Heat shock protein peptide

Raz, I., Elias, D., Avron, A., Tamir, M., Metzger, M and Cohen, I.R. (2001) Betacell function in new-onset type 1 diabetes and immunomodulation with a heat-shock protein peptide (DiaPep277) a randomised, double-blind, phase II trial. Lancet 24, 1749-1753. 

Oncophage (vitespen) is a vaccine that contains gp96 heat shock protein/peptide complex from an individual patient s tumor. It has been evaluated in phase III trials for kidney cancer and metastatic melanoma. 

Heat Shock Protein-Peptide Complexes as Anti-Viral Agents... 

Srivastava PK (1997) Purification of heat shock protein-peptide complexes for use in vaccination against cancers and intracellular pathogens. Methods 12 165-171 Srivastava PK, Menoret A, Basu S, Binder RJ, McQimde KL (1998) Heat shock proteins come of age primitive functions acquire new roles in an adaptive world. Immunity 8 657-665... 

Pervin KCA, Shinnick T, Mizydiima Y, et al. T cells epitope expression of myco-hacterial and homologous human 65-kilodalton heat shock protein peptides in short term cell hnes from patients with Behget s disease. J Immunol 1993 151 2273-2282. 

For MK2, one may use a peptide substrate (see, e.g., Manke et al, 2005) or recombinant heat shock protein (hsp) 25 (Stokoe et al, 1992). For the peptide substrate, analysis is as described for the p90RSK assay. If using hsp27 as substrate, samples of the reaction products are analyzed by SDS-PAGE and autoradiography or quantitation performed by phosphorimager. 

Photocrosslinkers have been incorporated in E. coli to confirm close contact between specific residues of a protein and its substrate. ClpB, a heat shock protein that aids in the disaggregation and refolding of proteins during the heat shock response, has a conserved aromatic residue (Tyr251) in the central pore of its AAA+ domain, considered to be the main substrate recognition residue. " After Tyr251 in ClpB was replaced with />BpA, biotinylated substrate peptides were shown to be crosslinked upon UV light exposure, but not if BpA was incorporated elsewhere in the AAA+ domain of this protein. 

Nelson RJ, Ziegelhoffer T, Nicolet C, Werner-Washburne M, Craig EA (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71 97-105 Nissen P, Hansen J, Ban N, Moore PB, Steitz TA (2000) The structural basis of ribosome activity in peptide bond synthesis. Science 289 920-930... 

Upon entering the cell, the steroid molecule initially binds to the steroid receptor protein (E domain) to form the steroid-hormone-receptor complex. This complex concomitantly binds to an additional eight or more other peptides (also via the E domain) these peptides are termed chaperone peptides and consist of macromolecules such as heat shock proteins (e.g., hsp70, hsp90). The chaperone peptides help to twist and turn the steroid receptor protein into an improved three-dimensional shape for final and optimal binding of the steroid molecule. Following binding of the chaperone peptides, the steroid-hormone-receptor complex becomes a mature steroid-hormone-receptor... 

Calabrese Y, Calvani M, Butterfield DA. 2006d. Acetyl-L-camitine-induced up-regulation of heat shock proteins protects cortical neurons against amyloid-beta peptide 1-42-mediated oxidative stress and neurotoxicity Implications for Alzheimer s disease. 

Otvos, L., Jr., Rogers, M. E., Consolvo, P. J., Condie, B. A., Lovas, S., Bulet, P. and Blaszczyk-Thurin, M. (2000) Interaction between heat shock proteins and antimicrobial peptides. Biochemistry 39, 14150-14159. 

The conformation of Xaa-Pro peptide bonds in the newly synthesized polypeptide chains prior to cellular folding is not known. The product of protein biosynthesis could be a uniform chain with all peptide bonds in the trans conformation. If this chain starts to fold immediately, then the trom-prolines would be in the correct conformation already, the cis-prolines would be in the incorrect isomeric state, and their trans — cis isomerization would be involved in the folding of all molecules. Alternatively, if there is sufficient time available for the Xaa-Pro bonds of the nascent chains to reach a cis/trans equilibrium (e.g., when folding is transiently arrested by binding to other proteins, such as heat-shock protein (HSP70), then the distribution of prolyl cis and trans isomers prior to cellular folding could be similar to the distribution found in the unfolded protein in vitro. Such a case was encountered in the maturation... 

Galazka G, Stasiolek M, Walczak A, Jurewicz A, Zylicz A, Brosnan CF, Rtiine CS, Sehnaj KW (2006) Brain-derived heat shock protein 70-peptide complexes induce NK cell-dependent tolerance to experimental autoimmune encephalomyelitis. J Immunol 176 1588-1599 Galea E, Heneka MT, Russo CD, Feinstein DL (2003) Intrinsic regulations of biain infleunmatory responses. Cell Mol Neurobiol 23 625-635... 

Figure 12 TEM micrographs of Au nanoparticle synthesis mediated hy an HRE peptide integrated heat shock protein (Hsp 60) from Sulfolobus shibatae. (a) TEM of Au /(HRE)-Hsp complex prepared from addition of AuCLt , reduced hy citrate, and negatively stained hy uranyl acetate, (b) TEM of An /(HRE)-Hsp prepared from insoluble An precursor of AuClP(CH3)3 and reduced by borohydride (unstained)...

The members of the 70-kDa heat shock protein (hspVO) family perform functions that are essential for cell viability, both under normal and stress conditions. Constitutively expressed hsp70s are thought to be involved in the folding and assembly of newly synthesized proteins, disassembly of oligomeric proteins, protein degradation, and the transport of nascent peptide chains across membranes (l, 2). 

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