Synthesis of active high mannose-type lipoprotein lipase in human adipose tissues.

Lipoprotein lipase (LPL) activity in the retroperitoneal adipose tissue of a patient with Cushing's syndrome and in the subcutaneous adipose tissue of a patient with aseptic necrosis of the femoral head was higher than that in the corresponding tissues of the control subjects. The amount of [35S]methionine incorporated into LPL was also higher in these patients than in control subjects. However, the ratio of activity and amount of radioactivity in the LPL of patients was identical to that of control subjects, indicating that LPL synthesized in the adipose tissues of patients had a normal specific activity. LPL with Mr = 57000 was composed of two types of subunits: one type was partially endo H-sensitive, yielding a product with Mr = 55000, and the other was totally endo H-sensitive, yielding a product with Mr = 52000. Both retroperitoneal and subcutaneous adipose tissues of control subjects contained nearly equal amounts of partially and totally endo H-sensitive subunits. In the retroperitoneal adipose tissue of a patient with Cushing's syndrome, 8% of subunits were partially endo H-sensitive and 92% were totally endo H-sensitive. In the subcutaneous adipose tissue of a patient with aseptic necrosis of the femoral head, 21% of subunits were partially endo H-sensitive and 79% were totally endo H-sensitive. The 24-h treatment of subcutaneous adipose tissue of a control subject with 1 mM 1-deoxymannojirimycin (dMM) caused the synthesis of active, but totally endo H-sensitive, LPL. Thus, in human adipose tissue, the processing of one oligosaccharide chain of an LPL subunit to a complex type chain in the trans Golgi was not necessary for the expression of activity.