| Interacting proteins: P04156 and P10809 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P04156 and P10809 |
Pubmed |
SVM Score :0.0 |
| To study a role of PrPC in the regulation of expression of heat shock proteins ( HSPs ) , a group of molecular chaperones , heat induced expression of major HSPs ( HSP 105 , HSP90alpha , HSP 72 , HSC 70 , HSP 60 , and HSP 25 ) was investigated in cultured skin fibroblasts isolated from the mice homogeneous for a disrupted PrP gene ( PrP / mice ) by Western blot analysis and immunocytochemistry . ^^^ Furthermore , the levels of constitutive expression of HSP 105 , HSC 70 , HSP 60 , and HSP 25 were similar between the brain tissues isolated from the PrP / and PrP+ / + mice . ^^^ |
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| Interacting proteins: P04156 and P10809 |
Pubmed |
SVM Score :0.0 |
| Here we report that the bacterial chaperonin GroEL , a close homolog of eukaryotic Hsp 60 , can catalyze the aggregation of chemically denatured and of folded , recombinant PrP in a model reaction in vitro . ^^^ These results show that chaperonins of the Hsp 60 class can , in principle , mediate PrP aggregation de novo , i . e . independently of a pre existent PrP ( Sc ) template . . ^^^ |
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| Interacting proteins: P04156 and P10809 |
Pubmed |
SVM Score :0.0 |
| A series of structural intermediates in the putative pathway from the cellular prion protein PrP ( C ) to the pathogenic form PrP ( Sc ) was established by systematic variation of low concentrations ( < 0 . 1 % ) of the detergent sodium dodecyl sulfate ( SDS ) or by the interaction with the bacterial chaperonin GroEL . ^^^ |
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| Interacting proteins: P04156 and P10809 |
Pubmed |
SVM Score :0.0 |
| The specificity of the interaction was confirmed in vitro for the recombinant proteins PrPc 23 231 and rPrP 27 30 fused to glutathione S transferase with recombinant human Hsp 60 as well as the bacterial GroEL . ^^^ The interaction site for recombinant Hsp 60 and GroEL proteins was mapped between amino acids 180 and 210 of the prion protein by screening with a set of recombinant PrPc fragments . ^^^ Screening of a HeLa cDNA library identified heat shock protein 60 ( Hsp 60 ) , a cellular chaperone as a major interactor for PrPc . ^^^ Prion protein PrPc interacts with molecular chaperones of the Hsp 60 family . ^^^ |
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| Interacting proteins: P04156 and P10809 |
Pubmed |
SVM Score :0.0 |
| We report here that Hsp 60 , a member of the GroEL family of chaperonins , of B . abortus is capable of interacting directly or indirectly with cellular prion protein ( PrPC ) on host cells . ^^^ Under in vitro and in vivo conditions , Hsp 60 of B . abortus bound to PrPC . ^^^ Hsp 60 of B . abortus , expressed on the surface of Lactococcus lactis , promoted the aggregation of PrPC but not PrPC tail formation on macrophages . ^^^ These results indicate that signal transduction induced by the interaction between bacterial Hsp 60 and PrPC on macrophages contributes to the establishment of B . abortus infection . . ^^^ |
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| Interacting proteins: P04156 and P10809 |
Pubmed |
SVM Score :0.0 |
| The cellular prion protein ( PrPC ) along with Hsp 60 was coimmunoprecipitated with 14 3 3 in the human brain protein extract . ^^^ By protein overlay , 14 3 3 interacted with both recombinant human Hsp 60 and PrPC produced by Escherichia coli , indicating that the molecular interaction is phosphorylation independent . ^^^ The 14 3 3 binding domain was located in the N terminal half ( NTF ) of Hsp 60 spanning amino acid residues 27 287 and the NTF of PrPC spanning amino acid residues 23 137 . ^^^ By immunostaining , the 14 3 3 protein Hsp 60 and PrPC were colocalized chiefly in the mitochondria of human neuronal progenitor cells in culture , and were coexpressed most prominently in neurons and reactive astrocytes in the human brain . ^^^ These observations indicate that the 14 3 3 protein forms a molecular complex with Hsp 60 and PrPC in the human CNS under physiological conditions and suggest that this complex might become disintegrated in the pathologic process of prion diseases . . ^^^ |
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