Back to Search
Start Over
Heat shock proteins induce pores in membranes.
- Source :
-
Bioscience reports [Biosci Rep] 1990 Dec; Vol. 10 (6), pp. 509-18. - Publication Year :
- 1990
-
Abstract
- Human heat shock protein (hsp) 70 and bacterial protein groEL promote leakage of calcein from liposomes induced by human serum albumin signal peptide, by S. aureus alpha toxin or by diphtheria toxin. Hsp 70 and groEL, as well as two mycobacterial homologues hsp 71 and hsp 65, induce ion conducting pores across planar lipid bilayers at low or neutral pH. It is concluded that hsp induce pores in membranes and that this may contribute to their action within cells.
- Subjects :
- Amino Acid Sequence
Cell Membrane Permeability drug effects
Cell Membrane Permeability physiology
Chaperonin 60
Drug Synergism
Heat-Shock Proteins isolation & purification
Hydrogen-Ion Concentration
Ion Channel Gating physiology
Liposomes
Molecular Sequence Data
Protein Sorting Signals chemical synthesis
Protein Sorting Signals pharmacology
Type C Phospholipases pharmacology
Bacterial Proteins pharmacology
Fluoresceins metabolism
Heat-Shock Proteins pharmacology
Ion Channel Gating drug effects
Subjects
Details
- Language :
- English
- ISSN :
- 0144-8463
- Volume :
- 10
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Bioscience reports
- Publication Type :
- Academic Journal
- Accession number :
- 1982226
- Full Text :
- https://doi.org/10.1007/BF01116611