Five proteins were expressed in larval honey bee fat bod incubated in vitro
in response to heat shock, as shown by SDS-PAGE and fluorography. The larg
e heat shock proteins (82, 70 kDa) were inducible throughout the 5th instar
whereas the small ones (29, 26, 16 kDa) were inducible only in certain pha
ses of this instar. The synthesis of these HSPs was accompanied by generali
zed inhibition of overall protein synthesis and secretion in the culture me
dium. Fluorograms showed that the 76 and 74 kDa proteins were strongly inhi
bited by heat treatment. Western blots using a mouse monoclonal antibody ag
ainst HSP72 and HSC73 permitted the inference that the 70 kDa larval protei
n accumulated in the honey bee fat body in response to heat shock correspon
ds to the HSP72 isoform. The Western blots also showed a 70 kDa faint band
in fat bodies incubated at the control temperature (34 degrees C). This pro
tein, also detected in incubation media independently of the temperature us
ed, was interpreted as being the constitutively synthesized and secreted HS
C73 isoform.