Eur. J. Entomol. 93 (3): 419-433, 1996
Tracking the profile of a specific antifreeze protein and its contribution to the thermal hysteresis activity in cold hardy insects
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This study summarizes some important new directions in research on antifreeze protein biosynthesis and regulation. It describes the recent development and availability of essential biochemical and cellular tools that make possible more direct cellular investigations, and an assessment of the relationship between thermal hysteresis protein (THP) levels and antifreeze activity (both thermal hysteresis and recrystallization inhibition [RI]). These tools include: 1) the isolation of a specific THP of high activity designated Tm 12.86), and an additional endogenous activating factor of this antifreeze protein; 2) the ability to track the cellular and secretory patterns of Tm 12.86 immunologically; 3) the use of an in vitro fat body cell culture system for direct investigation of cellular events, and, 4) a means of quantifying RI behavior of purified Tm 12.86, and samples of unknown concentrations of THPs, to provide a more sensitive detection method for antifreeze activity at scaled down values associated with the in vitro system. In combination, these studies indicate that the adaptation mechanisms contributing to the overall antifreeze protein response in a cold hardy insect involves a complex interaction between antifreeze proteins and endogenous activators of these proteins. With the availability of these key tools, the details of a precise and seasonal regulation of these antifreeze protein/activator interactions, which ultimately generate an efficient cold hardy response, now have the potential to be worked out.
Keywords: Antifreeze proteins, thermal hysteresis, Tm 12.86, activators, cold hardiness, Tenebrio molitor
Accepted: June 10, 1996; Published: September 30, 1996 Show citation
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