Heat shock proteins and

Molecular chaperone (relative molecular mass 78 K) found in the lumen of the ER. BiP is related to the Hsp70 family of heat-shock proteins and was originally described as immunoglobulin heavy chain binding protein. 

Aguas, A., Esaguy, N., Sunkel, C.E., Silva, M.T. (1990). Cross-reactivity and sequence homology between the 65 kilodalton mycobacterial heat shock protein and human lactoferrin, transferrin, and DR beta subsets of major histocompatibility complex class II molecules. Infect. Immun. 58, 1461-1470. 

Chang, C.C., Konno, S., Wu, J.M. (1991). Enhanced expression of heat shock protein and mRNA synthesis by type I interferon in human HL-60 leukemic cells. Biochem Inti. 24, 369-377. 

McAlister, L. Finkelstein, D.B. (1980). Heat shock proteins and thermal resistance in yeast. Biochem. Biophys. Res. Commun. 93,819-824. 

Altschuler, M. Mascarenhas, J.P. (1982). Heat shock proteins and effects of heat shock in plants. Plant Molecular Biology, 1, 103-15. 

Guidon, P.T. Hightower, L.E. (1986). Purification and initial characterization of the 71-kilodalton rat heat-shock protein and its cognate as fatty acid binding proteins. Biochemistry, 25, 3231-9. 

Lin, C.Y., Roberts, J.K. Key, J.L. (1984). Acquisition of thermotolerance in soybean seedlings synthesis and accumulation of heat shock proteins and their cellular localization. Plant Physiology, 74,152-60. 

Major Heat Shock Proteins and Their Function... 

Pratt WB, Toft DO. (1997) Steroid receptor interactions with heat shock protein and immu-nophilin chaperones. Endocr Rev. 18, 306-360. 

Ballinger, C. A., P. Connell, Y. Wu, Z. Hu, L. J. Thompson, L. Y. Yin, and C. Patterson. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol. 19 4535-45.1999. 

Morrow, G. and Tanguay, R. M. (2003). Heat shock proteins and aging in Drosophila melano-gaster. Semin. Cell Dev. Biol. 14,291-299. 

Proteomics in parasitic flatworms can be completed on intracellular fractions (e.g. microsomal or cytosol) or at the host-interface on excretory-secretory (ES) products. ES analysis can be completed during in vitro culture or in vivo by, for example, bile or gut content analysis. In all cases, a rapid and careful preparation is vital to prevent altered pro-teomic profiles due to stress responses (upreg-ulation of heat shock proteins) and action of proteases. Parasitic flatworms are best extracted from fresh host material, washed with a buffered saline solution at approximately the host s body temperature. In F. hepatica, for example, this will allow regurgitation of gut contents to remove digested material from, and removal of host material adherent to the outer surfaces of the parasite (Jefferies et al., 2001), both of which can subsequently complicate separation and identification. 

Helm, K.W. Abernethy, R.H. (1990). Heat shock proteins and their mRNAs in dry and early imbibing embryos of wheat. Plant Physiology 93, 1626-33. 

Henry EC, Gasiewicz TA. 1993. Transformation of the aryl hydrocarbon receptor to a DNA-binding form is accompanied by release of the 90 kDA heat-shock protein and increased affinity for... 

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. 

Martin, J.L., Mestril, R., Hilal-Dandan, R., Brunton, L.L., and Dillmann, W.H. 1997. Small heat shock proteins and protection against ischemic injury in cardiac myocytes. Circulation 96 4343-4348. 

Feder, M. (1999). Organismal, ecological, and evolutionary aspects of heat-shock proteins and the stress response established conclusions and unresolved issues. Amer. Zool. 39 857-864. 

Physiological events which are the basis of gradual or sudden changes in product formation of a culture can be followed by analysing the biosynthetic components of the pathways involved, or of signal molecules. Examples include enzyme activities and molecules related to stress response, like heat shock proteins and other stress proteins. 

In summary, the KinaTor technology appears to be extremely potent for potentially revealing all binding partners of biologically active kinase inhibitors. Transmembrane domain proteins bind, as well as lipid kinases and other nucleotidebinding proteins, such as heat-shock proteins and oxidoreductases (unpublished data). So far, there are no limitations. 

Recently progress has been made in studying various aspects of one particular stress, i.e., the process by which plants protect themselves from heat. Under normal conditions, it has been found that plants produce enzymes required for normal cellular metabolism (Figure 23A). Figure 23B illustrates the situation when the plant senses an increase in temperature. New genes, called the "heat shock genes", are turned on, with the subsequent production of heat shock proteins and expression of normal metabolism genes is reduced. 

SecB is an acidic, soluble, tetramer of identical 17-kDa subunits. It comprises only 0.08% of the cytosolic proteins. The secB gene is conditionally essential in that secB null strains cannot grow on rich media or at subbasal levels of heat-shock protein synthesis, but can grow on minimal media. Overexpression of heat-shock proteins can partially suppress the export and growth defects in secB null strains. SecB is not a heat-shock protein, and ATP has no known effect on its function. 

Tolson, J.K., Roberts, S.M., Jortner, B., Pomeroy, M., Barber, D.S. (2005). Heat shock proteins and acquired resistance to uranium nephrotoxicity. Toxicology 206 59-73. 

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