Share this post on:

Principle of protein-dye binding. Anal Biochem 72:248?54 Brown MA, Zhu L, Schmidt C, Tucker PW (2007) Hsp90 rom signal transduction to cell transformation. Biochem Biophys Res Commun 363:241?46 Byun S, Lee KW, Jung SK, Lee EJ, Hwang MK, Lim SH, Bode AM, Lee HJ, Dong Z (2010) Luteolin inhibits protein kinase C(epsilon) and c-Src activities and UVB-induced skin cancer. Cancer Res 70:2415?423 Cai J, Kirlin WG, Chen Y, Yan X, Jones DP, Sartorelli AC (2006) Overexpression of heat shock factor 1 inhibits butyrate-induced differentiation in colon cancer cells. Cell Stress Chaperones 11:199?07 Chen G, Gharib TG, Huang CC et al (2002) Discordant protein and mRNA expression in lung adenocarcinomas. Mol Cell Proteomics 1:304?13 Cho YM, Bae SH, Choi BK, Cho SY, Song CW, Yoo JK, Paik YK (2003) Differential expression of the liver proteome in senescence accelerated mice. Proteomics 3:1883?894 Christofk HR, Vander Heiden MG, Bayer 41-4109MedChemExpress Bay 41-4109 Harris MH, Ramanathan A, Gerszten RE, Wei R, Fleming MD, Schreiber SL, Cantley LC (2008a) The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature 452:230?233 Christofk HR, Vander Heiden MG, Wu N, Asara JM, Cantley LC (2008b) Pyruvate kinase M2 is a phosphotyrosine-binding protein. Nature 452:181?86 Decaux JF, Antoine B, Kahn A (1989) Regulation of the expression of the L-type pyruvate kinase gene in adult rat hepatocytes in primary culture. J Biol Chem 264:11584?1590 Diehl MC, Idowu MO, Kimmelshue K, York TP, Elmore LW, Holt SE (2009) Elevated expression of nuclear Hsp90 in invasive breast tumors. Cancer Biol Ther 8:1952?acetylated HSP90 increases in this process, previous investigations demonstrated no effect of butyrate on acetylation status and ATP binding of HSP90 (Bali et al. 2005). The missing alteration is due to the structure of the SCFA. Only hydroxamic acid derivates and seemingly phenolic components, like genistein, are able to inhibit HDAC6 activity, whereas butyrate is specifically blocking HDAC1 and 3 (Barlow et al. 2001; Marks and Xu 2009; Thangaraju et al. 2009). In a human tumor model of leukemia, a synergistic interaction has been observed by combining butyrate and the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (Rahmani et al. 2003). Looking at the individual data, some donors have been found with increased HSP90b levels in tumor tissue after butyrate treatment. Increased expression of HSPs or the transcriptional regulator heat shock factor 1, respectively, is associated with decreased sensitivity of tumor cells to chemopreventive drugs, such as butyrate (Cai et al. 2006) or curcumin (Rashmi et al. 2003), by protecting those from apoptosis or differentiation inducing mechanisms. To assess the meaning of this increase and its consequences for the application of chemopreventive drugs, kinetic studies will prospectively clarify, if this increase is of transient or persistent nature. In summary, PKM2 has been identified as a potential target of the chemopreventive agent butyrate in human colon tumors. Although HSP90b was not modified by the SCFA in malignant tissue in general, a group of patients was observed with increased levels of HSP90b after treatment. PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/27741243 Further studies should clarify which conditions permit this reaction and its duration, as well as find out more details about the post-transcriptional and translational machinery of PKM2.Acknowledgments The present study was supported by the German Research Foundation (DFG, PO 284/8-3). Additionally, we ar.

Share this post on:

Author: Proteasome inhibitor