Abstract
The induction of heat shock proteins in three species of Leishmania, L. tropica, L. enrietti, and L. donovani is reported. When cultures of promastigotes are shifted from 26 degrees C to 37 degrees C or 40 degrees C, the synthesis of proteins with apparent molecular weights of 88,000, 74,000, and 54,000 is stimulated. Actinomycin D added just prior to the shift prevented the appearance of these proteins but had no effect when present 30 min after the transfer onward, suggesting that the regulation of leishmanial heat shock proteins occurs at the transcriptional level. Exposure of L. tropica promastigotes to sodium arsenite elicits the synthesis of three major and four minor polypeptides. Their apparent molecular weights are, respectively, 94,000, 78,000, and 56,000 and 70,000, 45,000, 22,000, and 18,000. The response of Leishmania organisms to heat shock and to sodium arsenite is similar to that of other organisms, but some of the proteins identified as stress proteins in the parasite differ in size. The heat shock proteins might play a role in cytodifferentiation during the life cycle of the parasite and also in cellular adaptation to higher temperatures.
Full text
PDF



Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Ashburner M., Bonner J. J. The induction of gene activity in drosophilia by heat shock. Cell. 1979 Jun;17(2):241–254. doi: 10.1016/0092-8674(79)90150-8. [DOI] [PubMed] [Google Scholar]
- Bensaude O., Babinet C., Morange M., Jacob F. Heat shock proteins, first major products of zygotic gene activity in mouse embryo. Nature. 1983 Sep 22;305(5932):331–333. doi: 10.1038/305331a0. [DOI] [PubMed] [Google Scholar]
- Berger E. M., Woodward M. P. Small heat shock proteins in Drosophila may confer thermal tolerance. Exp Cell Res. 1983 Sep;147(2):437–442. doi: 10.1016/0014-4827(83)90225-2. [DOI] [PubMed] [Google Scholar]
- Chang K. P. Human cutaneous lieshmania in a mouse macrophage line: propagation and isolation of intracellular parasites. Science. 1980 Sep 12;209(4462):1240–1242. doi: 10.1126/science.7403880. [DOI] [PubMed] [Google Scholar]
- Daniels C. J., McKee A. H., Doolittle W. F. Archaebacterial heat-shock proteins. EMBO J. 1984 Apr;3(4):745–749. doi: 10.1002/j.1460-2075.1984.tb01878.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DiDomenico B. J., Bugaisky G. E., Lindquist S. The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels. Cell. 1982 Dec;31(3 Pt 2):593–603. doi: 10.1016/0092-8674(82)90315-4. [DOI] [PubMed] [Google Scholar]
- Fong D., Chang K. P. Tubulin biosynthesis in the developmental cycle of a parasitic protozoan, Leishmania mexicana: changes during differentiation of motile and nonmotile stages. Proc Natl Acad Sci U S A. 1981 Dec;78(12):7624–7628. doi: 10.1073/pnas.78.12.7624. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hunter K. W., Cook C. L., Hayunga E. G. Leishmanial differentiation in vitro: induction of heat shock proteins. Biochem Biophys Res Commun. 1984 Dec 14;125(2):755–760. doi: 10.1016/0006-291x(84)90603-x. [DOI] [PubMed] [Google Scholar]
- Johnston D., Oppermann H., Jackson J., Levinson W. Induction of four proteins in chick embryo cells by sodium arsenite. J Biol Chem. 1980 Jul 25;255(14):6975–6980. [PubMed] [Google Scholar]
- Kelley P. M., Schlesinger M. J. Antibodies to two major chicken heat shock proteins cross-react with similar proteins in widely divergent species. Mol Cell Biol. 1982 Mar;2(3):267–274. doi: 10.1128/mcb.2.3.267. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kelley P. M., Schlesinger M. J. The effect of amino acid analogues and heat shock on gene expression in chicken embryo fibroblasts. Cell. 1978 Dec;15(4):1277–1286. doi: 10.1016/0092-8674(78)90053-3. [DOI] [PubMed] [Google Scholar]
- LaThangue N. B., Shriver K., Dawson C., Chan W. L. Herpes simplex virus infection causes the accumulation of a heat-shock protein. EMBO J. 1984 Feb;3(2):267–277. doi: 10.1002/j.1460-2075.1984.tb01796.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Lambowitz A. M., Kobayashi G. S., Painter A., Medoff G. Possible relationship of morphogenesis in pathogenic fungus, Histoplasma capsulatum, to heat shock response. Nature. 1983 Jun 30;303(5920):806–808. doi: 10.1038/303806a0. [DOI] [PubMed] [Google Scholar]
- Li G. C. Induction of thermotolerance and enhanced heat shock protein synthesis in Chinese hamster fibroblasts by sodium arsenite and by ethanol. J Cell Physiol. 1983 May;115(2):116–122. doi: 10.1002/jcp.1041150203. [DOI] [PubMed] [Google Scholar]
- Li G. C., Werb Z. Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts. Proc Natl Acad Sci U S A. 1982 May;79(10):3218–3222. doi: 10.1073/pnas.79.10.3218. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lowe D. G., Fulford W. D., Moran L. A. Mouse and Drosophila genes encoding the major heat shock protein (hsp70) are highly conserved. Mol Cell Biol. 1983 Aug;3(8):1540–1543. doi: 10.1128/mcb.3.8.1540. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mitchel R. E., Morrison D. P. Heat-shock induction of ultraviolet light resistance in Saccharomyces cerevisiae. Radiat Res. 1983 Oct;96(1):95–99. [PubMed] [Google Scholar]
- Rodbard D., Wachslicht-Rodbard H., Rodbard S. Temperature: a critical factor determining localization and natural history of infectious, metabolic, and immunological diseases. Perspect Biol Med. 1980 Spring;23(3):439–474. doi: 10.1353/pbm.1980.0062. [DOI] [PubMed] [Google Scholar]
- Sacks D. L., Barral A., Neva F. A. Thermosensitivity patterns of Old vs. New World cutaneous strains of Leishmania growing within mouse peritoneal macrophages in vitro. Am J Trop Med Hyg. 1983 Mar;32(2):300–304. doi: 10.4269/ajtmh.1983.32.300. [DOI] [PubMed] [Google Scholar]
- Singh M. K., Yu J. Accumulation of a heat shock-like protein during differentiation of human erythroid cell line K562. Nature. 1984 Jun 14;309(5969):631–633. doi: 10.1038/309631a0. [DOI] [PubMed] [Google Scholar]
- Vincent M., Tanguay R. M. Different intracellular distributions of heat-shock and arsenite-induced proteins in Drosophila Kc cells. Possible relation with the phosphorylation and translocation of a major cytoskeletal protein. J Mol Biol. 1982 Dec 5;162(2):365–378. doi: 10.1016/0022-2836(82)90532-0. [DOI] [PubMed] [Google Scholar]
- Walsh C. Appearance of heat shock proteins during the induction of multiple flagella in Naegleria gruberi. J Biol Chem. 1980 Apr 10;255(7):2629–2632. [PubMed] [Google Scholar]
- Welch W. J., Feramisco J. R. Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells. J Biol Chem. 1984 Apr 10;259(7):4501–4513. [PubMed] [Google Scholar]




