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From: TSS ()
Subject: The 14-3-3 Protein Forms a Molecular Complex with Heat Shock Protein Hsp60 and Cellular Prion Protein
Date: October 11, 2005 at 2:47 pm PST

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The 14-3-3 Protein Forms a Molecular Complex with Heat Shock
Tue Oct 11, 2005 16:38
70.110.83.173

The 14-3-3 Protein Forms a Molecular Complex with Heat Shock Protein Hsp60 and Cellular Prion Protein.
Journal of Neuropathology & Experimental Neurology. 64(10):858-868, October 2005.
Satoh, Jun-ichi MD, PhD; Onoue, Hiroyuki MD, PhD; Arima, Kunimasa MD, PhD; Yamamura, Takashi MD, PhD
Abstract:
The 14-3-3 protein family consists of acidic 30-kDa proteins composed of 7 isoforms expressed abundantly in neurons and glial cells of the central nervous system (CNS). The 14-3-3 protein identified in the cerebrospinal fluid provides a surrogate marker for premortem diagnosis of Creutzfeldt-Jakob disease, although an active involvement of 14-3-3 in the pathogenesis of prion diseases remains unknown. By protein overlay and mass spectrometric analysis of protein extract of NTera2-derived differentiated neurons, we identified heat shock protein Hsp60 as a 14-3-3-interacting protein. The 14-3-3[zeta] and [gamma] isoforms interacted with Hsp60, suggesting that the interaction is not isoform-specific. Furthermore, the interaction was identified in SK-N-SH neuroblastoma, U-373MG astrocytoma, and HeLa cervical carcinoma cells. The cellular prion protein (PrPC) along with Hsp60 was coimmunoprecipitated with 14-3-3 in the human brain protein extract. By protein overlay, 14-3-3 interacted with both recombinant human Hsp60 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 Hsp60 spanning amino acid residues 27-287 and the NTF of PrPC spanning amino acid residues 23-137. By immunostaining, the 14-3-3 protein Hsp60 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 Hsp60 and PrPC in the human CNS under physiological conditions and suggest that this complex might become disintegrated in the pathologic process of prion diseases.

(C) 2005 American Association of Neuropathologists, Inc


http://www.jneuropath.com/pt/re/jnen/abstract.00005072-200510000-00004.htm;jsessionid=DMtnIWUn96qXEOCLOnxxqId8RosR7pAEOV6DN1gPliFYMJmAfx6O!-365670234!-949856145!9001!-1


TSS

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