A protein that binds to the main apoprotein, apoA‐I, of human high density lipoprotein (HDL) has been isolated from human placenta. Ligand blotting after SDS gel electrophoresis indicated that the 120 kDa protein in the absence of reducing agents binds apoA‐I. If gel electrophoresis was performed under reducing conditions two main bands, approx. 50 and 30 kDa that did not bind apoA‐I, were evident. In an enzyme‐linked immunosorbent assay the binding protein specifically bound apoA‐I, delipidated or as HDL. ApoA‐II, apo E and LDL did not compete with apoA‐I for binding to this protein.

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Adenosine content in abdominal and femoral adipose tissue in menstruating women was 0.38 \ m=+-\ 0.10 and 0.59 \ m=+-\ 0.14 nmol/g of wet weight, respectively (mean \m=+-\sem; N = 17). No difference in adenosine sensitivity was found between abdominal and femoral adipocytes. In lactating women, the adenosine content was lower in femoral than in abdominal adipose tissue (0.40 \ m=+-\0.08 and 0.57 \ m=+-\0.08 nmol/g of wet weight, respectively; N = 10). Adenosine sensitivity in femoral adipocytes was not increased during lactation. As adenosine is a locally acting insulin-like effector, these results suggest that the higher adenosine content in femoral adipose tissue in menstruating women could explain its higher lipoprotein lipase activity and tendency to accumulate fat. During lactation, the lower extracellular adenosine concentration would allow lipid mobilization preferentially from the femoral site.

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