Do bacteria shape our development? Crosstalk between intestinal microbiota and HPA axis

Contains fulltext : 179965.pdf (publisher's version ) (Closed access)The human body contains as many bacteria in the intestine as the total number of human body cells. These bacteria have a central position in human health and disease, and would also play a role in the regulation of emotions, behavior, and even higher cognitive functions. The Hypothalamic-Pituitary-Adrenal axis (HPA axis) is a major physiological stress system that produces cortisol. This hormone is involved in responding to environmental stress and also shapes many aspects of brain development. Both the HPA axis and the intestinal microbiota show rapid and profound developmental changes during the first years of life. Early environmental disturbances can affect the development of both systems. Early adversity, for example, is known to lead to later unbalances in both, as well as to psychopathological behavior and emotions. The goal of this theoretical review is to summarize current knowledge on the developmental crosstalk between the intestinal microbiota and the HPA axis, providing a basis for understanding the development and bidirectional communication between these two essential systems in human functioning.14 p

Effects of Gigapascal Level Pressure on Protein Structure and Function

Information on very high pressure (VHP) effects on proteins is limited and therefore effects of VHP on chemistry, structure and function of two model proteins in medical use were studied. VHP (8 GPa) application to l-asparaginase (L-ASNase) resulted in faster mobility on clear native gels. VHP induced generation of lower-MW forms of L-ASNase but VHP treatment did not deteriorate asparaginase activity. Electrophoretic patterns in native and denaturing gels were comparable for untreated and pressurized recombinant human growth hormone (rhGH). rhGH function, however, was deteriorated as shown by a bioassay. In L-ASNase and rhGH a series of protein modifications and amino acid exchanges (indicating cleavage of covalent bonds) were revealed that may probably lead to functional and conformational changes. The findings have implications in protein chemistry, structure, and function and are useful for designing biotechnological applications of protein products

Effects of Gigapascal Level Pressure on Protein Structure and Function

Information on very high pressure (VHP) effects on proteins is limited and therefore effects of VHP on chemistry, structure and function of two model proteins in medical use were studied. VHP (8 GPa) application to l-asparaginase (L-ASNase) resulted in faster mobility on clear native gels. VHP induced generation of lower-MW forms of L-ASNase but VHP treatment did not deteriorate asparaginase activity. Electrophoretic patterns in native and denaturing gels were comparable for untreated and pressurized recombinant human growth hormone (rhGH). rhGH function, however, was deteriorated as shown by a bioassay. In L-ASNase and rhGH a series of protein modifications and amino acid exchanges (indicating cleavage of covalent bonds) were revealed that may probably lead to functional and conformational changes. The findings have implications in protein chemistry, structure, and function and are useful for designing biotechnological applications of protein products

Effects of Gigapascal Level Pressure on Protein Structure and Function

Information on very high pressure (VHP) effects on proteins is limited and therefore effects of VHP on chemistry, structure and function of two model proteins in medical use were studied. VHP (8 GPa) application to l-asparaginase (L-ASNase) resulted in faster mobility on clear native gels. VHP induced generation of lower-MW forms of L-ASNase but VHP treatment did not deteriorate asparaginase activity. Electrophoretic patterns in native and denaturing gels were comparable for untreated and pressurized recombinant human growth hormone (rhGH). rhGH function, however, was deteriorated as shown by a bioassay. In L-ASNase and rhGH a series of protein modifications and amino acid exchanges (indicating cleavage of covalent bonds) were revealed that may probably lead to functional and conformational changes. The findings have implications in protein chemistry, structure, and function and are useful for designing biotechnological applications of protein products