Background: Although soy protein may have many health benefits derived from its associated antioxidants, many male exercisers avoid soy protein. This is due partly to a popular, but untested notion that in males, soy is inferior to whey in promoting muscle weight gain. This study provided a direct comparison between a soy product and a whey product.

) describes the cloning of a fulllength cDNA corresponding to a candidate cell surface HP/HS interacting protein, HIP, expressed by a variety of human epithelia. A synthetic peptide was synthesized corresponding to an amino acid sequence predicted from the cDNA sequence and used to prepare a rabbit polyclonal antibody. This antibody reacted with a protein with an apparent M r of 24,000 by SDS-polyacrylamide gel electrophoresis that was highly enriched in the 100,000 ؋ g particulate fraction of RL95 cells. This molecular weight is similar to that of the protein expressed by 3T3 cells transfected with HIP cDNA. HIP was solubilized from this particulate fraction with NaCl concentrations 0.8 M demonstrating a peripheral association consistent with the lack of a membrane spanning domain in the predicted cDNA sequence. HIP was not released by heparinase digestion suggesting that the association is not via membrane-bound HS proteoglycans. NaCl-solubilized HIP bound to heparin-agarose in physiological saline and eluted with NaCl concentrations of 0.75 M and above. Furthermore, incubation of Heparan sulfate proteoglycans (HSPGs) 1 located either on cell surfaces or in extracellular matrices are found in nearly all mammalian tissues (1-5). Functionally, HSPGs and a variety of HP/HS-binding proteins have been shown to participate in a diverse range of biological processes such as cell attachment, growth factor binding, cell proliferation, migration, morphogenesis, and viral pathogenicity (6 -8). Several lines of evidence indicate that HSPGs play an important role during the initial attachment of the apical plasma membrane of trophectodermal cells of the blastocyst to the apical plasma membrane of the uterine epithelium. In mice, HSPGs are expressed on the cell surfaces of two-cell stage and post-implantation stage embryos (9). Furthermore, blastocyst attachment to laminin, fibronectin, and isolated mouse uterine epithelial cells is inhibited by HP. Embryo attachment also is inhibited by the treatment of embryos with HP/HS lyases or inhibitors of proteoglycan biosynthesis (10, 11). Immunological studies of murine embryo implantation sites indicated that the core protein of the basement membrane HSPG, perlecan, and HP/HS chains are located between the apical cell surfaces of trophectodermal cells and uterine epithelial cells during the peri-implantation stage (12). Expression of perlecan on the external trophectodermal surface correlates with acquisition of attachment competence in vitro as well. Externally disposed H/HS-binding sites have been described on the cell surface of mouse uterine epithelial cells (13). Furthermore, using a heterologous cell adhesion assay, we demonstrated that HP/HS-like glycosaminoglycans participate in the initial attachment between two human cell lines, JAR and RL95, used to mimic the initial attachment of the human embryonic trophectoderm to human uterine epithelial cells, respectively (14). As is the case for mouse uterine epithelia, the human uterine epithelial cell line, RL95, has specific,...

The 24-h patterns of plasma concentration change in dopamine (DA) and its immediate deaminated metabolite, dihydroxyphenylacetic acid (DOPAC), were determined in 6 normal women (16 studies) by a modified radioenzymatic assay. Changes in DOPAC levels exhibited a marked circadian rhythm, with peak during the day and a nadir at night. At 1200 h, the DOPAC concentration increased significantly (P less than 10(-4)) to a peak value 62.9 +/- 8.4 ng/ml) 117% higher than the 24-h mean. At 2200 h, plasma DOPAC decreased (P less than 10(-4)) to a nadir concentration (10.0 +/- 3.3 ng/ml) 66% lower than the 24-h mean. The circadian rhythm of DOPAC could be reproducibly demonstrated over at least 4 successive days in individual subjects. There were no well defined circadian variations in plasma concentrations of DA. Since the plasma DOPAC concentration appears to reflect central nervous system dopaminergic neuronal activity, the present demonstration of a circadian rhythm of plasma DOPAC suggests that the activity of central nervous system DA-containing cells is higher during the day than at night.

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