Abstract

A truncated form of a' chain (ta'), the soybean 7S globulin, active in controlling the cholesterol and triglyceride homeostasis in in vitro and in vivo models, was cloned and expressed in the yeast Pichia pastoris. The recombinant polypeptide spanned 216 amino acid residues from the N-terminal side and included the N-terminal extension region of the soybean subunit. The ta' polypeptide was purified by conventional biochemical techniques and its potential to modulate the activity of the LDL-receptor was evaluated in a human hepatoma cell line (Hep G2) by monitoring the uptake and degradation of labeled LDL. The LDL uptake (+ 192%) and degradation (+ 143%) by cells tested at the highest ta' dose (8 µM) were similar to those found in cells incubated with 1 µM simvastatin, a potent inhibitor of cholesterol biosynthesis. The cell response to ta' was found to be dose-dependent.


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Document History
  • Publication: Dec 23, 2010
  • Application: Jun 16, 2010
    WO EP 2010003626 W
  • Priority: Jun 17, 2009
    EP EP 09162935 A

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