The patterns of heat-induced synthesis (37 degrees C to 45 degrees C) of he
at shock proteins (Hsps) in different tissues of grasshoppers and cockroach
es from natural populations and in laboratory-reared gram-pest (Heliothis a
rmigera) were examined by S-35-methionine labeling and sodium dodecyl sulfa
te-polyacrylamide gel electrophoresis fluorography. Whereas 45 degrees C wa
s lethal in most cases, optimal induction of Hsp synthesis was seen between
37 degrees C and 42 degrees C. The ongoing protein synthesis was not much
affected at these temperatures, except in the tissues of adult H armigera e
xposed to 42 degrees C. The profiles of the Hsps induced in the tissues of
the insects, however, were different. From the relative abundance of the sy
nthesis of 70-kDa (Hsp70) and 64-kDa (Hsp64) polypeptides, three categories
of heat shock response were identified: (1) induction of abundant Hsp70 bu
t little Hsp64 (malpighian tubules, male accessory glands, and ovaries of a
dult grasshoppers), (2) abundant Hsp64 but little Hsp70 (testes of adult gr
asshoppers, testes and malpighian tubules of adult cockroaches, and testes,
malpighian tubules, and fat bodies of H armigera larvae), and (3) inductio
n of both Hsp70 and Hsp64 in more of less equal abundance (ovaries of adult
cockroaches, salivary glands of H armigera larvae, and malpighian tubules,
male accessory glands, testes, and ovaries of adult H armigera). Cockroach
es collected from storerooms showed detectable synthesis of Hsp64 and/or Hs
p70 only after heat shock, but those collected from drains showed detectabl
e synthesis of both Hsp70 and Hsp64 in different tissues without heat stres
s. Western blotting showed that the 64-kDa polypeptide in these insects is
a member of the Hsp60 family. Grasshopper testes, which synthesized negligi
ble Hsp70 but abundant Hsp64 after heat shock, developed thermotolerance. T
hus, heat shock response is modulated by developmental and environmental fa
ctors in different tissues of insects.