ABSTRACT
Plants are particularly suitable bioreactors for the production of proteins, as their eukaryotic nature frequently directs the appropriate post-translational modifications of recombinant proteins to retain native biological activity. The autotrophic growth of plants makes this in vivo biosynthesis system economically competitive for supplementation or replacement of conventional production systems in the future. For the production of biologically active proteins, food plants provide the advantage of direct delivery via consumption of transformed plant tissues. Here we describe the production of recombinant human milk proteins in food plants for improvements in human nutrition and health, with emphasis on enhanced nutrition for non-breast fed infants as well as children and adults. Nutritional improvements in edible plants generated through advancements in recombinant DNA technology are rapidly repositioning the world for enjoyment of a more healthful diet for humans in all age groups.
Subject(s)
Milk Proteins/genetics , Milk, Human/chemistry , Plants, Genetically Modified/metabolism , Adult , Animals , Bioreactors , Caseins/biosynthesis , Cattle , Humans , Lactalbumin/biosynthesis , Lactoferrin/biosynthesis , Milk Proteins/biosynthesis , Recombinant Proteins/biosynthesis , Solanum tuberosumABSTRACT
We have demonstrated that insulin-like growth factor I (IGF-I), at physiological concentrations, is a potent mitogen of bovine undifferentiated mammary epithelial cells cultured in collagen in serum-free medium. Its activity is independent of insulin, although at pharmacological concentrations insulin may substitute for IGF-I. The maximal [3H]thymidine incorporation stimulated by either IGF-I or insulin was only 25-40% of that in medium supplemented with 10% fetal calf serum (FCS) only. Epidermal growth factor (EGF) exhibited low mitogenic activity which was not synergistic with IGF-I in serum-free medium. IGF-I and EGF had low synergistic activity when added separately to 10% FCS-supplemented medium. Strong synergism (100% or more) was observed, however, when both factors were added simultaneously, indicating that their maximum mitogenic effect is dependent on a simultaneous presence of other factors existing in FCS. The galactopoietic effect of IGF-I was tested in organ culture of bovine lactating mammary gland. Neither fatty acid synthesis nor alpha-lactalbumin secretion was stimulated by IGF-I, even at 2000 ng/ml. These results indicate that, at least in our in vitro system, galactopoiesis is not affected by IGF-I.