HSP70 and lysosomal storage disorders: novel therapeutic opportunities.
Lysosomes, with their arsenal of catabolic enzymes and crucial metabolic housekeeping functions are experiencing a revived research interest after having lived a rather quiet life for the last few decades. With the discovery of the interaction of the lysosomes with another ancient component of cellular homoeostasis, the molecular chaperone HSP70 (heat-shock protein 70), the stage seems set for further discoveries of the mechanisms regulating cellular and physiological stress responses to otherwise detrimental challenges.
Danish Cancer Society, Strandboulevarden 49, 2100 Copenhagen, Denmark.
Nikolaj H T
NH
Petersen
Thomas
T
Kirkegaard
D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006706:Homeostasis; D006801:Humans; D008246:Lysophospholipids / Q000378:metabolism; D016464:Lysosomal Storage Diseases / Q000378:metabolism* / Q000503:physiopathology / Q000628:therapy*; D008247:Lysosomes / Q000378:metabolism / Q000648:ultrastructure; D008958:Models, Molecular; D050178:Monoglycerides / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D013108:Sphingomyelin Phosphodiesterase / Q000378:metabolism; D013312:Stress, Physiological
D018840:HSP70 Heat-Shock Proteins; D008246:Lysophospholipids; D050178:Monoglycerides; C012786:bis(monoacylglyceryl)phosphate; C112980:acid sphingomyelinase-1; D013108:Sphingomyelin Phosphodiesterase