ArticleCellular and molecular life sciences : CMLS2011
Heat-shock protein 60 translocates to the surface of apoptotic cells and differentiated megakaryocytes and stimulates phagocytosis.
Article in Cellular and molecular life sciences : CMLS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 34 citations in OpenAlex.
- Enhanced inhibitory effects of mianserin in combination with sorafenib on liver cancer growth through targeting the CCR9-AKT pathway.American journal of cancer research · 2025Article
- Pharmacologic dissection of the overlapping impact of heat shock protein family members on platelet function.Journal of thrombosis and haemostasis : JTH · 2020Article
- Analysis of the spleen proteome of chickens infected with reticuloendotheliosis virus.Archives of virology · 2017Article
- Microglia and Monocyte-Derived Macrophages in Stroke.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2016Review
- The evolving biology of microglia in Alzheimer's disease.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2015Review
- The expression and release of Hsp60 in 6-OHDA induced in vivo and in vitro models of Parkinson's disease.Neurochemical research · 2013Article
- Janus-faced microglia: beneficial and detrimental consequences of microglial phagocytosis.Frontiers in cellular neuroscience · 2013Article
- Purification of mitochondrial proteins HSP60 and ATP synthase from ascidian eggs: implications for antibody specificity.PloS one · 2013Article
- CHCM1/CHCHD6, novel mitochondrial protein linked to regulation of mitofilin and mitochondrial cristae morphology.The Journal of biological chemistry · 2012Article
- Circulating heat shock protein 60 levels are elevated in HIV patients and are reduced by anti-retroviral therapy.PloS one · 2012Article
Corrections and comments
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Authors and funding
9 authors at 7 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat-shock protein 60 (Hsp60) is a highly conserved stress protein which has chaperone functions in prokaryotes and mammalian cells. Hsp60 is associated with the mitochondria and the plasma membrane through phosphorylation by protein kinase A, and is incorporated into lipid membranes as a protein-folding chaperone. Its diverse intracellular chaperone functions include the secretion of proteins where it maintains the conformation of precursors and facilitates their translocation through the plasma membrane. We report here that Hsp60 is concentrated in apoptotic membrane blebs and translocates to the surface of cells undergoing apoptosis. Hsp60 is also enriched in platelets derived from terminally differentiated megakaryocytes and expressed at the surface of senescent platelets. Furthermore, the exposure of monocytic U937 cells to Hsp60 enhanced their phagocytic activity. Our results suggests that externalized Hsp60 in apoptotic cells and senescent platelets influences events subsequent to apoptosis, such as the clearance of apoptotic cells by phagocytes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.