The heat shock protein 90 of Leishmania donovani.
The 90-kDa heat shock protein (Hsp90) of Leishmania donovani is a highly abundant cytoplasmic protein and is involved in a variety of cellular processes. Pharmacological deactivation of Hsp90 leads to growth arrest and induces the synthesis of heat shock proteins. Moreover, treatment of promastigote parasites with Hsp90 inhibitors induces the synthesis of amastigote-specific marker proteins and a morphological alteration similar to axenic amastigote differentiation. We propose a role for Hsp90 in the feedback control of the cellular stress response and in the control of the parasite's life cycle.
Wiesgigl
M
M
Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany.
Clos
J
J
D000818:Animals; D016227:Benzoquinones; D002454:Cell Differentiation / Q000187:drug effects; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors / Q000502:physiology*; D006801:Humans; D047029:Lactams, Macrocyclic; D007893:Leishmania donovani / Q000187:drug effects / Q000254:growth & development / Q000502:physiology*; D008018:Life Cycle Stages; D011809:Quinones / Q000494:pharmacology
D016227:Benzoquinones; D018841:HSP90 Heat-Shock Proteins; D047029:Lactams, Macrocyclic; D011809:Quinones; C001277:geldanamycin