A single type of high density lipoprotein (HDLp) binding sites is present at intact fat body tissue and in fat body membranes of larval and adult locusts. HDLp is bound with high affinity (Kd approximately 10(-7) M). This interaction does not require divalent cations and is heat-labile because heat-treatment of fat body membranes results in a substantial reduction of the maximal binding capacity. In addition to unlabeled HDLp and low density lipophorin (LDLp), human low density lipoprotein also seems to compete with radiolabeled HDLp for this binding site, suggesting a relaxed specificity. Induction of lipid mobilization with adipokinetic hormone did not change the binding characteristics of the fat body. An increase in the binding capacity of intact fat body tissue in the adult stage suggests that the number of cell surface binding sites is upregulated during development. However, the total number of HDLp binding sites appears to be constant, because larval and adult fat body membranes have similar binding capacities.