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Gene Review

HSPA8  -  heat shock 70kDa protein 8

Gallus gallus

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High impact information on HSPA8

  • Fourth, the proposed capping protein regulators, Hsc70 and S100, had no effect on capping protein binding to actin in vitro [1].
  • Modulation of the chaperone heat shock cognate 70 by embryonic (pro)insulin correlates with prevention of apoptosis [2].
  • Novobiocin interferes with association of the co-chaperones Hsc70 and p23 with Hsp90 [3].
  • Our results support the conclusion that hsc70 and hsp90 gene expression is regulated posttranscriptionally in TGF beta-treated CEC, and the mechanism likely involves a nuclear event such as increasing the half-lives of nuclear RNA transcripts, processing, or transport into the cytoplasm [4].
  • This cytokine did not increase rates of hsc70 and hsp90 gene transcription as measured by run-on transcription assays of isolated nuclei [4].

Biological context of HSPA8

  • This highly regulated expression of Hsc70 is likely to reflect specific developmental functions, besides its well-characterized role in protein folding [5].

Anatomical context of HSPA8

  • Herein, 32P-labeled cDNA probes encoding Hsc70 and Hsp90 were used to show that levels of the corresponding mRNAs increased as a fraction of total RNA and in polysomes within five hours of treatment of CEC with TGF beta [4].
  • On the other hand, retinal ganglion cells, differentiating in the opposite central-to-peripheral gradient, retained Hsc70 immunostaining [6].
  • The early widespread Hsc70 immunostaining corresponding to most, if not all, of the neuroepithelial cells becomes restricted to a subpopulation of these cells in the peripheral retina as development proceeds [6].
  • In stage 10 embryos, Hsc70 protein was expressed in the neural tube with increasing rostrocaudal and decreasing dorsoventral gradients, and in some somite cells [5].

Associations of HSPA8 with chemical compounds

  • Both Hsc70 and Hsp90 mRNAs had relatively short half-lives, measured by Northern blot analyses of dactinomycin chases, which were not altered substantially in TGF beta-treated cells [4].
  • Hsp90 is required for the normal function of steroid receptors, but its binding to steroid receptors is mediated by Hsc70 and several hsp-associated accessory proteins [7].

Other interactions of HSPA8

  • They also showed decreasing immunostaining patterns as neurogenesis proceeds, although distinctive from that of Hsc70, whereas Hsp70 was not detected in the embryonic retina [6].
  • Other molecular chaperones, the heat-shock proteins Hsp40, Hsp60 and Hsp90, did not seem to compensate the loss of Hsc70 [6].


  1. Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides. Schafer, D.A., Jennings, P.B., Cooper, J.A. J. Cell Biol. (1996) [Pubmed]
  2. Modulation of the chaperone heat shock cognate 70 by embryonic (pro)insulin correlates with prevention of apoptosis. de la Rosa, E.J., Vega-Núñez, E., Morales, A.V., Serna, J., Rubio, E., de Pablo, F. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  3. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. Marcu, M.G., Chadli, A., Bouhouche, I., Catelli, M., Neckers, L.M. J. Biol. Chem. (2000) [Pubmed]
  4. Regulation of chicken Hsp70 and Hsp90 family gene expression by transforming growth factor-beta 1. Takenaka, I.M., Hightower, L.E. J. Cell. Physiol. (1993) [Pubmed]
  5. Dynamic restricted expression of the chaperone Hsc70 in early chick development. Vega-Núñez, E., Peña-Melián, A., de la Rosa, E.J., de Pablo, F. Mech. Dev. (1999) [Pubmed]
  6. Heat shock proteins in retinal neurogenesis: identification of the PM1 antigen as the chick Hsc70 and its expression in comparison to that of other chaperones. Morales, A.V., Hadjiargyrou, M., Díaz, B., Hernández-Sánchez, C., de Pablo, F., de la Rosa, E.J. Eur. J. Neurosci. (1998) [Pubmed]
  7. Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants. Chen, S., Sullivan, W.P., Toft, D.O., Smith, D.F. Cell Stress Chaperones (1998) [Pubmed]
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