Synthesis of heat shock proteins in quail red blood cells following brief, physiologically relevant increases in whole body temperature.
Cultured RBCs from quail respond to thermal stress (heat shock) by a rapid and dramatic change in gene expression. This change in gene expression includes the new and/or enhanced non-coordinate synthesis of a small group of heat shock polypeptides (HSPs) having molecular masses of 90,000, 70,000 and 26,000. RBCs obtained from hyperthermic quail exhibit a change in gene expression similar to that observed in RBCs heat-shocked in vitro. Since in vitro studies have linked the synthesis of HSPs in heat-stressed cells with thermotolerance, the similar change in gene expression in RBCs from hyperthermic quail suggests that, here too, this cellular response may be an important homeostatic mechanism by which avian RBCs cope with and/or survive hyperthermic conditions.
D000818:Animals; D001831:Body Temperature; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000097:blood* / Q000302:isolation & purification; D007700:Kinetics; D008715:Methionine / Q000097:blood; D008970:Molecular Weight; D011784:Quail; D013462:Sulfur Radioisotopes
D006360:Heat-Shock Proteins; D013462:Sulfur Radioisotopes; D008715:Methionine