PMID- 17180927
OWN - NLM
STAT- MEDLINE
DCOM- 20070110
LR  - 20140401
IS  - 2310-6972 (Print)
IS  - 2310-6905 (Linking)
VI  - 52
IP  - 5
DP  - 2006 Sep-Oct
TI  - [The non-functioning chaperonin GroEL stimulates protein aggregation].
PG  - 518-24
AB  - To clarify the role of chaperones in the development of amyloid diseases, the 
      interaction of the chaperonin GroEL with misfolded proteins and recombinant 
      prions has been studied. The efficiency of the chaperonin-assisted folding of 
      denatured glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was shown to decrease 
      in the presence of prions. Prions are capable of binding to GroEL immobilized on 
      Sepharose, but this does not prevent the interaction between GroEL and other 
      denatured proteins. The sizes of individual proteins (GroEL, GAPDH, and the 
      recombinant prion), as well as aggregates formed after their mixing, were 
      determined by the dynamic light scattering method. It was shown that at 25 
      degrees C the non-functioning chaperonin (equimolar mixture of GroEL and GroES in 
      the absence of Mg-ATP) bound prion yielding large aggregates (greater than 400 
      nm). The addition of Mg-ATP decreased significantly the aggregate size to 70-80 
      nm. On the blocking of one of the chaperonin centers by oxidized denatured GAPDH, 
      the aggregate size increased to 1200 nm, and the addition of Mg-ATP did not 
      prevent the aggregation. These data indicate the significant role of chaperonins 
      in the formation of amyloid structures and demonstrate the acceleration of 
      aggregation in the presence of functionally inactive chaperonins. The suggested 
      model can be used for the analysis of the efficiency of antiaggregants in the 
      system containing chaperonins.
FAU - Naletov, I N
AU  - Naletov IN
FAU - Shmal'gauzen, E V
AU  - Shmal'gauzen EV
FAU - Shalova, I N
AU  - Shalova IN
FAU - Pleten', A P
AU  - Pleten' AP
FAU - Tsiriul'nikov, K
AU  - Tsiriul'nikov K
FAU - Ertl', T
AU  - Ertl' T
FAU - Muronets, V I
AU  - Muronets VI
LA  - rus
PT  - English Abstract
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Russia (Federation)
TA  - Biomed Khim
JT  - Biomeditsinskaia khimiia
JID - 101196966
RN  - 0 (Amyloid)
RN  - 0 (Chaperonin 60)
RN  - 0 (Prions)
RN  - EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases)
SB  - IM
MH  - Amyloid/*chemistry/metabolism
MH  - Amyloidosis/metabolism
MH  - Animals
MH  - Chaperonin 60/*chemistry/metabolism
MH  - Glyceraldehyde-3-Phosphate Dehydrogenases/*chemistry/metabolism
MH  - Prions/*chemistry/metabolism
MH  - Protein Binding
MH  - Protein Denaturation
MH  - Rats
MH  - Sheep
EDAT- 2006/12/22 09:00
MHDA- 2007/01/11 09:00
CRDT- 2006/12/22 09:00
PHST- 2006/12/22 09:00 [pubmed]
PHST- 2007/01/11 09:00 [medline]
PHST- 2006/12/22 09:00 [entrez]
PST - ppublish
SO  - Biomed Khim. 2006 Sep-Oct;52(5):518-24.