Factors causing compositional changes in soy protein hydrolysates and effects on cell culture functionality.

Soy protein hydrolysates significantly enhance cell growth and recombinant protein production in cell cultures. The extent of this enhancement in cell growth and IgG production is known to vary from batch to batch. This can be due to differences in the abundance of different classes of compounds (e.g., peptide content), the quality of these compounds (e.g., glycated peptides), or the presence of specific compounds (e.g., furosine). These quantitative and qualitative differences between batches of hydrolysates result from variation in the seed composition and seed/meal processing. Although a considerable amount of literature is available that describes these factors, this knowledge has not been combined in an overview yet. The aim of this review is to identify the most dominant factors that affect hydrolysate composition and functionality. Although there is a limited influence of variation in the seed composition, the overview shows that the qualitative changes in hydrolysate composition result in the formation of minor compounds (e.g., Maillard reaction products). In pure systems, these compounds have a profound effect on the cell culture functionality. This suggests that the presence of these compounds in soy protein hydrolysates may affect hydrolysate functionality as well. This influence on the functionality can be of direct or indirect nature. For instance, some minor compounds (e.g., Maillard reaction products) are cytotoxic, whereas other compounds (e.g., phytates) suppress protein hydrolysis during hydrolysate production, resulting in altered peptide composition, and, thus, affect the functionality.

Toward establishing structure-activity relationships for oxygenated coumarins as differentiation inducers of promonocytic leukemic cells.

The presumption that some coumarins might be lead compounds in the search for new differentiation agents against leukemia is based on the fact that natural coumarins, 5-(3-methyl-2-butenyloxy)-6,7-methylenedioxycoumarin (C-2) and 5-methoxy-6,7-methylenedioxycoumarin (C-1) inhibit proliferation and induce differentiation in U-937 cells [Riveiro, M. E.; Shayo, C.; Monczor, F.; Fernandez, N.; Baldi, A.; De Kimpe, N.; Rossi, J.; Debenedetti, S.; Davio, C. Cancer Lett.2004, 210, 179-188]. These promising findings prompted us to investigate the anti-leukemia activity of a broader range of related polyoxygenated coumarins. Twenty related natural or synthetically prepared coumarins, including a range of 5-substituted ayapin derivatives which have become easy accessible via newly developed synthesis methods, were evaluated, where treatments with 5-(2,3-dihydroxy-3-methylbutoxy)-6,7-methylenedioxycoumarin (D-3) and 5-(2-hydroxy-3-methoxy-3-methylbutoxy)-6,7-methylenedioxycoumarin (D-2) were able to inhibit the cell growth and induce the differentiation of U-937 cells after 48 h treatment. These results provide insight into the correlation between some structural properties of polyoxygenated coumarins and their in vitro leukemic differentiation activity.

Coumarins from Cnidium monnieri and their antiosteoporotic activity.

Bioactivity-guided fractionation has led to the successful isolation of antiosteoporotic components, i. e., osthole, imperatorin and bergapten from an ethanolic extract of the fruits of Cnidium monnieri (L.) Cusson. Among them, osthole was determined as the major compound possessing antiosteoporotic activity. Further study showed that osthole not only promoted the proliferation and activity of alkaline phosphatase of osteoblasts in neonatal calvaria cultures, but also inhibited the bone resorption by decreasing the formation, differentiation and TRAP activity of osteoclasts derived from rat marrow cells.