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Expression of heat shock proteins in response to high and low temperature extremes in diapausing pharate larvae of the gypsy moth, Lymantria dispar
Author(s) -
Yocum George D.,
Joplin Karl H.,
Denlinger David L.
Publication year - 1991
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940180406
Subject(s) - lymantria dispar , heat shock protein , biology , shock (circulatory) , gypsy moth , protein biosynthesis , cold shock domain , heat shock , hsp70 , microbiology and biotechnology , dispar , biochemistry , larva , immunology , botany , medicine , gene , rna , entamoeba histolytica
Diapausing pharate first instars of the gypsy moth, Lymantria dispar , respond to high temperature (37–41°C) by suppressing normal protein synthesis and synthesizing a set of seven heat shock proteins with M r s of 90,000, 75,000, 73,000, 60,000, 42,000, 29,000, and 22,000 as determined by SDS‐PAGE. During recovery at 25°C from heat shock, synthesis of the heat shock proteins gradually decreases over a period of 6 h, while normal protein synthesis is restored. A subset of these same heat shock proteins is also expressed during recovery at 4°C or 25°C from brief exposures to low temperature (‐10 to 20°C), and its expression is more intense with increased severity of cold exposure. During recovery at 4°C after 24 h at −20°C, both 90,000 and 75,000 M r heat shock proteins are expressed for more than 96 h. While normal protein synthesis is suppressed during heat shock and recovery from heat shock, normal protein synthesis coincides with synthesis of the heat shock proteins during recovery from low temperatures, thus implying that expression of the heat shock proteins is not invariably linked to suppression of normal protein synthesis. Western transfer, using a monoclonal antibody that recognizes the inducible form of the human 70,000 M r heat shock protein, demonstrates that immunologically related proteins in the gypsy moth are expressed at 4°C and during recovery from cold and heat shock.