡΠΎΠ²Π°ΡΡ ΠΈΡ Π±Π΅Π»ΠΎΠΊ-ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΡΡΡΠΈΠΌ ΡΠΈΡΡΠ΅ΠΌΠ°ΠΌ (Morimoto et al., 1997). ΠΠ°Π½Π½ΡΠ΅ ΠΎΠ³ΡΠΎΠΌΠ½ΠΎΠ³ΠΎ ΡΠΈΡΠ»Π° ΡΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΠΎΠ² in vitro ΠΈ in vivo ΡΠ±Π΅Π΄ΠΈΡΠ΅Π»ΡΠ½ΠΎ ΡΠ²ΠΈΠ΄Π΅ΡΠ΅Π»ΡΡΡΠ²ΡΡΡ ΠΎ ΡΠΎΠΌ, ΡΡΠΎ Hsp70 ΠΏΡΠ΅Π΄ΡΡΠ°Π²Π»ΡΠ΅Ρ ΡΠΎΠ±ΠΎΠΉ Π½Π°ΠΈΠ±ΠΎΠ»Π΅Π΅ ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΡΡ ΠΈ ΠΊΠΎΠ½ΡΠ΅ΡΠ²Π°ΡΠΈΠ²Π½ΡΡ Π·Π°ΡΠΈΡΠ½ΡΡ ΡΠΈΡΡΠ΅ΠΌΡ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΈ ΡΠ΅Π»ΠΎΠ³ΠΎ ΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠ° (Jaattela, 1999; ΠΠ°ΡΠ³ΡΠ»ΠΈΡ, ΠΡΠΆΠΎΠ²Π°, 2009).
ΠΡΡΠΎΠΊΠΈΠΉ ΡΡΠΎΠ²Π΅Π½Ρ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠΈ Hsp70, ΠΎΠ±Π½Π°ΡΡΠΆΠ΅Π½Π½ΡΠΉ Π² ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΊΠ°Ρ , ΠΏΠΎ-Π²ΠΈΠ΄ΠΈΠΌΠΎΠΌΡ, ΡΠ²Π»ΡΠ΅ΡΡΡ ΠΏΡΠ΅ΠΏΡΡΡΡΠ²ΠΈΠ΅ΠΌ Π΄Π»Ρ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΠΎΠΉ ΡΠ΅ΡΠ°ΠΏΠΈΠΈ, ΠΈ ΡΠ²ΠΈΠ΄Π΅ΡΠ΅Π»ΡΡΡΠ²ΡΠ΅Ρ ΠΎ Π½Π΅Π±Π»Π°Π³ΠΎΠΏΡΠΈΡΡΠ½ΠΎΠΌ ΠΏΡΠΎΠ³Π½ΠΎΠ·Π΅ Π΄Π»Ρ Π±ΠΎΠ»ΡΠ½ΠΎΠ³ΠΎ ΠΏΡΠΈ Π½Π΅ΠΊΠΎΡΠΎΡΡΡ Π²ΠΈΠ΄Π°Ρ Π½ΠΎΠ²ΠΎΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΠΉ (Ciocca et al., 1993; Ricaniadis et al., 2001). Π Π°Π½Π΅Π΅ Π±ΡΠ»ΠΎ ΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΎ, ΡΡΠΎ Hsp70 ΡΠΏΠ°ΡΠ°Π΅Ρ ΡΠ°ΠΊΠΎΠ²ΡΠ΅ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΎΡ Π΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΌΠ½ΠΎΠ³ΠΈΡ ΡΠ°ΠΊΡΠΎΡΠΎΠ², Π²ΡΠ·ΡΠ²Π°ΡΡΠΈΡ Π°ΠΏΠΎΠΏΡΠΎΠ·, Π²ΠΊΠ»ΡΡΠ°Ρ ΡΠ°ΠΊΠΈΠ΅, ΠΊΠ°ΠΊ TNF-a, ΡΡΠ°ΡΡΠΎΡΠΏΠΎΡΠΈΠ½, ΠΆΠ΅ΡΡΠΊΠΈΠΉ ΡΠ΅ΠΏΠ»ΠΎΠ²ΠΎΠΉ ΡΡΡΠ΅ΡΡ ΠΈ ΠΌΠ½ΠΎΠ³ΠΈΠ΅ Π΄ΡΡΠ³ΠΈΠ΅. (Samali, Orrenius, 1998; ΠΡΠΆΠΎΠ²Π° ΠΈ Π΄Ρ., 2000). ΠΠΎΠ»Π΅Π΅ ΡΠΎΠ³ΠΎ, Hsp70 ΠΌΠΎΠΆΠ΅Ρ ΡΠΎΡΠΌΠΎΠ·ΠΈΡΡ ΠΏΡΠΎΡΠ΅ΡΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Π½Π° ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ Π΅Π³ΠΎ ΡΠ°Π·Π°Ρ . ΠΠ°ΠΈΠ±ΠΎΠ»Π΅Π΅ ΡΠ±Π΅Π΄ΠΈΡΠ΅Π»ΡΠ½ΠΎΠ΅ Π΄ΠΎΠΊΠ°Π·Π°ΡΠ΅Π»ΡΡΡΠ²ΠΎ ΠΏΡΠΎΡΠΈΠ²ΠΎΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠ³ΠΎ Π΄Π΅ΠΉΡΡΠ²ΠΈΡ Hsp70 Π±ΡΠ»ΠΎ ΠΏΡΠ΅Π΄ΡΡΠ°Π²Π»Π΅Π½ΠΎ Π² ΡΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΠ°Ρ Π½Π° ΠΊΠ°ΡΡΠΈΠ½ΠΎΠΌΠ΅ ΠΌΠΎΠ»ΠΎΡΠ½ΠΎΠΉ ΠΆΠ΅Π»Π΅Π·Ρ ΠΠ‘Π-7, Π² ΠΊΠΎΡΠΎΡΡΡ Π² ΠΊΠ»Π΅ΡΠΊΠΈ Π²Π²ΠΎΠ΄ΠΈΠ»ΠΈ Π°Π½ΡΠΈ-ΡΠΌΡΡΠ»ΠΎΠ²ΡΡ mRNA ΠΊ Hsp70, Π² ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΠ΅ ΡΠ΅Π³ΠΎ ΠΎΠ½ΠΈ ΠΏΠΎΠ³ΠΈΠ±Π°Π»ΠΈ ΠΏΡΡΠ΅ΠΌ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° (Nylandsted et al., 2000). ΠΠ΅ΡΠΌΠΎΡΡΡ Π½Π° ΠΈΠ½ΡΠ΅Π½ΡΠΈΠ²Π½ΡΠ΅ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ, ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌ Π·Π°ΡΠΈΡΠ½ΠΎΠΉ ΡΡΠ½ΠΊΡΠΈΠΈ Hsp70 ΠΎΡΡΠ°Π΅ΡΡΡ Π½Π΅ΡΡΠ½ΡΠΌ. ΠΠ΄Π½Π°ΠΊΠΎ Π±ΠΎΠ»ΡΡΠΈΠ½ΡΡΠ²ΠΎ Π΄Π°Π½Π½ΡΡ ΡΠ²ΠΈΠ΄Π΅ΡΠ΅Π»ΡΡΡΠ²ΡΠ΅Ρ ΠΎ ΠΏΡΠ΅Π²Π°Π»ΠΈΡΡΡΡΠ΅ΠΉ ΡΠΎΠ»ΠΈ Hsp70 Π² ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΠ²Π°Π½ΠΈΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΠΎΠ³ΠΎ ΠΏΡΡΠΈ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° (Beere, Green, 2001). ΠΡΡ ΠΎΠ΄Ρ ΠΈΠ· Π²ΡΡΠ΅ΠΈΠ·Π»ΠΎΠΆΠ΅Π½Π½ΡΡ ΡΠ°ΠΊΡΠΎΠ², ΠΌΠΎΠΆΠ½ΠΎ ΠΏΡΠ΅Π΄ΠΏΠΎΠ»ΠΎΠΆΠΈΡΡ, ΡΡΠΎ Hsp70 ΡΠ°ΠΊΠΆΠ΅ ΡΠΏΠΎΡΠΎΠ±Π΅Π½ ΠΊ ΠΊΠΎΠΎΠΏΠ΅ΡΠ°ΡΠΈΠΈ Ρ ΠΡΡ Π² ΠΏΡΠΎΡΠ΅ΡΡΠ΅ ΠΊΠ°Π½ΡΠ΅ΡΠΎΠ³Π΅Π½Π΅Π·Π°.
Π¦Π΅Π»ΠΈ ΠΈ Π·Π°Π΄Π°ΡΠΈ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ.
Π¦Π΅Π»ΡΡ Π½Π°ΡΡΠΎΡΡΠ΅ΠΉ ΡΠ°Π±ΠΎΡΡ ΡΠ²Π»ΡΠ΅ΡΡΡ ΠΈΠ·ΡΡΠ΅Π½ΠΈΠ΅ ΡΡΠ½ΠΊΡΠΈΠΈ ΡΠ°ΠΏΠ΅ΡΠΎΠ½Π° Hsp70 Π½Π° ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΌ ΠΈ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΠΎΠΌ ΡΡΠΎΠ²Π½ΡΡ Π² ΠΏΡΠΎΡΠ΅ΡΡΠ΅ Π°ΠΏΠΎΠΏΡΠΎΠ·Π°, ΡΡΠΈΠΌΡΠ»ΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠΌ Π΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ΠΌ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ², Π² ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΊΠ°Ρ Ρ Π½ΠΎΡΠΌΠ°Π»ΡΠ½ΠΎΠΉ ΠΈ ΠΏΠΎΠ²ΡΡΠ΅Π½Π½ΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠ΅ΠΉ ΠΏΡΠΎΡΠΎΠΎΠ½ΠΊΠΎΠ³Π΅Π½Π° ΠΡΡ.
Π ΡΠ°Π±ΠΎΡΠ΅ Π±ΡΠ»ΠΈ ΡΡΠΎΡΠΌΡΠ»ΠΈΡΠΎΠ²Π°Π½Ρ ΡΠ»Π΅Π΄ΡΡΡΠΈΠ΅ ΡΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΠ°Π»ΡΠ½ΡΠ΅ Π·Π°Π΄Π°ΡΠΈ:
1. ΠΡΡΡΠ½ΠΈΡΡ, ΠΌΠΎΠΆΠ΅Ρ Π»ΠΈ ΠΏΠΎΠ²ΡΡΠ΅Π½Π½Π°Ρ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΡ Hsp70 ΠΏΠΎΠ΄Π°Π²Π»ΡΡΡ Π΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ², Π½Π°ΠΏΡΠ°Π²Π»Π΅Π½Π½ΠΎΠ΅ Π½Π° ΠΈΠ½Π΄ΡΠΊΡΠΈΡ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Π² ΠΏΠΎΠΏΡΠ»ΡΡΠΈΠΈ ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ.
2. Π‘ΡΠ°Π²Π½ΠΈΡΡ ΠΎΠ±ΡΡΠ»ΠΎΠ²Π»Π΅Π½Π½ΡΡ Hsp70 ΡΡΡΠΎΠΉΡΠΈΠ²ΠΎΡΡΡ ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ Ρ Π½ΠΎΡΠΌΠ°Π»ΡΠ½ΠΎΠΉ ΠΈ ΠΏΠΎΠ²ΡΡΠ΅Π½Π½ΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠ΅ΠΉ ΠΡΡ ΠΊ Π΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΠ².
3. ΠΡΠΏΠΎΠ»ΡΠ·ΡΡ ΠΌΠΎΠ΄Π΅Π»Ρ Π½Π° ΠΎΡΠ½ΠΎΠ²Π΅ ΠΊΠ»Π΅ΡΠΎΠΊ U937, Π²ΡΡΡΠ½ΠΈΡΡ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌ ΠΏΠΎΠ΄Π°Π²Π»Π΅Π½ΠΈΡ Hsp70 Π°ΠΏΠΎΠΏΡΠΎΠ·Π°, ΡΠΏΡΠ°Π²Π»ΡΠ΅ΠΌΠΎΠ³ΠΎ v-Myc.
4. ΠΡΡΡΠ½ΠΈΡΡ, ΡΠΏΠΎΡΠΎΠ±Π΅Π½ Π»ΠΈ Hsp70 ΠΈΠ·ΠΌΠ΅Π½ΡΡΡ ΠΊΠΈΠ½Π΅ΡΠΈΠΊΡ Π°ΠΊΡΠΈΠ²Π°ΡΠΈΠΈ ΡΡΡΠ΅ΠΊΡΠΎΡΠ½ΡΡ ΠΊΠ°ΡΠΏΠ°Π· Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ ΠΌΠΈΠ΅Π»ΠΎΠΈΠ΄Π½ΠΎΠΉ Π»Π΅ΠΉΠΊΠ΅ΠΌΠΈΠΈ ΡΠ΅Π»ΠΎΠ²Π΅ΠΊΠ°.
5. ΠΡΠΎΠ²Π΅ΡΠΈΡΡ Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎΡΡΡ Π²Π·Π°ΠΈΠΌΠΎΠ΄Π΅ΠΉΡΡΠ²ΠΈΡ Hsp70 Ρ ΡΡΡΠ΅ΠΊΡΠΎΡΠ½ΡΠΌΠΈ ΠΊΠ°ΡΠΏΠ°Π·Π°ΠΌΠΈ Π² Ρ ΠΎΠ΄Π΅ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° ΠΊΠ»Π΅ΡΠΎΠΊ ΠΌΠΈΠ΅Π»ΠΎΠΈΠ΄Π½ΠΎΠΉ Π»Π΅ΠΉΠΊΠ΅ΠΌΠΈΠΈ ΡΠ΅Π»ΠΎΠ²Π΅ΠΊΠ°, ΠΈΠ½Π΄ΡΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΠΌΠΈ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠ°ΠΌΠΈ.
2. ΠΠΠΠΠ ΠΠΠ’ΠΠ ΠΠ’Π£Π Π«.
2.1. ΠΠΏΠΎΠΏΡΠΎΠ·.
6. Π²ΡΠ²ΠΎΠ΄Ρ.
1. Hsp70 ΠΎΠ±Π»Π°Π΄Π°Π΅Ρ ΡΠΈΠ»ΡΠ½ΡΠΌ ΠΏΡΠΎΡΠΈΠ²ΠΎΠ°ΠΏΠΎΠΏΡΠΎΡΠΈΡΠ΅ΡΠΊΠΈΠΌ ΡΡΡΠ΅ΠΊΡΠΎΠΌ ΠΏΡΠΈ Π΄Π΅ΠΉΡΡΠ²ΠΈΠΈ Π½Π° ΡΠ°ΠΊΠΎΠ²ΡΠ΅ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΠΌΠΈ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠ°ΠΌΠΈ — Π°Π΄ΡΠΈΠ°ΠΌΠΈΡΠΈΠ½ΠΎΠΌ, ΡΡΠΎΠΏΠΎΠ·ΠΈΠ΄ΠΎΠΌ ΠΈ ΠΊΠ°ΠΌΠΏΡΠΎΡΠ΅ΡΠΈΠ½ΠΎΠΌ.
2. ΠΠ°ΡΠΈΡΠ½ΡΠΉ ΡΡΡΠ΅ΠΊΡ Hsp70 Π½Π°ΠΈΠ±ΠΎΠ»Π΅Π΅ Π²ΡΡΠ°ΠΆΠ΅Π½ Π² ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΊΠ°Ρ Ρ ΠΏΠΎΠ²ΡΡΠ΅Π½Π½ΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠΈ ΠΏΡΠΎΡΠΎΠΎΠ½ΠΊΠΎΠ³Π΅Π½Π° ΠΡΡ. Π ΠΊΠ»Π΅ΡΠΊΠ°Ρ ΠΊΡΡΡΠΈΠ½ΡΡ ΡΠΈΠ±ΡΠΎΠ±Π»Π°ΡΡΠΎΠ² RatlMycERHsp70, Π² ΠΊΠΎΡΠΎΡΡΡ ΠΌΠΎΠΆΠ½ΠΎ Π΄ΡΠΎΠ±Π½ΠΎ ΠΏΠΎΠ²ΡΡΠ°ΡΡ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΡ Hsp70, Π·Π°ΡΠΈΡΠ½ΡΠΉ ΡΡΡΠ΅ΠΊΡ ΡΠ°ΠΏΠ΅ΡΠΎΠ½Π° Π½ΠΎΡΠΈΡ Π΄ΠΎΠ·Π°Π·Π°Π²ΠΈΡΠΈΠΌΡΠΉ Ρ Π°ΡΠ°ΠΊΡΠ΅Ρ.
3. Π ΠΊΠ»Π΅ΡΠΊΠ°Ρ U-937 Ρ ΠΏΠΎΡΡΠΎΡΠ½Π½ΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠ΅ΠΉ ΠΡΡ Π°ΠΏΠΎΠΏΡΠΎΠ· ΠΏΡΠΎΡΠ΅ΠΊΠ°Π΅Ρ ΠΏΡΠ΅ΠΈΠΌΡΡΠ΅ΡΡΠ²Π΅Π½Π½ΠΎ ΠΏΠΎ ΠΏΡΡΠΌΠΎΠΌΡ ΠΏΡΡΠΈ ΠΎΡ ΠΊΠ°ΡΠΏΠ°Π·Ρ 8 ΠΊ ΡΡΡΠ΅ΠΊΡΠΎΡΠ½ΡΠΌ ΠΊΠ°ΡΠΏΠ°Π·Π°ΠΌ, Π² ΡΠΎ Π²ΡΠ΅ΠΌΡ ΠΊΠ°ΠΊ Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ Ρ ΠΏΠΎΠ²ΡΡΠ΅Π½Π½ΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠ΅ΠΉ ΠΡΡ ΠΎΡΠ½ΠΎΠ²Π½ΡΠΌ ΠΏΡΡΠ΅ΠΌ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° ΡΠ²Π»ΡΠ΅ΡΡΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠ°Π»ΡΠ½ΡΠΉ Ρ Π²ΠΎΠ²Π»Π΅ΡΠ΅Π½ΠΈΠ΅ΠΌ Π°ΠΊΡΠΈΠ²Π°ΡΠΈΠΈ ΠΊΠ°ΡΠΏΠ°Π·Ρ 9.
4.ΠΠ½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠ΅ Π΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ Hsp70 Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ U-937 ΠΊΠ°ΠΊ Ρ ΠΏΠΎΠ²ΡΡΠ΅Π½Π½ΠΎΠΉ, ΡΠ°ΠΊ ΠΈ Ρ ΠΏΠΎΡΡΠΎΡΠ½Π½ΠΎΠΉ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠ΅ΠΉ ΠΏΡΠΎΡΠΎΠΎΠ½ΠΊΠΎΠ³Π΅Π½Π° ΠΡΡ ΠΎΡΡΡΠ΅ΡΡΠ²Π»ΡΠ΅ΡΡΡ ΠΏΠΎΡΠ»Π΅ Π²ΡΠ±ΡΠΎΡΠ° ΡΠΈΡΠΎΡ ΡΠΎΠΌΠ° Ρ ΠΈΠ· ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ.
5. ΠΠ°ΡΠΏΠ°Π·Π° 3 ΠΈ ΠΊΠ°ΡΠΏΠ°Π·Π° 7 — Π½ΠΎΠ²ΡΠ΅ ΠΌΠΈΡΠ΅Π½ΠΈ Π΄Π»Ρ ΠΎΡΡΡΠ΅ΡΡΠ²Π»Π΅Π½ΠΈΡ Π°Π½ΡΠΈΠ°ΠΏΠΎΠΏΡΠΎΠ·Π½ΠΎΠΉ ΡΡΠ½ΠΊΡΠΈΠΈ Hsp70.
Π‘ΠΏΠΈΡΠΎΠΊ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- ΠΡΠΆΠΎΠ²Π° Π.Π., ΠΠ°ΡΡΠ½ΡΠΊΠ°Ρ Π. Π., ΠΠΈΠ»ΡΡΡΠΎΠ½ Π., ΠΠ°ΡΠΈΠ΅Π²Π° Π. Π., ΠΠ°ΡΠ³ΡΠ»ΠΈΡ Π. Π. 2000. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΡΠ΅ΠΏΠ»ΠΎΠ²ΠΎΠ³ΠΎ ΡΠΎΠΊΠ° Π½Π° ΠΏΡΠΎΡΠ΅ΡΡΡ Π΄ΠΈΡΡΠ΅ΡΠ΅Π½ΡΠΈΡΠΎΠ²ΠΊΠΈ ΠΈ Π°ΠΏΠΎΠΏΡΠΎΠ·Π° Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ U-937. Π¦ΠΈΡΠΎΠ»ΠΎΠ³ΠΈΡ. 42(7): 653−658.
- ΠΡΠΆΠΎΠ²Π° Π.Π., ΠΠ°ΡΠ³ΡΠ»ΠΈΡ Π. Π. 2000. ΠΠ½Π΄ΡΠΊΡΠΈΡ ΠΈ Π½Π°ΠΊΠΎΠΏΠ»Π΅Π½ΠΈΠ΅ ΠΠ’1Π70 ΠΏΡΠΈΠ²ΠΎΠ΄ΡΡ ΠΊ ΡΠΎΡΠΌΠΈΡΠΎΠ²Π°Π½ΠΈΡ Π΅Π³ΠΎ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² Ρ Π΄ΡΡΠ³ΠΈΠΌΠΈ ΠΊΠ»Π΅ΡΠΎΡΠ½ΡΠΌΠΈ Π±Π΅Π»ΠΊΠ°ΠΌΠΈ. Π¦ΠΈΡΠΎΠ»ΠΎΠ³ΠΈΡ. 42(7): 647 652.
- ΠΠ°ΡΠ³ΡΠ»ΠΈΡ Π.Π., ΠΡΠΆΠΎΠ²Π° Π. Π. 2000. ΠΠ΅Π»ΠΊΠΈ ΡΡΡΠ΅ΡΡΠ° Π² ΡΡΠΊΠ°ΡΠΈΠΎΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΊΠ»Π΅ΡΠΊΠ΅. Π¦ΠΈΡΠΎΠ»ΠΎΠ³ΠΈΡ. 42(4): 323−342.
- ΠΠ°ΡΠ³ΡΠ»ΠΈΡ Π.Π., ΠΡΠΆΠΎΠ²Π° Π. Π. 2009. ΠΠ²ΠΎΠΉΠ½Π°Ρ ΡΠΎΠ»Ρ ΡΠ°ΠΏΠ΅ΡΠΎΠ½ΠΎΠ² Π² ΠΎΡΠ²Π΅ΡΠ΅ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΈ Π²ΡΠ΅Π³ΠΎ ΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠ° Π½Π° ΡΡΡΠ΅ΡΡ. Π¦ΠΈΡΠΎΠ»ΠΎΠ³ΠΈΡ. 51(3): 219−228.
- ΠΠΎΠ²ΠΎΡΠ΅Π»ΠΎΠ² Π‘.Π‘., ΠΠ΅ΡΠ±ΠΎΠ²Π° Π. Π., ΠΠ°ΡΠΈΠ»ΡΠ΅Π²Π° Π. Π., ΠΠΎΡΠΎΠ±ΡΠ΅Π²Π° Π. Π., ΠΠ°ΡΠ³ΡΠ»ΠΈΡ Π. Π., ΠΡΠΆΠΎΠ²Π° Π. Π. 2004. ΠΠ½Π°Π»ΠΈΠ· ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠΈ Π±Π΅Π»ΠΊΠΎΠ²-ΡΠ°ΠΏΠ΅ΡΠΎΠ½ΠΎΠ² Hsp70 ΠΈ Hdjl Π² ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΡ ΠΊΠ»Π΅ΡΠΊΠ°Ρ ΡΠ΅Π»ΠΎΠ²Π΅ΠΊΠ°. ΠΠΎΠΏΡΠΎΡΡ ΠΎΠ½ΠΊΠΎΠ»ΠΎΠ³ΠΈΠΈ. 50: 174−178.
- ΠΠ΅Π²ΡΡΠΊΠΈΠΉ Π.Π. 1996. ΠΡΠΎΠ³ΡΠ°ΠΌΠΌΠΈΡΠΎΠ²Π°Π½Π½Π°Ρ Π³ΠΈΠ±Π΅Π»Ρ ΠΊΠ»Π΅ΡΠΎΠΊ ΠΈ Π°ΠΏΠΎΠΏΡΠΎΠ·: Π·Π½Π°ΡΠ΅Π½ΠΈΠ΅ Π΄Π»Ρ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΠΈ ΡΡΠ½ΠΊΡΠΈΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΠΈΠΌΠΌΡΠ½Π½ΠΎΠΉ ΡΠΈΡΡΠ΅ΠΌΡ. ΠΠ΅ΡΡΠ½. ΠΠΊΠ°Π΄. ΠΠ΅Π΄. ΠΠ°ΡΠΊ. 6: 43−50.
- Adrain Π‘., Martin S.J. 2001. The mitochondrial apoptosome: a killer unleashed by the cytochrome seas. Trends. Biochem. Sci. 26: 390−396.
- Alnemri E.S., Livingston D.J., Nicholson D. W., Salvesen G. Thornberry N.A., Wong W.W., Yuan. I 1996. Human ICE/CED-3 protease nomenclature. Cell. 87: 171−77.
- Amanullah A., Liebermann D.A., Hoffman B. 2002. Deregulated c-Myc prematurely recruits both Type I and Type II CD95/Fas apoptotic pathways associated with terminal myeloid differentiation. Oncogene. 21: 1600 — 1610.
- Amati Π., Frank S.R., Donjerkovic D., Taubert S. 2001. Function of the c-Myc oncoprotein in chromatin remodeling and transcription. Biochim. Biophys. Acta. 1471: 135 145.
- Arango D., Mariadason J.M., Wilson A. J., Yang W., Corner G.A., Nicholas C., Aranes M.J., Augenlicht L.H. 2003. c-Myc overexpression sensitizes colon cancer cells to camptothecin-induced apoptosis. Br. J. Cancer. 89: 1757 1765.
- Aravind /., Dixit V.M., Koonin E.V. 1999. The domains of death: evolution of the apoptosis machinery. TIBS. 24: 47−53.
- Ashkenazi A., Herbst R.S. 2008. To kill a tumor cell: the potential of proapoptotic receptor agonists. J.Clin. Invest. 118: 1979−1990.
- Aujame L., Firko H. 1988. The major inducible heat shock protein hsp68 is not required for acquisition of thermal resistance in mouse plasmacytoma cell lines. Mol. Cell Biol. 8:5486−5494.
- Baker S.J., Reddy E.P. 1998. Modulation of life and death by the TNF receptor super! amily. Oncogene. 17: 3261−3270.
- Barnett Π’., Altschuler M., McDaniel C.N., Mascarenhas J. P. 1980. Heat shock induced proteins in plant cells. Dev. Genetics. 1: 331−344.
- Barr R.K., Bogoyevitch M.A. 2001. The c-Jun N-terminal protein kinase family of mitogen-activated protein kinases (JNK MAPKs). Int. J. Biochem. Cell Biol. 33: 1047−1063.
- Beere H.M., Green D.R. 2001. Stress management heat shock protein-70 and the regulation of apoptosis. Trends. Cell Biol. 11: 6−10.
- Bellamy C.O.C., Malcomison R.D.G., Harrison D.J., Wyllie A.H. 1995. Cell death in health desease: the biology and regulation of apoptosis. Sem. Cancer Biol. 6: 3−16.
- Bensaude O., Pinto M., Dubuis M.F., Nguyen V.T., Morange M. 1991. Protein denaturation during heat shock and related stress. Heat shock proteins. Berlin Springer-Verlag. 89−99.
- Blachere N.E., Udono H., Janetzki S., Li Z., Heike M., Srivastava P.K. 1993. Heat shock protein vaccines against cancer. J. Immunother. Emphasis. Tumor. Immunol. 14(4): 352−356.
- Boldin M.P., Goncharov T.M., Goltsev Y.V., Wallach D. 1996. Involvement of MACH, a novel MORTl/FADD-interacting protease, in Fas/APOl- and TNF receptor-induced cell death. Cell. 85: 803−815.
- Borner C., Monney L. 1999. Apoptosis without caspase: an inefficient molecular guillotine. Cell Death Diff. 6: 497−507.
- Bradford M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248 254.
- Buchberger A., Schroder H., Buttner M., Valencia A., Bukau B. 1994. A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Structural. Biology. 1: 95−101.
- Castedo M., Perfettinni J.-L., Roumier Π’., Andreau K., Medema R., Kroemer G. 2004. Cell death by mitotic catastrophe: a molecular definition. Oncogene. 23: 2825 2837.
- Chaudhary P.M., Eby M., Jasmin A. 1997. Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-ΠΊΠ pathway. Immunity. 7: 821−830.
- Chirico W.J., Waters M.G., Blobel G. 1988. 70K heat shock related protein stimulate protein translocation into microsomes. Nature. 333: 805−810.
- Ciocca D.R., Clark G.M., Tandon A. K., Fuqua S.A., Welch W.J., McGuire W.L. 1993. Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: prognostic implications. Natl. Cancer Inst. 85(7): 570−774.
- Ciocca D.R., Clark G.M., Tandon A.K., Fuqua S.A., Welch W.J., McGuire W.L. 1993. Biological and clinical implications of heat shock protein 27,000 (Hsp27): a review. J. Natl. Cancer Inst. 85: 570−574.
- Clemons N.J., Buzzard K., Steel R., Anderson R.L. 2005. Hsp72 inhibits Fas-mediated apoptosis upstream of the mitochondria in type II cells. J. Biol. Chem. 280: 9005−9012.
- Cohen G.M., Sun X.-M., Showden R.T., Dinsdale D" Skilleter D.N. 1992. Key morphological features of apoptosis may occur in the absence of internucleosomal DNA fragmentation. Biochem. 286: 331−334.
- Coultas L" Strasser A. 2003. The role of the Bcl-2 proteins un cancer. Semin. Cancer Biol. 13: 115−123.
- Davie J.R. 1998. Covalent modification of histones: expression from chromatin templates. Curr. Opin. Genet. Dev. 8: 173−178.
- Desagher S., Martinou J.C. 2000. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10(9): 369−377.
- Dignam J., Lebovitz R., Roeder R. 1983. Accurate transcription initiation by RNA-polymerase II in a soluble extract from isolated mammalian nuclei. Nucl. Acids Res. 5: 14 751 489.
- Dragovich Π’., Rudin C. M, Thompson C.B. 1998. Signal transduction pathways that regulate cell survival and cell death. Oncogene. 17: 3207−3213.
- Dubois M.F., Hovanessian A.G., Bensaude O. 1991. Heat-shock-induced denaturation of proteins. Characterization of the insolubilization of the interferone induced p68 kinase. J. Biol. Chem. 266: 9707−9711.
- Dworniczak Π., Mirault M.-E. 1987. Structure and expression of a human gene coding for a 71 kd heat shock «cognate» protein. Nucl. Acid Res. 15: 5181−5197.
- Eilers M., Picard D., Yamamoto K.R., Bishop J.M. 1989. Chimaeras of myc oncoprotein and steroid receptors cause hormone-dependent transformation of cells. Nature. 340: 66−68.
- Ellis R.J. 1987. Proteins as molecular chaperones. Nature. 328: 378−379.
- Evan G., Littlewood T. 1998. A matter of life and cell death. Science. 281(5381): 1317−1322.
- Fearnhead Π.Π., Rodrigues J., Govek E.E., Guo W., Kobayashi R., Hannon G., Lazebnik Y.A. 1998. Oncogene-dependent apoptosis is mediated by caspase-9. Proc. Natl. Acad. Sci. USA. 95: 13 664−13 669.
- Fehrenbacher N., Gyrd-Hansen M., Poulsen Π., Felbor U., Kallunki Π’., Boes M., Weber E., Leist M., Jaattela M. 2004. Sensitization to the lysosomal death pathway upon immortalization and transformation. Cancer Res. 64(15): 5301−5310.
- Fest Π’., Mougey V., Dalstein V., Hagerty M" Milette D., Silva S" Mai S. 2002. c-Myc overexpression in Ba/F3 cells simultaneously elicits genomic instability and apoptosis. Oncogene. 21: 2981 2990.
- Flaherty K.M., DeLuca-Flaherty C., McKay D.B. 1990. Three- dimentional structure of the ATP-ase fragment of a 70k heat-shock cognate protein. Nature. 346: 623−628.
- Flechtner J.B., Cohane K.P., Mehta S., Slusarewicz P., Leonard A.K., Barber B.H., Levey D.L., Andjelic S. 2006. High-affinity interactions between peptides and heat shock protein 70 augment CD8+ T lymphocyte immune responses. J. Immunol. 177: 1017−1027.
- Frydman J., Honfeld J. 1997. Chaperones get in touch: the Hip-Hop connection. Trends Biocem. Sci. 22: 87−92.
- Fulda S" Debatin KM. 2006. Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy. Oncogene. 25: 4798−4811.
- Fulda S., Lutz JK. Schwab M, Debatin K.-M. 1999. MycN sensitizes neuroblastoma cells for drug-induced apoptosis. Oncogene. 18: 1479 1486.
- Gabai V.L., Meriin Π.Π., Mosser D.D. 1997. Hsp70 prevents activation of stress kinases. A novel pathway of cellular thermotolerance. J. Biol. Chem. 272: 18 033−18 037.
- Gartel A.L., Shchors K. 2003. Mechanisms of c-myc mediated transcriptional repression of growth arrest genes. Exp. Cell. Res. 283: 17−21.
- Gastpar R., Gross C., Rossbacher L., Ellwart J., Riegger J., Multhoff G. 2004. The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells. J. Immunol. 172: 972−980.
- Ghobrial I.M., Witzig Π’.Π., Adjei A.A. 2005. Targeting apoptosis pathways in cancer therapy. CA Cancer J. Clin. 55(3): 178−194.
- Gotoh Π’. Terada K., Oyadomari S., Mori M. 2004. Hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ. 11: 390−402.
- Green D.R., Evan G.I. 2002. A matter of life and death. Cancer Cell. 2: 19−29.
- Green D.R., ReedJ.C. 1998. Mitochondria and apoptosis. Science. 281: 1309−1312.
- Guzhova I. V., Darieva Z.A., Rocha Melo A., Margulis B.A. 1997. Major stress protein 70kDa and subunits of NF-kB regulatory complex are associated in human T-lymphoma cells. Cell Stress Chap. 2: 132−139.
- Heads R.J., Latchman D.S., Yellon D.M. 1994. Stable high level expression of a transfected human HSP70 gene protects a heart-derived muscle cell line against thermal stress. J. Mol. Cell. Cardiol. 26: 695−699.
- Hengartner M.O., Horvitz H.R. 1994. C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell. 76: 665−676.
- Hoffman Π., Lieberman D.A. 1998. The protooncogene c-myc and apoptosis. Oncogene. 17: 3351−3357.
- Hogarty M.D. 2003. The requirement for evasion of programmed cell death in neuroblastomas with MYCN amplification. Cancer Lett. 197: 173 179.
- Hohfeld J., Jentsch S. 1997. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16: 6209−6216.
- Hsu H., Huang J., Shu H.B. 1996. TNF-dependent recruitment of the protein kinase RIP to the TNFreceptor-1 signaling complex. Immunity. 4: 387−396.
- Huang P., Oliff A. 2001. Signaling pathways in apoptosis as potential targets for cancer therapy. Trends Cell Biol. 11: 343−348.
- Huang C., Yu Π―, Wang Q., Ma W" Xia D., Yi P., Zhang L., Cao X 2004. Potent antitumor effect elicited by superantigen-1 inked tumor cells transduced with heat shock protein 70 gene. Cancer Sci. 95: 160−167.
- Hunt C., Morimoto R.I. 1985. Concerved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc. Natl. Ac. Sci. USA. 82: 6455−6459.
- Jaattela M. 1999. Escaping cell death: survival proteins in cancer. Exp. Cell Res. 248(1): 30−43.
- Jaattela M., Wissing D., Kokholm K. 1998. Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J. 17: 6124−6134.
- Jiang M.-R., Li Y.-C., Yang Y., Wu J.-R. 2003. c-Myc degradation induced by DNA damage results in apoptosis of CHO cells. Oncogene. 22: 3252 3259.
- Joza N., Kroemer G., Penninger M. 2002. Genetic analysis of the mammalian cell death machinery. Trends Genet. 18: 142−150.
- Juin P., Hueber A.O., Littlewood Π’., Evan G. 1999. c-Myc-induced sensitization to apoptosis is mediated through cytochrome Ρ release. Genes Dev. 13: 1367−1381.
- Juin P., Hunt A., Littlewood Π’., Griffiths Π., Swigart L.B., Korsmeyer S., Evan G. 2002. c-Myc functionally cooperates with Bax to induce apoptosis. Mol. Cell Biol. 22: 6158 -6169.
- Kampinga H.H. 2006. Chaperones in preventing protein denaturation in living cells and protecting against cellular stress. Handb. Exp. Pharmacol. 172: 1−42.
- Kampinga H.H., Brunsting J.F., Konings A.W.T. 1992. Acquisition of thermotolerance induced by heat and arsenite in HeLa S3 cells: multiple pathways to induce tolerance? J. Cell Physiol. 150: 406−415.
- Kelley P.M., Schlesinger M.J. 1982. The effect of amino acid analogues and heat shock on gene expression in chicken fibroblasts. Cell. 15: 1277−1286.
- Kerr J.F.R., Wyllie A.H., Currie A.R. 1972. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Brit. J. Cancer. 26: 239−257.
- Kislin K.L., Marron M.T., Li G., Graner M.W., Katsanis E. 2007. Chaperone-rich cell lysate embedded with BCR-ABL peptide demonstrates enhanced anti-tumor activity against a murine BCR-ABL positive leukemia. FASEB J. 21: 2173−2184.
- Klefstrom J., Verschuren E.W., Evan G. 2002. c-Myc augments the apoptotic activity of cytosolic death receptor signaling proteins by engaging the mitochondrial apoptotic pathway. J. Biol. Chem. 277(45): 43 224−43 232.
- Klein S.D., Brune B. 2002. Heat shock protein attenuates nitric oxide-induced apoptosis inRAW macrophages by preventing cytochrome Ρ release. Biochem. J. 362: 635 641.
- Kochevar D.T., Aucoin M.M., Cooper J. 1991. Mammalian heat shock proteins: an overview with a systems perspective. Toxicology Letters. 56: 243−267.
- Kost S.L., Smith D. E, Sullivan W.P., Welch W.J., Toft D.O. 1989. Binding of heat shock proteins to the avian progesteron receptor. Mol. Cell Biol. 9: 3829−3838.
- Kumar S., Colussi P.A. 1999. Prodomains-adaptors-oligomerization: the pursuit of caspase activation in apoptosis. TIBS. 24: 1−4.
- C.Y., Lee J.S., ΠΠΎ Y.G., Kim J.I., Seo J.S. 2000. Heat shock protein 70 inhibits apoptosis downstream of cytochrome Ρ release and upstream of caspase-3 activation. J. Biol. Chem. 275: 25 665−25 671.
- Maclean ΠΠ., Keller U.B., Rodrigues-Galindo C., Nilsson J.A., Cleveland J.L. 2003. c-Myc augments gamma irradiation-induced apoptosis by suppressing Bc1-Xl. Mol. Cell. Biol. 23: 4256−4270.
- Ma kin G., Hickman J.A. 2000. Apoptosis and cancer chemotherapy. Cell Tissue Res. 301: 143−152.
- McAllister L, Finkelstein D.B. 1980. Heat shock response and thermal resistance in Yeast. Biochemical and Biophysical Research Communications. 93: 819−824.
- Meriin A.B., Gabai V.L. 1998. Proteasome inhibitors activate stress kinases and induce Hsp72. Diverse effects on apoptosis. J. Biol. Chem. 273: 6373−6379.
- Mestril R., Dillmann W.H. 1995. Heat shock proteins and protection against myocardial ischemia. J. Mol. Cell Cardiol. 27: 45−52.
- Mitchell K.O., Ricci S" Myashita Π’., Dicker D., Jin Z., Reed J., El-Deiry W.S. 2000. Bax is a transcriptional target and mediator of c-Myc-induced apoptosis. Cancer Res. 60: 6318−6325.
- Moreno de Alboran I., Baena E., Martinez-A. C. 2004. c-Myc-deficient Π lymphocytes are resistant to spontaneous and induced cell death. Cell Death Diff. 11: 61−68.
- Morimoto R.I., Kline M.P., Bimston D.N., Cotto J.J. 1997. The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones. Essays Biochem. 32: 17−29.
- Morrish F., Giedi C, Hockenbery D. 2003. c-MYC apoptotic function is mediated by NRF-1 target genes. Genes Dev. 17(2): 240−255.
- Mosser D.D., Caron A.W., Bourget L. 1997. Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol. Cell. Biol. 17: 5317−5327.
- Mosser D.D., Caron A.W., Bourget L., Meriin A.B., Sherman M.Y., Morimoto R.I., Massxe B. 2000. The chaperone function of hsp70 is required for protection against stress-induced apoptosis. Mol. Cell Biol. 20: 7146−7159.
- Mailer P., Hrstka R., Coomber D" Lane D.P., VojtesekB. 2008. Chaperone-dependent stabilization and degradation of p53 mutants. Oncogene. 27: 3371−3383.
- Nagata S., Golshtein P. 1995. The Fas death factor. Science. 267: 1449−1456.
- Nikiforov M.A., Popov N., Kotenko ./., Henriksson M" Cole M.D. 2003. The Mad and ΠΡΡ domains are fiintionally equivalent. J. Biol. Chem. 278: 11 094−11 099.
- Nilsson J.A., Cleveland J.L. 2003. ΠΡΡ pathways provoking cell suicide and cancer. Oncogene. 22: 9007 9021.
- Pandey P., Farber R., Nakazawa A. 2000. Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3. Oncogene. 19: 1975−1981.
- Park H.S., Lee J.S., Huh S., Seo J., Choi E. 2001. Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase. EMBO J. 20: 446−456.
- Pelengaris S., Khan M. 2003. The many faces of c-Myc. Arch. Biochem. Biophys. 416: 129−136.
- Pelham H.R.B. 1986. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell. 46: 956−961.
- Perreault J., Lemieux R. 1993. Rapid apoptotic cell death of B-cell hybridomas in absence of gene expression. J. Cell Physiol. 156: 286−293.
- Piura Π., Rabinovich A. Yavelsky V., Wolfson M. 2002. Heat shock proteins and malignancies of the female genital tract. Harefuah. 141: 969−1010.
- Polla B.S., Kantengwa S. 1996. Mitochondria are selective targets for the protective effects of heat shock against oxidative injury. PNAS. 93: 6458−6463.
- Prendergast G.C. 1999. Mechanisms of apoptosis by c-Myc. Oncogene. 18: 29 672 987.
- Rashmi R., Kumar S., Karunagaran D. 2004. Ectopic expression of HSP70 confers resistance, and silencing its expression sensitizes human colon cancer cells to curcumin-induced apoptosis. Carcinogenesis. 25: 179−187.
- Ravagnan L., Gurbuxani S" Susin S.A., Maisse C., Datigas E., Zamzami N., ΠΠ°ΠΊ Π’. Jaattela M., Penninger J.M., Garrido C. Kroemer G. 2001. Heat-shock protein 70 antagonizes apoptosis-inducing factor. Nature Cell. 3: 839−843.
- Reed J. C. 2003. Apoptosis-targeted therapies for cancer. Cancer Cell. 3: 17−22.
- Reed J.C. 2006. Drug insight: cancer therapy strategies based on restoration of endogenous cell death mechanisms. NatClin. Pract. Oncol. 3: 388−398.
- Ricaniadis Π7!, Kataki A., Agnantis N. Androulakis G., Karakousis C.P. 2001. Long-term prognostic significance of HSP-70, c-myc and HLA-DR expression in patients with malignant melanoma. Eur. J. Surg. Oncol. 27(1): 88−93.
- Ritossa F. 1962. A new puffing pattern induced by heat shock and DNP in Drosophila melanogaster. Experientia. 18: 671−573.
- Ruchalski Π, Mao H., Li Z., Wang Z., Gillers S., Wang Y" Mosser D.D., Gabai .V, Schwartz J.H., Borkan S.C. 2006. Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation. J. Biol. Chem. 281: 7873−7880.
- Ruiz-Vela A., A/bar J.P., Martinez C.A. 2001. Apaf-1 localization is modulated indirectly by Bcl-2 expression. FEBS Lett. 501: 79−83.
- Saleh A., Srinivasula S.M., Balkir L., Robbins P.D., Alnemri E.S. 2000. Negative regulation of the Apaf-1 apoptosome by Hsp70. Nat. Cell Biol. 2: 476−483.
- Samali A., Cai J., Zhivotovsky Π., Jones D.P., Orrenius S. 1999. Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and HsplO in the mitochondrial fraction of Jurkat cells. EMBO J. 18(8): 2040−2048.
- Samali A., Holmberg Π‘Π., Sistonen L" Orrenius S. 1999. Thermo tolerance and cell death are distinct cellular responses to stress: dependence on heat shock protein. FEBS Letters. 461: 306−310.
- Samali A., Orrenius S. 1998. Heat shock proteins: regulators of stress response and apoptosis. Cell Stress Chaperones. 3(4): 228−236.
- Sanders E.J., Wride M.A. 1995. Programmed cell death in development.Int. Rev. Cytol. 163: 105−173.
- Salon A., Taira Π’., Iguchi- Ariga S., Ariga II. 2001. A novel transrepression pathway of c-Myc. J. Biol. Chem. 276: 46 562−46 567.
- Scherer L.C., Dalman F.S., Massa E., Mechinchi S., Pratt W.B. 1990. Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex. J. Biol. Chem. 265: 21 397−21 400.
- Schneider P., Thome M, Burns K. 1997. TRAIL Receptors 1 (DR4) and 2 (DR5) signal FADD-dependent apoptosis and activate NF-ΠΊΠ. Immunity. 7: 831−836.
- Simpson N.H., Milner A.N., Al-Rubeai M. 1997. Prevention of hybridoma cell death by bcl-2 during sub-optimal culture conditions. Biotechnol. Bioeng. 54: 1−16.
- Soucek L., Nasi S., Evan G.I. 2004. Omomyc expression in skin prevents Myc-induced papillomatosis. Cell Death Dif. 33: 1−8.
- Soucie E.L., Annis M.G., Sedivy J., Filmus J., Leber Π., Andrews D.W., Penn L.Z. 2001. ΠΡΡ potentiates apoptosis by stimulating Bax activity at the mitochondria. Mol. Cell. Biol. 21:4725−4736.
- Sriram M., Osipiuk J., Freeman Π., Morimoto R., Jochimiak A. 1997. Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain. Structure. 5: 403 414.
- Stankiewicz A.R., Lachapelle G., Foo C.P., Radicioni S.M., Mosser D.D. 2005. Hsp70 inhibits heat-induced apoptosis upstream of mitochondria by preventing Bax translocation. J. Biol. Chem. 280: 38 729−38 739.
- Steel R., Doherty J.P., Buzzard K., Clemons N., Hawkins C.J., Anderson R.L. 2004. Hsp72 inhibits apoptosis upstream of the mitochondria and not through interactions with Apaf-1. J. Biol. Chem. 279: 51 490−51 499.
- Stennicke H.R., Ryan C.A., Salvesen G.S. 2002. Reprieval from execution: the molecular basis of caspase inhibition. Trends Biochem. Sci. 27(2): 94−101.
- Stevenson M.A., Calderwood S.K. 1990. Members of the 70-kilodalton heat shock protein family contain highly conserved calmodulin-binding domain. Mol. Cell Biol. 10: 1234−1238.
- Slomberg P.W. 1991. Control cell lineage and cell fate during nematode development. Cuit. Top. Dev. Biol. 25: 177−225.
- Sun Y., Ouyang Y.B., Xu L., Chow A.M., Anderson R., Hecker J.G., GiffardR.G. 2006. The carboxyl-terminal domain of inducible Hsp70 protects from ischemic injury in vivo and in vitro. J. Cereb. Blood Flow Metab. 26: 937−950.
- Syrigos K.N., Harrington K.J., Karayiannakis A.J., Sekara E., Chatziyianni E., Syrigou E.I., and Waxman J. 2003. Clinical significance of heat shock protein-70 expression in bladder cancer. Urology. 61: 677−680.
- Tavaria M., Gabriele Π’., Kola /., Anderson R.L. 1996. A hitchhiker’s guide to the human HSP70 family. Cell Stress Chap. 1(1): 23−28.
- Thornberry N.A., Lazebnik Y. 1998. Caspases: enemies within. Science. 281(5381): 1312−1316.
- Tissieres A., Mitchell H. K, Tracy U.M. 1974. Protein synthesis in salivary glands of Drosophila melongaster. J. Mol. Biol. 84: 389−398.
- Towbin H., Staeheln Π’., Gordon J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. PNAS. 7: 4350−4354.
- Towbin H, Gordon J. 1984. Immunoblotting and dot immunobinding--current status and outlook. J. Immunol. Methods. 72(2): 313−340.
- Vaux D.L. 1999. Caspases and apoptosis biology and terminology. Cell Death Diff. 6: 493−494.
- Vaux D.L., Strasser A. 1996. The molecular biology of apoptosis. PNAS USA. 93: 2239−2244.
- Vermeulen K., Van Bockstaele D.R., Berneman Z.N. 2005. Apoptosis: mechanisms and relevance in cancer. Ann. Hematol. 84(10): 627−39.
- Vol loch V, Gabai V.L., Rits S., Sherman M.Y. 1999. ATPase activity of the heat shock protein is dispensable for its effects on dephosphorilation of stress kinase JNK and on heat-induced apoptosis. FEBS Lett. 461: 73−76.
- Volloch V., Gabai V.L. Rits S. Force Π’., Sherman M.Y. 2000. HSP72 can protect cells from heat-induced apoptosis by accelerating the inactivation of stress kinase JNK. Cell Stress & Chap. 5(2): 139−147.
- Vousden K.H., LuX., 2002. Live or let die: cell’s response to p53. Nat. Rev. Cancer. 2: 594−604.
- Welch W.J. 1990. The mammalian stress response: Cell physiology and biochemistry of stress proteins. Stress proteins in biology and medicine. New York CSH Press, p. 223−278.
- Welch W.J., Feramisco J.R. 1985. Rapid purification of mammalian 70-kDa stress proteins: affinity of the proteins for nucleotides. Mol. Cell Biol. 5: 1229−1237.
- Wu Y., Mehew J.A., Heckman C.A., Arcinas M., Boxer L.M. 2001. Negative regulation of bcl-2 expression by p53 in hemapoetric cells. Oncogene. 20: 240−251.
- Xanthoudakis S., Roy S., Rasper D., Hennessey Π’., Aubin Y., Cassady R., Tawa Π’., Ruel R., Rosen A., Nicholson D.W. 1999. Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis. EMBO J. 18: 2049−2056.
- Xia Z, Dickens M., Raingeaud J. 1995. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science. 270: 1326−1331.
- Yamamori Π’., Ito K., Nakamura Y, Yura T. 1978. Transient regulation of protein synthesis in Escherichia coli upon shift-up of growth temperature. J. Bacteriol. 134: 11 331 140.
- Yost H.J., Lindquist S. 1991. Heat shock proteins affect RNA processing during heat shock response. Mol. Cell Biol. 11: 1062−1068.
- Zornig A., Hueber A.O., Baum W., Evan G. 2001. Apoptosis regulators and their role in tumorigenesis. Biochim. Biophys. Acta. 1551: 1−37.