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Heat shock 70kDa protein 8

This gene encodes a member of the heat shock protein 70 family, which contains both heat-inducible and constitutively expressed members. This protein belongs to the latter group, which are also referred to as heat-shock cognate proteins. It functions as a chaperone, and binds to nascent polypeptides to facilitate correct folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2011] (from NCBI)
Top mentioned proteins: HSP70, CAN, Hsp90, ACID, HAD
Papers using HSC70 antibodies
Protein aggregation containing beta-amyloid, alpha-synuclein and hyperphosphorylated tau in cultured cells of hippocampus, substantia nigra and locus coeruleus after rotenone exposure.
Cai Huaibin, In PLoS ONE, 2009
... MA]; anti-Beclin 1 CAT# NBP1-45382 from Novus Biologicals, LLC [Littleton, CO]; anti-beta Synuclein CAT# ab25650 and anti-Hsc70 [N27F34] CAT# ab90347 from Abcam PLC [Cambridge, MA]; and ...
Structural and functional consequences of c-N-Ras constitutively associated with intact mitochondria
Eng Charis et al., In Human Molecular Genetics, 2005
... Antibodies used were α-PTEN monoclonal antibody clone 6H2.1 (Cascade Biosciences, Portland, OR, USA), α-Hsc70, α-tubulin and PARP-1 (Cell Signaling Technologies, Danvers, MA, USA) ...
Expression of Fas ligand in arteries of hypercholesterolemic rabbits accelerates atherosclerotic lesion formation.
Rieux-Laucat Frederic, In PLoS ONE, 1999
... For Western blotting experiments, anti-GAPDH, anti-PI3K, anti-HSC70 were obtained from Santa Cruz Biotechnology (CA, USA), anti-phospho-Akt from ...
Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: implications for intercellular signaling
Katsoris Panagiotis et al., In Molecular Cancer, 1997
... Polyclonal antibodies against HSC70 were purchased from Santa Cruz Biotechnology, Inc ...
Papers on HSC70
Salivary protein histatin 3 regulates cell proliferation by enhancing p27(Kip1) and heat shock cognate protein 70 ubiquitination.
Sogawa et al., Shiojiri, Japan. In Biochem Biophys Res Commun, 14 Feb 2016
We previously reported that histatin 3 binds to heat shock cognate protein 70 (HSC70), which is constitutively expressed, and induces DNA synthesis stimulation and promotes human gingival fibroblast (HGF) survival.
Deacetylation of tumor-suppressor MST1 in Hippo pathway induces its degradation through HBXIP-elevated HDAC6 in promotion of breast cancer growth.
Ye et al., Tianjin, China. In Oncogene, 14 Jan 2016
Deacetylation of MST1 promoted the interaction of MST1 with HSC70 in the cells, resulting in a lysosome-dependent degradation of MST1 via chaperone-mediated autophagy (CMA).
Structural studies of UBXN2A and mortalin interaction and the putative role of silenced UBXN2A in preventing response to chemotherapy.
Rezvani et al., United States. In Cell Stress Chaperones, 04 Jan 2016
As revealed by chase experiments in the presence of cycloheximide, overexpression of UBXN2A seems to interfere with the mortalin-CHIP E3 ubiquitin ligase and consequently suppresses the C-terminus of the HSC70-interacting protein (CHIP)-mediated destabilization of p53, resulting in its stabilization in the cytoplasm and upregulation in the nucleus.
Opposing Effects on Two Phases of Defense Responses from Concerted Actions of HEAT SHOCK COGNATE70 and BONZAI1 in Arabidopsis.
Hua et al., Ürümqi, China. In Plant Physiol, Nov 2015
The HEAT SHOCK COGNATE70 (HSC70), while previously known as a negative regulator of stomatal closure, is a positive regulator of immune responses mediated by the immune receptor protein SUPPRESSOR OF NPR1-1, CONSTITUTIVE1 (SNC1) as well as basal defense responses.
UBXN2A regulates nicotinic receptor degradation by modulating the E3 ligase activity of CHIP.
De Biasi et al., Houston, United States. In Biochem Pharmacol, Nov 2015
UBXN2A also cross-talks with VCP/p97 and HSC70/HSP70 proteins in a complex where α3 is likely to be targeted by CHIP.
Heat stress induces formation of cytoplasmic granules containing HSC70 protein.
Razin et al., Moscow, Russia. In Dokl Biochem Biophys, Jul 2015
Using indirect immunofluorescence, in this study we showed that the constitutive heat shock protein HSC70 forms granule-like structures in the cytoplasm of human cells several days after the exposure to heat stress.
Quantitative analysis of the interplay between hsc70 and its co-chaperone HspBP1.
Stochaj et al., Montréal, Canada. In Peerj, 2014
In particular, hsp70 family members and their co-chaperones are essential to repair damaged proteins.
Low Dose Administration of Glutamate Triggers a Non-Apoptotic, Autophagic Response in PC12 Cells.
Kritis et al., In Cell Physiol Biochem, 2014
RESULTS: Administration of glutamate in PC12 cells in doses as low as 10 μM causes an up-regulation of GRP78, GRP94 and HSC70 protein levels, while their mRNA levels show the opposite kinetics.
Investigating Apoptozole as a Chemical Probe for HSP70 Inhibition.
Jones et al., London, United Kingdom. In Plos One, 2014
Apoptozole is a recently identified small molecule, which has been reported to possess strong affinity for the HSP70 isoforms HSP72 and HSC70.
Ecdysone-Related Biomarkers of Toxicity in the Model Organism Chironomus riparius: Stage and Sex-Dependent Variations in Gene Expression Profiles.
Servia et al., Madrid, Spain. In Plos One, 2014
Real-Time PCR was used to analyze: EcR and usp, two genes encoding the two dimerizing partners of the functional ecdysone receptor; E74, an early response gene induced by ecdysteroids; vg (vitellogenin), an effector gene; hsp70 and hsc70, two heat-shock genes involved in the correct folding of the ecdysone receptor; and rpL13, as a part of the ribosomal machinery.
Lysine-5 acetylation negatively regulates lactate dehydrogenase A and is decreased in pancreatic cancer.
Guan et al., Shanghai, China. In Cancer Cell, 2013
Furthermore, the K5-acetylated LDH-A is recognized by the HSC70 chaperone and delivered to lysosomes for degradation.
Matrine modulates HSC70 levels and rescues ΔF508-CFTR.
Mazzei et al., Salerno, Italy. In J Cell Physiol, 2012
downregulation of HSC70 resulted in increased levels of DeltaF508-CFTR complexes with the co-chaperone BAG3 that in addition appeared to co-localize with the mutated protein on the cell surface.
Heat shock cognate 70 regulates the translocation and angiogenic function of nucleolin.
Luo et al., Beijing, China. In Arterioscler Thromb Vasc Biol, 2012
Hsc70 is a prerequisite for the surface translocation and angiogenic function of nucleolin, which suggests strategies to target both Hsc70 and NCL for more effective antiangiogenic therapies.
The cellular chaperone hsc70 is specifically recruited to reovirus viral factories independently of its chaperone function.
Parker et al., Ithaca, United States. In J Virol, 2012
Hsc70 is recruited to reovirus viral factories independently of its chaperone function.
A small molecule that binds to an ATPase domain of Hsc70 promotes membrane trafficking of mutant cystic fibrosis transmembrane conductance regulator.
Shin et al., Seoul, South Korea. In J Am Chem Soc, 2012
It is proposed that Az suppresses ubiquitination of DeltaF508-CFTR maybe by blocking interaction of the mutant with Hsc70 and CHIP, and, as a consequence, it enhances membrane trafficking of the mutant
Heat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport.
Binder et al., Chicago, United States. In Biochemistry, 2011
Addition of Hsp70 to a mixture of oligomeric and fibrillar tau aggregates prevents the toxic effect of these tau species on fast axonal transport.
Molecular mechanism and physiological functions of clathrin-mediated endocytosis.
Boucrot et al., Cambridge, United Kingdom. In Nat Rev Mol Cell Biol, 2011
The process involves the formation of a putative FCH domain only (FCHO) initiation complex, which matures through adaptor protein 2 (AP2)-dependent cargo selection, and subsequent coat building, dynamin-mediated scission and finally auxilin- and heat shock cognate 70 (HSC70)-dependent uncoating.
Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein.
Nukina et al., Wako, Japan. In Nat Biotechnol, 2010
As the polyglutamine binding peptide 1 (QBP1) is known to bind an expanded polyQ tract but not the polyQ motif found in normal HTT, we selectively targeted mutant HTT for degradation by expressing a fusion molecule comprising two copies of QBP1 and copies of two different heat shock cognate protein 70 (HSC70)-binding motifs in cellular and mouse models of HD.
Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis.
Workman et al., United Kingdom. In Cancer Cell, 2008
Simultaneously reducing the expression of both HSC70 and HSP72 induces proteasome-dependent degradation of HSP90 client proteins, G1 cell-cycle arrest, and extensive tumor-specific apoptosis in human tumor cell lines.
Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens.
Blum et al., Indianapolis, United States. In Immunity, 2005
Manipulating APC expression of heat shock cognate protein 70 (hsc70), a cofactor for Lamp-2a, also altered cytoplasmic class II peptide presentation.
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