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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
A central role for HSC70 in regulating antigen trafficking and MHC class II presentation.
Blum et al., Indianapolis, United States. In Mol Immunol, 31 Dec 2015
An abundant, constitutively expressed cytoplasmic chaperone, HSC70 plays a central role in modulating antigen transport within cells to control MHC class II presentation during nutrient stress.
UBXN2A regulates nicotinic receptor degradation by modulating the E3 ligase activity of CHIP.
De Biasi et al., Houston, United States. In Biochem Pharmacol, 15 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.
Opposing effects on two phases of defense responses from concerted actions of HSC70 and BON1 in Arabidopsis.
Hua et al., Ithaca, United States. In Plant Physiol, 25 Oct 2015
The heat shock protein HSC70, while previously known as a negative regulator of stomatal closure, is a positive regulator of immune responses mediated by the immune receptor protein SNC1 as well as basal defense responses.
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.
Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones.
Goloubinoff et al., Lausanne, Switzerland. In Front Mol Biosci, Dec 2014
The heat-inducible form HSP70 (HSPA1A) and its major cognates, cytosolic HSC70 (HSPA8), endoplasmic reticulum BIP (HSPA5), mitochondrial mHSP70 (HSPA9) and related HSP110s (HSPHs), contribute about 3% of the total protein mass of human cells.
Investigating Apoptozole as a Chemical Probe for HSP70 Inhibition.
Jones et al., London, United Kingdom. In Plos One, Dec 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, Dec 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.
HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.
Muller et al., Strasbourg, France. In Autophagy, 2013
HSPA8/HSC70 protein is a fascinating chaperone protein.
The critical roles of HSC70 in physiological and pathological processes.
Tang et al., Chongqing, China. In Curr Pharm Des, 2013
The heat stress cognate 70 is one of the major cytoplasmic chaperones to supply a multitude of the housekeeping chaperoning functions.
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.
Integrated pathways of parkin control over mitochondrial maintenance - relevance to Parkinson's disease pathogenesis.
Zekanowski et al., Warsaw, Poland. In Acta Neurobiol Exp (wars), 2012
We discuss possible underlying molecular mechanisms, exerted by parkin in cooperation with other mitochondrial maintenance factors such as TFAM, PGC-1alpha, mortalin, HSP70/HSC70 and LRPPRC, all of them implicated in PD pathogenesis.
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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