ArticleThe Journal of biological chemistry2014
Heat shock protein 70.1 (Hsp70.1) affects neuronal cell fate by regulating lysosomal acid sphingomyelinase.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 40 citations in OpenAlex.
- Lipid-gated vesicular trafficking directs HSPA1A to the plasma membrane through the endo-lysosomal network.Cell stress & chaperones · 2026Article
- Preformed fibrils of α-synuclein rapidly activate LRRK2 on early endosomes, driving Rab5 phosphorylation and disrupting endolysosomal and synaptic function.NPJ Parkinson's disease · 2026Article
- Review
- Different concentrations of 2-Undecanone triggers repellent and nematicidal responses in Caenorhabditis elegans.Scientific reports · 2025Article
- Ion Channel Dysregulation Following Intracerebral Hemorrhage.Neuroscience bulletin · 2024Review
- RIPK1 inhibition contributes to lysosomal membrane stabilization in ischemic astrocytes via a lysosomal Hsp70.1B-dependent mechanism.Acta pharmacologica Sinica · 2023Article
- Nutri-stress, mitochondrial dysfunction, and insulin resistance-role of heat shock proteins.Cell stress & chaperones · 2023Review
- High PPT1 expression predicts poor clinical outcome and PPT1 inhibitor DC661 enhances sorafenib sensitivity in hepatocellular carcinoma.Cancer cell international · 2022Article
- Hsp70.1 carbonylation induces lysosomal cell death for lifestyle-related diseases.Frontiers in molecular biosciences · 2022Review
- Hydroxynonenal Causes Hepatocyte Death by Disrupting Lysosomal Integrity in Nonalcoholic Steatohepatitis.Cellular and molecular gastroenterology and hepatology · 2022Article
- Intake of ω-6 Polyunsaturated Fatty Acid-Rich Vegetable Oils and Risk of Lifestyle Diseases.Advances in nutrition (Bethesda, Md.) · 2020Review
- The dynamics and role of sphingolipids in eukaryotic organisms upon thermal adaptation.Progress in lipid research · 2020Review
- The role of lysosome in regulated necrosis.Acta pharmaceutica Sinica. B · 2020Review
- Lysosomal dysfunction-induced autophagic stress in diabetic kidney disease.Journal of cellular and molecular medicine · 2020Review
- Cathepsin B in neurodegeneration of Alzheimer's disease, traumatic brain injury, and related brain disorders.Biochimica et biophysica acta. Proteins and proteomics · 2020Review
- Lipid-Binding Proteins in Brain Health and Disease.Frontiers in neurology · 2019Review
- The heat shock protein amplifier arimoclomol improves refolding, maturation and lysosomal activity of glucocerebrosidase.EBioMedicine · 2018Article
- P2X7 Receptor-Associated Programmed Cell Death in the Pathophysiology of Hemorrhagic Stroke.Current neuropharmacology · 2018Review
- Article
- Heat shock protein-based therapy as a potential candidate for treating the sphingolipidoses.Science translational medicine · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The inducible expression of heat shock protein 70.1 (Hsp70.1) plays cytoprotective roles in its molecular chaperone function. Binding of Hsp70 to an endolysosomal phospholipid, bis(monoacylglycero)phosphate (BMP), has been recently shown to stabilize lysosomal membranes by enhancing acid sphingomyelinase (ASM) activity in cancer cells. Using the monkey experimental paradigm, we have reported that calpain-mediated cleavage of oxidized Hsp70.1 causes neurodegeneration in the hippocampal cornu ammonis 1 (CA1), whereas expression of Hsp70.1 in the motor cortex without calpain activation contributes to neuroprotection. However, the molecular mechanisms of the lysosomal destabilization/stabilization determining neuronal cell fate have not been elucidated. To elucidate whether regulation of lysosomal ASM could affect the neuronal fate, we analyzed Hsp70.1-BMP binding and ASM activity by comparing the motor cortex and the CA1. We show that Hsp70.1 being localized at the lysosomal membrane, lysosomal lipid BMP levels, and the lipid binding domain of Hsp70.1 are crucial for Hsp70.1-BMP binding. In the postischemic motor cortex, Hsp70.1 being localized at the lysosomal membrane could bind to BMP without calpain activation and decreased BMP levels, resulting in increasing ASM activity and lysosomal stability. However, in the postischemic CA1, calpain activation and a concomitant decrease in the lysosomal membrane localization of Hsp70.1 and BMP levels may diminish Hsp70.1-BMP binding, resulting in decreased ASM activity and lysosomal rupture with leakage of cathepsin B into the cytosol. A TUNEL assay revealed the differential neuronal vulnerability between the CA1 and the motor cortex. These results suggest that regulation of ASM activation in vivo by Hsp70.1-BMP affects lysosomal stability and neuronal survival or death after ischemia/reperfusion.
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