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Role of chilling in the acquisition of cold tolerance and the capacitation to express stress proteins in diapausing pharate larvae of the gypsy moth, Lymantria dispar
Author(s) -
Denlinger David L.,
Lee Richard E.,
Yocum George D.,
Kukal Olga
Publication year - 1992
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.940210404
Subject(s) - biology , lymantria dispar , larva , cryoprotectant , gypsy moth , diapause , hardiness (plants) , botany , phormia regina , dispar , calliphoridae , cryopreservation , microbiology and biotechnology , embryo , cultivar , entamoeba histolytica
Cold hardiness in eggs (pharate first instar larvae) of the gypsy moth is not a component of the diapause program, but is acquired only after the pharate larvae have been chilled. The supercooling points of unchilled (25°C) and chilled (5°C) eggs are nearly the same (ca. −27°C), and chilling does not further elevate concentrations of glycerol, the major cryoprotectant, yet chilling at 5°C greatly increases the pharate larva's tolerance of −20°C. One conspicuous difference between the chilled and unchilled pharate larvae is their ability to express stress proteins. The most abundantly expressed stress protein, 75,000 M r , was expressed more highly in chilled pharate larvae than in unchilled pharate larvae, both at high temperatures (> 40°C) and in response to low temperature (−15°C). This correlation suggests a link between stress protein synthesis and the acquisition of cold tolerance. © 1992 Wiley‐Liss, Inc.