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].

References