Disease relevance of hsc70

• Given these results, we examined the effect of hyperthermia in vivo on the expression of five hsp genes (hsp70, hsc70, BiP, hsp90, and hsp30) in eye tissue [1].

High impact information on hsc70

• We have previously shown that the mouse U14 snRNA genes are positioned within introns 5, 6, and 8 on the coding strand of the constitutively expressed cognate hsc70 heat shock gene [2].
• Nuclear uptake studies were performed by microinjecting 125I-labeled B3/B4, rat hsc70, and BSA into the cytoplasm of oocytes, and examining their subsequent intracellular distributions [3].
• Collectively, these results show that B3, B4, and rat hsc70 are transported across the nuclear envelope and recycle between the nucleus and cytoplasm [3].
• Evidence based on high-affinity binding to ATP, cross-reactivity of B3/B4-specific antibodies with rat hsc70, and a comparison of cyanogen bromide cleavage peptide maps with hsc70, verified that B3 and B4 are members of the 70-kD family of heat-shock proteins [3].
• Although a subset of the hsp70/68 complex is expressed constitutively in the absence of heat shock in oocytes and embryos (hsc70), actual induction of hsps in response to stress does not occur until the blastula stage when transcription of the zygotic genome is first activated [4].

Biological context of hsc70

• We isolated a full-length cDNA clone encoding a Xenopus laevis 70-kDa heat shock cognate protein, hsc70.I. The protein coding region exhibits a high degree of identity with a number of mammalian hsc70 proteins, such as rat hsc71 (92%), whereas the identity to Xenopus hsp70 is only 80% [5].
• The effect of carboxyl-terminal deletions on the nuclear transport rate of rat hsc70 [6].
• Purified rat hsc70, and hybrid proteins, which contained either the full-length or the mutated forms of rat hsc70 fused with the maltose binding protein, were labeled with 125I and used as transport substrates [7].
• Our results show that specific inactivation of hsc70 mRNA by hsc70 antisense oligos led to a reversible inhibition of lampbrush chromosome transcription [8].

Associations of hsc70 with chemical compounds

• In one, nitrocellulose-bound proteins were incubated with hsc70, cross-linked with glutaraldehyde, and then bound hsc70 was probed with a monoclonal anti-hsc70 antibody [9].

Other interactions of hsc70

• We determined the identifies of six Ran-interacting proteins (Rips), and found that they include RanBP2/Nup358, Nup153, Importin beta, hsc70, RCC1, and RanBP1 [10].
• Characterization of Xenopus laevis U14 snoRNA genes has revealed that in addition to the anticipated location of U14 within introns of the amphibian hsc70 gene (introns 4, 5 and 7), additional intronic U14 snoRNAs are also found in the ribosomal protein S13 gene (introns 3 and 4) [11].

Analytical, diagnostic and therapeutic context of hsc70

• Microinjection of hsc70 pre-mRNAs into developing oocytes demonstrated that oocytes as early as stages II and III are capable of processing U14 snoRNA from the pre-mRNA precursor [11].
• In this study, we have employed whole-mount, in situ hybridization to study the spatial pattern of hsc70 and hsp70 mRNA accumulation in normal and heat shocked embryos during Xenopus laevis development [12].

References