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HSPB2  -  heat shock 27kDa protein 2

Homo sapiens

Synonyms: DMPK-binding protein, HSP27, Heat shock protein beta-2, Hs.78846, HspB2, ...
 
 
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Disease relevance of HSPB2

 

Psychiatry related information on HSPB2

 

High impact information on HSPB2

  • Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27 [6].
  • An upstream activator kinase phosphorylated a 40 kDa kinase (p40) upon threonine and tyrosine residues, which in turn phosphorylated a 50 kDa kinase (p50) upon threonine (and some serine) residues. p50 phosphorylated hsp27 upon serine. p40 and p50 were purified to near homogeneity [6].
  • An IL-1-stimulated protein kinase cascade resulting in phosphorylation of the small heat shock protein hsp27 has been identified in KB cells [6].
  • These results therefore demonstrate that Hsp27 is a heat-induced inhibitor of eIF4F-dependent mRNA translation [7].
  • Hsp27 negatively regulates cell death by interacting with cytochrome c [8].
 

Chemical compound and disease context of HSPB2

 

Biological context of HSPB2

  • The expression of HSPB2 protected the cells from heat-induced cell death [14].
  • HSP27 does not affect I-kappaBalpha phosphorylation but enhances the degradation of phosphorylated I-kappaBalpha by the proteasome [15].
  • Hsp27 plays a crucial role in the inhibition of apoptosis of oral SCC cells [1].
  • Conversely, cells expressing a dominant-negative mutant of Hsp27, in which three serine residues (15, 78 and 82) were replaced by glycine, were hypersensitive to the effects of IFN-gamma and exhibited a typical apoptotic phenotype [1].
  • Heat shock protein 27 (Hsp27) is a ubiquitously expressed member of the heat shock protein family that has been implicated in various biological functions including the response to heat shock, oxidative stress, and cytokine treatment [16].
 

Anatomical context of HSPB2

  • Association of HSPB2, a member of the small heat shock protein family, with mitochondria [14].
  • We previously identified HSPB2, a new member of the small heat shock protein family, expressed in heart and skeletal muscles [14].
  • Double staining with anti-HSPB2 and various markers for cytoplasmic structures showed that HSPB2 was present in the cytosol as granules, some of which colocalized with mitochondria [14].
  • These results suggest that MKBP constitutes a novel stress-responsive system independent of other known sHSPs in muscle cells and that DMPK may be involved in this system by being activated by MKBP [17].
  • LY294002 suppressed the heat-induced accumulation of heat shock protein 27 (hsp27) and heat shock protein 72 (hsp72) in these cell lines [18].
 

Associations of HSPB2 with chemical compounds

  • Induction of HSP27 nuclear immunoreactivity during stress is modulated by vitamin C [19].
  • These results suggest that LY294002 inhibits anti-apoptosis signaling through hsp27 and hsp72 as well as cell survival signaling through Akt and survivin [18].
  • Recently, we have identified that 27-kDa heat shock protein (HSP27) can serve as a sensitive marker of skin irritation, as exposure of human skin to sodium lauryl sulfate (SLS) both in vitro and in vivo induced relocalization of HSP27 from the cytoplasm to the cell nucleus [19].
  • HSP27 and alphaB-crystallin accumulated in both soluble and, more prominently, insoluble fractions after exposure to MG-132, a proteasome inhibitor [20].
  • Here we show that continued treatment of MM cells with bortezomib leads to a SCIO-469-enhanced downregulation of Hsp27 and to increased MM apoptosis [21].
 

Regulatory relationships of HSPB2

 

Other interactions of HSPB2

 

Analytical, diagnostic and therapeutic context of HSPB2

  • In addition, Northern blot analysis revealed that expression of HSPB2 mRNA is higher in slow-twitch muscle than in fast-twitch muscle, which correlates with the amounts of mitochondria present in these two types of tissue [14].
  • Most interestingly, from 2D gel electrophoresis analysis, we identified that the expression of heat shock protein 27 (HSP27), known as a suppressor of poly(Q)-mediated cell death, dramatically decreased in SK-N-SH cells stably transfected with full-length mutant MJD [27].
  • Western blotting analyses showed that MKBP level in rat heart rapidly increased, with a sharp peak at one week after birth (3-fold the level at the fetus), but that it rapidly decreased (1/10 of peak value at 13 weeks) [25].
  • Immunofluorescence analysis revealed that exposure to proteasome inhibitors induced the formation of aggresomes in U373 MG cells, to which HSP27 and alphaB-crystallin were recruited [20].
  • We describe a Western blot study measuring hsp27 levels in 425 patients and an immunohistochemistry (IHC) study analyzing 788 patients [28].

References

  1. Interferon-gamma downregulates Hsp27 expression and suppresses the negative regulation of cell death in oral squamous cell carcinoma lines. Yonekura, N., Yokota, S., Yonekura, K., Dehari, H., Arata, S., Kohama, G., Fujii, N. Cell Death Differ. (2003) [Pubmed]
  2. Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival. Shimura, H., Miura-Shimura, Y., Kosik, K.S. J. Biol. Chem. (2004) [Pubmed]
  3. Ischemia-induced increase of stiffness of alphaB-crystallin/HSPB2-deficient myocardium. Golenhofen, N., Redel, A., Wawrousek, E.F., Drenckhahn, D. Pflugers Arch. (2006) [Pubmed]
  4. Overexpression and abnormal modification of the stress proteins alpha B-crystallin and HSP27 in Alexander disease. Head, M.W., Corbin, E., Goldman, J.E. Am. J. Pathol. (1993) [Pubmed]
  5. Dementia, gliosis and expression of the small heat shock proteins hsp27 and alpha B-crystallin in Parkinson's disease. Renkawek, K., Stege, G.J., Bosman, G.J. Neuroreport (1999) [Pubmed]
  6. Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27. Freshney, N.W., Rawlinson, L., Guesdon, F., Jones, E., Cowley, S., Hsuan, J., Saklatvala, J. Cell (1994) [Pubmed]
  7. Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Cuesta, R., Laroia, G., Schneider, R.J. Genes Dev. (2000) [Pubmed]
  8. Hsp27 negatively regulates cell death by interacting with cytochrome c. Bruey, J.M., Ducasse, C., Bonniaud, P., Ravagnan, L., Susin, S.A., Diaz-Latoud, C., Gurbuxani, S., Arrigo, A.P., Kroemer, G., Solary, E., Garrido, C. Nat. Cell Biol. (2000) [Pubmed]
  9. Hsp27 overexpression inhibits doxorubicin-induced apoptosis in human breast cancer cells. Hansen, R.K., Parra, I., Lemieux, P., Oesterreich, S., Hilsenbeck, S.G., Fuqua, S.A. Breast Cancer Res. Treat. (1999) [Pubmed]
  10. Change in the localization of heat shock protein 27 (HSP 27) in BG-1 human ovarian cancer cells following treatment by the ether lipid ET-18-OCH3. Fujiwara, K., Shirafuji, H., Fushitani, K., Fujimoto, K., Kohno, I., Modest, E.J. Anticancer Res. (1999) [Pubmed]
  11. Hsp27 expression in neuroblastoma: correlation with disease stage. Ungar, D.R., Hailat, N., Strahler, J.R., Kuick, R.D., Brodeur, G.M., Seeger, R.C., Reynolds, C.P., Hanash, S.M. J. Natl. Cancer Inst. (1994) [Pubmed]
  12. Estrogen receptors, progesterone receptors and heat-shock 27-kD protein in liver biopsy specimens from patients with hepatitis B virus infection. Ciocca, D.R., Jorge, A.D., Jorge, O., Milutín, C., Hosokawa, R., Díaz Lestren, M., Muzzio, E., Schulkin, S., Schirbu, R. Hepatology (1991) [Pubmed]
  13. Blockade of Hsp27 overcomes Bortezomib/proteasome inhibitor PS-341 resistance in lymphoma cells. Chauhan, D., Li, G., Shringarpure, R., Podar, K., Ohtake, Y., Hideshima, T., Anderson, K.C. Cancer Res. (2003) [Pubmed]
  14. Association of HSPB2, a member of the small heat shock protein family, with mitochondria. Nakagawa, M., Tsujimoto, N., Nakagawa, H., Iwaki, T., Fukumaki, Y., Iwaki, A. Exp. Cell Res. (2001) [Pubmed]
  15. HSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradation. Parcellier, A., Schmitt, E., Gurbuxani, S., Seigneurin-Berny, D., Pance, A., Chantôme, A., Plenchette, S., Khochbin, S., Solary, E., Garrido, C. Mol. Cell. Biol. (2003) [Pubmed]
  16. Heat shock protein 27 association with the I kappa B kinase complex regulates tumor necrosis factor alpha-induced NF-kappa B activation. Park, K.J., Gaynor, R.B., Kwak, Y.T. J. Biol. Chem. (2003) [Pubmed]
  17. MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase. Suzuki, A., Sugiyama, Y., Hayashi, Y., Nyu-i, N., Yoshida, M., Nonaka, I., Ishiura, S., Arahata, K., Ohno, S. J. Cell Biol. (1998) [Pubmed]
  18. LY294002, an inhibitor of PI-3K, enhances heat sensitivity independently of p53 status in human lung cancer cells. Ohnishi, K., Yasumoto, J., Takahashi, A., Ohnishi, T. Int. J. Oncol. (2006) [Pubmed]
  19. Induction of HSP27 nuclear immunoreactivity during stress is modulated by vitamin C. Boxman, I.L., Kempenaar, J., de Haas, E., Ponec, M. Exp. Dermatol. (2002) [Pubmed]
  20. Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-crystallin to aggresomes. Ito, H., Kamei, K., Iwamoto, I., Inaguma, Y., García-Mata, R., Sztul, E., Kato, K. J. Biochem. (2002) [Pubmed]
  21. Inhibition of p38alpha MAPK enhances proteasome inhibitor-induced apoptosis of myeloma cells by modulating Hsp27, Bcl-X(L), Mcl-1 and p53 levels in vitro and inhibits tumor growth in vivo. Navas, T.A., Nguyen, A.N., Hideshima, T., Reddy, M., Ma, J.Y., Haghnazari, E., Henson, M., Stebbins, E.G., Kerr, I., O'Young, G., Kapoun, A.M., Chakravarty, S., Mavunkel, B., Perumattam, J., Luedtke, G., Dugar, S., Medicherla, S., Protter, A.A., Schreiner, G.F., Anderson, K.C., Higgins, L.S. Leukemia (2006) [Pubmed]
  22. p38 MAP kinase mediates platelet-derived growth factor-stimulated migration of hepatic myofibroblasts. Tangkijvanich, P., Santiskulvong, C., Melton, A.C., Rozengurt, E., Yee, H.F. J. Cell. Physiol. (2002) [Pubmed]
  23. Phosphorylated HSP27 modulates the association of phosphorylated caldesmon with tropomyosin in colonic smooth muscle. Somara, S., Bitar, K.N. Am. J. Physiol. Gastrointest. Liver Physiol. (2006) [Pubmed]
  24. Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation. Sugiyama, Y., Suzuki, A., Kishikawa, M., Akutsu, R., Hirose, T., Waye, M.M., Tsui, S.K., Yoshida, S., Ohno, S. J. Biol. Chem. (2000) [Pubmed]
  25. Transient up-regulation of myotonic dystrophy protein kinase-binding protein, MKBP, and HSP27 in the neonatal myocardium. Shama, K.M., Suzuki, A., Harada, K., Fujitani, N., Kimura, H., Ohno, S., Yoshida, K. Cell Struct. Funct. (1999) [Pubmed]
  26. Interleukin 1-induced phosphorylation of MAD3, the major inhibitor of nuclear factor kappa B of HeLa cells. Interference in signalling by the proteinase inhibitors 3,4-dichloroisocoumarin and tosylphenylalanyl chloromethylketone. Guesdon, F., Ikebe, T., Stylianou, E., Warwick-Davies, J., Haskill, S., Saklatvala, J. Biochem. J. (1995) [Pubmed]
  27. Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3. Wen, F.C., Li, Y.H., Tsai, H.F., Lin, C.H., Li, C., Liu, C.S., Lii, C.K., Nukina, N., Hsieh, M. FEBS Lett. (2003) [Pubmed]
  28. The small heat shock protein HSP27 is not an independent prognostic marker in axillary lymph node-negative breast cancer patients. Oesterreich, S., Hilsenbeck, S.G., Ciocca, D.R., Allred, D.C., Clark, G.M., Chamness, G.C., Osborne, C.K., Fuqua, S.A. Clin. Cancer Res. (1996) [Pubmed]
 
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