Heat-shock response in camel (Camelus dromedarius) blood cells and adaptation to hyperthermia.

1. We demonstrate the difference between the reactions of camel (Camelus dromedarius) lymphocytes and erythrocytes to heat-shock treatment. 2. Lymphocytes of this organism characteristically have a higher resistance of general protein synthesis to elevated temperature in comparison with human lymphocytes. 3. Camel lymphocytes exhibited strong induction of constitutively expressed 73 kDa heat-shock protein (hsp 73) after heat-shock but failed to synthesize an inducible member of the same family (hsp 72) at high temperatures. 4. Nucleated camel erythrocytes do not synthesize any heat-shock proteins after temperature elevation. 5. Western blot analysis, using polyclonal antibody for hsp 73, revealed high levels of this protein in camel lymphocytes and diminished, but significant, amounts of hsp 73 protein in the erythrocytes under normal physiological conditions. 6. The role of 73 kDa hsp in providing thermotolerance of camel blood cells is discussed.

[Molecular mechanisms of adaptation to hyperthermia in higher organisms. III. Induction of heat-shock proteins in two Leishmania species]. / Molekuliarnye mekhanizmy adaptatsii k gipertermii u vysshikh organizmov. III. Induktsiia belkov teplovogo shoka u dvukh vidov leishmanii.

The heat-shock proteins (hsp) induction in two species of Leishmania have been investigated. The species studied are parasites of two species of lizards (Lymnodactylus caspins and Agama caucasica) differing by temperature of correspondent ecological niche. Our results show that Leishmania species restricted to high-temperature host (Agama) is capable to synthesize its proteins at extreme temperatures (38, 40 degrees C) with greater intensity. Moreover, the species of Leishmania studied differed by heat-shock proteins pattern, the intensive synthesis of hsp88 and hsp48 being the characteristic features of Leishmania species, restricted to the high-temperature host.