ArticleMolecular and cellular biochemistry2004
Expression of 60 kDa heat shock protein (Hsp60) on plasma membrane of Daudi cells.
Article in Molecular and cellular biochemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Ectopic CH60 mediates HAPLN1-induced cell survival signaling in multiple myeloma.Life science alliance · 2023Article
- Role of heat shock protein 60 in primed and naïve states of human pluripotent stem cells.PloS one · 2022Article
- Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets.Cells · 2020Review
- Elevated sodium leads to the increased expression of HSP60 and induces apoptosis in HUVECs.PloS one · 2017Article
- Molecular cloning, characterization, and expression of hsp60 in caudal fin regeneration of Misgurnus anguillicaudatus.Molecular and cellular biochemistry · 2014Article
- Antigen-specificity of oligoclonal abnormal protein bands in multiple myeloma after allogeneic stem cell transplantation.Cancer immunology, immunotherapy : CII · 2012Article
- S-layer, surface-accessible, and concanavalin A binding proteins of Methanosarcina acetivorans and Methanosarcina mazei.Journal of proteome research · 2009Article
- Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60.The Biochemical journal · 2005Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Daudi cells, a fraction of the 60 kDa heat shock protein (Hsp60), which is typically a mitochondrial protein, is located on cell membrane. This was demonstrated by the recovery of biotinylated Hsp60 in the anti-Hsp60 immunoprecipitate obtained from cells in which surface-exposed proteins were selectively labeled with biotin. In further experiments, isolated membrane proteins (obtained by two different biochemical methods) were probed in Western blot with two antibodies (N-20 and K-19) directed against different epitopes located, respectively, at the amino- and at the carboxyl-terminus of the Hsp60. Both these antibodies recognized, among the isolated membrane proteins, a unique band with an electrophoretic mobility identical to that of the cytoplasmic Hsp60, thus demonstrating that Hsp60 is present on cell surface as an intact, full-length, protein. FACS analysis, performed with the same two highly specific anti-Hsp60 antibodies, confirmed that both the N-terminus and the C-terminus of the Hsp60 are exposed outside the cell and are accessible for recognition by the corresponding antibody. Moreover, quantitative analysis of the data showed that constitutive cell surface expression of the Hsp60 is limited to a small fraction (about 10%) of the whole cell population.
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