Specificity and localisation of lipoprotein lipase in the flight muscles of Locusta migratoria.
Using natural lipoproteins as substrates, lipase activity has been measured in leg muscle, fat body, midgut and flight muscles of Locusta migratoria. The enzymic activity in the flight muscles is higher than in those other tissues tested, confirming the potential of the flight muscles to utilise lipids at high rates. In addition, a membrane-bound lipoprotein lipase can be extracted from flight muscle. The flight muscle enzyme activity shows a marked substrate specificity; at lipoprotein concentrations equivalent to those found normally in flown or resting locusts respectively, the enzyme hydrolyses diacylglycerols associated with lipoprotein A+ (present in the haemolymph of flown or adipokinetic hormone-injected locusts) at about 4 times the rate of those associated with lipoprotein Ayellow (which is the major lipoprotein in resting locusts). In addition, the hydrolysis of lipids carried by lipoprotein Ayellow is dramatically reduced in the presence of lipoprotein A+. These observations indicate that the enzyme plays a specific role in the uptake of lipids at the flight muscles to ensure a smooth transition from carbohydrate to lipid based metabolism during flight.
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D005426:Flight, Animal; D006110:Grasshoppers / Q000378:metabolism*; D006458:Hemolymph / Q000378:metabolism; D008071:Lipoprotein Lipase / Q000032:analysis*; D009132:Muscles / Q000201:enzymology* / Q000648:ultrastructure; D013379:Substrate Specificity
D008071:Lipoprotein Lipase