PMID- 15120623
OWN - NLM
STAT- MEDLINE
DCOM- 20040625
LR  - 20201208
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 318
IP  - 2
DP  - 2004 May 28
TI  - Interaction of the hepatitis B virus X protein (HBx) with heat shock protein 60 
      enhances HBx-mediated apoptosis.
PG  - 461-9
AB  - Understanding the function of the hepatitis B virus X protein (HBx) is 
      fundamental to elucidating the underlying mechanisms of hepatitis and 
      hepatocarcinogenesis caused by hepatitis B virus (HBV) infection. We identified 
      heat shock protein 60 (Hsp60) as a novel cellular target of HBx by the 
      combination of affinity purification and mass spectrometry. Physical interaction 
      between HBx and Hsp60 was confirmed by standard immunoprecipitation and 
      immunoblot methods. Analysis of HBx deletion constructs showed that amino acids 
      88-117 of HBx were responsible for the binding to Hsp60. Confocal laser 
      microscopy demonstrated that HBx and Hsp60 colocalized in mitochondria. 
      Furthermore, terminal deoxynucleotidyl transferase-mediated dUTP end labeling 
      (TUNEL) revealed that the introduction of Hsp60 into cells facilitated 
      HBx-induced apoptosis. These findings suggest the importance of the molecular 
      chaperon protein Hsp60 to the function of HBV viral proteins.
FAU - Tanaka, Yasuo
AU  - Tanaka Y
AD  - Department of Gastroenterology, Graduate School of Medicine, University of Tokyo, 
      7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan.
FAU - Kanai, Fumihiko
AU  - Kanai F
FAU - Kawakami, Takayuki
AU  - Kawakami T
FAU - Tateishi, Keisuke
AU  - Tateishi K
FAU - Ijichi, Hideaki
AU  - Ijichi H
FAU - Kawabe, Takao
AU  - Kawabe T
FAU - Arakawa, Yoshihiro
AU  - Arakawa Y
FAU - Kawakami, Takao
AU  - Kawakami T
FAU - Nishimura, Toshihide
AU  - Nishimura T
FAU - Shirakata, Yumiko
AU  - Shirakata Y
FAU - Koike, Katsuro
AU  - Koike K
FAU - Omata, Masao
AU  - Omata M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Chaperonin 60)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Trans-Activators)
RN  - 0 (Viral Regulatory and Accessory Proteins)
RN  - 0 (hepatitis B virus X protein)
SB  - IM
MH  - Amino Acid Sequence
MH  - Apoptosis/*physiology
MH  - Cell Line
MH  - Chaperonin 60/genetics/*metabolism
MH  - Chromatography, Affinity
MH  - Hepatocytes/cytology/metabolism
MH  - Humans
MH  - Immunoblotting
MH  - Immunohistochemistry
MH  - In Situ Nick-End Labeling
MH  - Mass Spectrometry
MH  - Mitochondria/metabolism
MH  - Molecular Sequence Data
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Recombinant Proteins/genetics/metabolism
MH  - Sequence Analysis, Protein/methods
MH  - Sequence Deletion
MH  - Trans-Activators/*metabolism/physiology
MH  - Transfection
MH  - Viral Regulatory and Accessory Proteins
EDAT- 2004/05/04 05:00
MHDA- 2004/06/26 05:00
CRDT- 2004/05/04 05:00
PHST- 2004/02/17 00:00 [received]
PHST- 2004/05/04 05:00 [pubmed]
PHST- 2004/06/26 05:00 [medline]
PHST- 2004/05/04 05:00 [entrez]
AID - S0006291X04007673 [pii]
AID - 10.1016/j.bbrc.2004.04.046 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2004 May 28;318(2):461-9. doi: 
      10.1016/j.bbrc.2004.04.046.