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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

HSP27  -  heat shock 27kDa protein 1

Sus scrofa

 
 
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Disease relevance of Hsp27

  • The effects of hypoxia on the neonatal brain were characterized through a time-course analysis of levels of various proteins such as heat shock proteins (HSP27, 70, and 90), hypoxia inducible factor-1alpha (HIF-1alpha), neuronal nitric oxide synthase (nNOS), hemeoxygenase-2 (HO-2), and caspase-3 [1].
  • Immunohistochemically, HSP27 immunostaining was seen mainly in ganglion cell bodies in the ganglion cell layer, and in some processes of astrocytes in the innermost nerve fiber layer [2].
 

High impact information on Hsp27

 

Chemical compound and disease context of Hsp27

  • After western blotting, alphaB crystallin, HSP 27, and HSP 70 expressions were determined in newborn controls and piglets exposed to 1 or 4 h hypoxia (5% O2, 95% N2) allowed to recover from 1 to 68 h [5].
 

Biological context of Hsp27

  • This observation dissociates the response to low oxygenation of alphaB-crystallin and other stress-associated proteins including Hsp27, and it indicates that heme oxygenase is not alone among HSPs in its oxygen-related gene expression [6].
  • Overexpression of a phosphorylation-defective mutant Hsp27 acted as a dominant negative and accelerated the DCVC-induced changes in the focal adhesions as well as the onset of apoptosis [4].
  • In summary, this finding suggests that HSP27 plays an important role in signal transduction of glial cells and neuronal cells in the retina [2].
  • Muscles leading to darker meat had a more oxidative metabolism, indicated by more abundant mitochondrial enzymes of the respiratory chain, hemoglobin, and chaperone or regulator proteins (HSP27, alphaB-crystallin, and glucose-regulated protein 58 kDa) [7].
  • The HSC70 and HSP27 both belong to the heat shock family and are known to play a role during muscle development [8].
 

Anatomical context of Hsp27

  • FPI increased the cerebrospinal fluid (CSF) concentration of HSP-27 from 0.051 +/- 0.012 to 0.113 +/- 0.035 ng/ml but decreased the CSF concentration of HSP-70 from 50.42 +/- 8.96 to 30.9 +/- 9.9 ng/ml at 1 h postinsult [9].
  • Phosphorylated Hsp27 was excluded from the leading edge and restricted to the base of the lamellipodia [10].
  • Control of actin dynamics by p38 MAP kinase - Hsp27 distribution in the lamellipodium of smooth muscle cells [10].
  • Our data indicate that nonphosphorylated Hsp27 might contribute to the formation of a short, branched actin network at the leading edge, whereas phosphorylated Hsp27 might stabilize the actin network at the base of lamellipodia, which is composed of long, unbranched actin filaments [10].
  • We studied expression of these proteins in porcine lens, brain, heart, liver, kidney, lung, skeletal muscle, stomach, and colon, and found a ubiquitous expression of Hsp20 and HspB8 as earlier reported for Hsp27 and alphaB-crystallin [11].
 

Associations of Hsp27 with chemical compounds

  • A potential role for Hsp27 in the cellular response to sublethal cadmium-induced injury is also implicated by our results [12].
  • Under nonbrain injury conditions, topical coadministration of exogenous HSP-27 (1 mug/ml) blunted dilation to cromakalim, CGRP, and NS-1619 (10(-8) and 10(-6) M; cromakalim and CGRP are K(ATP) agonists and NS-1619 is a K(Ca) agonist) [9].
  • The most prominent changes were found for Hsp27, which was related to a pI shift in association with an altered phosphorylation status of serine residue 82 [4].
 

Other interactions of Hsp27

  • Strong transcriptional activity was found for the ubiquitin and heat shock protein (hsp27, hsp70) genes, and for PAI-1 and GAPDH [13].
  • To investigate the mechanism of action of p38 MAPK, we explored its cellular localization and that of its indirect substrate, the heat shock protein Hsp27, during SMC spreading on fibronectin in the presence and absence of PDGF [10].
  • The protein levels of myoglobin, myosin light chain and HSP20 were higher in red muscle, whereas HSP27 was higher in white muscle [14].
 

Analytical, diagnostic and therapeutic context of Hsp27

  • The relative levels of alphaB-crystallin, HspB8, Hsp20, Hsp27, Hsp60, and Hsp70 as well as nitric oxide synthases (NOS) (endothelial NOS, inducible NOS, neuronal NOS) were examined by Western blot analysis [6].
  • Transcription of the Ub and hsp27 genes was increased during 30 and 120 min of the second reperfusion period [15].
  • Using northern blot hybridizations, several mRNAs encoding Ub, 0.9 kb mRNA encoding hsp27, and 2.2 kb mRNA encoding hsp60 were detected in sham operated, non-ischaemic, and ischaemic myocardial tissues [15].
  • The activation of these kinase cascades was also determined by resolving lysates on Mono Q using a fast protein liquid chromatography (FPLC) system and measuring the phosphorylation of specific substrates ERK1, c-Jun, and hsp27 [16].

References

  1. Effects of hypoxia on stress proteins in the piglet brain at birth. Chiral, M., Grongnet, J.F., Plumier, J.C., David, J.C. Pediatr. Res. (2004) [Pubmed]
  2. Immunohistochemical localization of heat shock protein 27 in the retina of pigs. Lee, J., Kim, H., Lee, J.M., Shin, T. Neurosci. Lett. (2006) [Pubmed]
  3. Drug-induced heat-shock preconditioning improves postischemic ventricular recovery after cardiopulmonary bypass. Maulik, N., Engelman, R.M., Wei, Z., Liu, X., Rousou, J.A., Flack, J.E., Deaton, D.W., Das, D.K. Circulation (1995) [Pubmed]
  4. Heat shock protein 27 is the major differentially phosphorylated protein involved in renal epithelial cellular stress response and controls focal adhesion organization and apoptosis. de Graauw, M., Tijdens, I., Cramer, R., Corless, S., Timms, J.F., van de Water, B. J. Biol. Chem. (2005) [Pubmed]
  5. Overexpression of alphaB crystallin in the gastrointestinal tract of the newborn piglet after hypoxia. Nefti, O., Grongnet, J.F., David, J.C. Shock (2005) [Pubmed]
  6. Effects of hypoxia on stress proteins in the piglet heart at birth. Louapre, P., Grongnet, J.F., Tanguay, R.M., David, J.C. Cell Stress Chaperones (2005) [Pubmed]
  7. Proteome analysis of the sarcoplasmic fraction of pig semimembranosus muscle: implications on meat color development. Sayd, T., Morzel, M., Chambon, C., Franck, M., Figwer, P., Larzul, C., Le Roy, P., Monin, G., Chérel, P., Laville, E. J. Agric. Food Chem. (2006) [Pubmed]
  8. Changes in the muscle proteome after compensatory growth in pigs. Lametsch, R., Kristensen, L., Larsen, M.R., Therkildsen, M., Oksbjerg, N., Ertbjerg, P. J. Anim. Sci. (2006) [Pubmed]
  9. Heat shock protein modulation of KATP and KCa channel cerebrovasodilation after brain injury. Armstead, W.M., Hecker, J.G. Am. J. Physiol. Heart Circ. Physiol. (2005) [Pubmed]
  10. Control of actin dynamics by p38 MAP kinase - Hsp27 distribution in the lamellipodium of smooth muscle cells. Pichon, S., Bryckaert, M., Berrou, E. J. Cell. Sci. (2004) [Pubmed]
  11. Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig. Verschuure, P., Tatard, C., Boelens, W.C., Grongnet, J.F., David, J.C. Eur. J. Cell Biol. (2003) [Pubmed]
  12. Hsp27, Hsp70, and metallothionein in MDCK and LLC-PK1 renal epithelial cells: effects of prolonged exposure to cadmium. Bonham, R.T., Fine, M.R., Pollock, F.M., Shelden, E.A. Toxicol. Appl. Pharmacol. (2003) [Pubmed]
  13. Changes in gene expression following short coronary occlusions studied in porcine hearts with run-on assays. Knöll, R., Arras, M., Zimmermann, R., Schaper, J., Schaper, W. Cardiovasc. Res. (1994) [Pubmed]
  14. Differential expression profiling of the proteomes and their mRNAs in porcine white and red skeletal muscles. Kim, N.K., Joh, J.H., Park, H.R., Kim, O.H., Park, B.Y., Lee, C.S. Proteomics (2004) [Pubmed]
  15. Expression of heat shock proteins in the normal and stunned porcine myocardium. Andres, J., Sharma, H.S., Knöll, R., Stahl, J., Sassen, L.M., Verdouw, P.D., Schaper, W. Cardiovasc. Res. (1993) [Pubmed]
  16. Simultaneous measurement of ERK, p38, and JNK MAP kinase cascades in vascular smooth muscle cells. Chevalier, D., Thorin, E., Allen, B.G. Journal of pharmacological and toxicological methods. (2000) [Pubmed]
 
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