Abstract
The liver plays an important role in the catabolism of High Density Lipoprotein (HDL). It has been difficult to identify HDL3 receptor because of HDL3 containing apo E. The present study is to elucidate the characteristics of HDL3 receptor by studying the binding of HDL3 with rat liver plasma membrane.In HDL3 isolated by sequential ultracentrifugation, the protein moiety consists more than 90 of apo A-I and A-II, and 0.1% of apo E. In isolated perfused rat liver, rat liver uptook 4% of HDL3 within the first pass and its ratio did not increase by the treatment of Ethynil-Estradiol.HDL3 bound to the rat liver plasma membrane in the fashion of time, temperature, and pH dependence. At 4°C, the specific binding of HDL3 was equilibrated and saturated after 60 min. The Kd was 11.0μg/ml. The binding sites showed heterogeneity by Scatchard analysis and the high affinity binding sites was 1.15μg/mg·membrane protein. The specific binding was Calcium independent and competed with HDL3, but not with LDL. This suggest that rat liver has HDL3 receptor different from apo B and E receptor and also apo E receptor. The HDL3 receptor binding assay may be useful to estimate the physiological and pathological circumstances.
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