Rheological properties of cross-linked hyaluronan-gelatin hydrogels for tissue engineering

Hydrogels that mimic the natural extracellular matrix (ECM) are used in three-dimensional cell culture, cell therapy, and tissue engineering. A semi-synthetic ECM based on cross-linked hyaluronana offers experimental control of both composition and gel stiffness. The mechanical properties of the ECM in part determine the ultimate cell phenotype. We now describe a rheological study of synthetic ECM hydrogels with storage shear moduli that span three orders of magnitude, from 11 to 3 500 Pa, a range important for engineering of soft tissues. The concentration of the chemically modified HA and the cross-linking density were the main determinants of gel stiffness. Increase in the ratio of thiol-modified gelatin reduced gel stiffness by diluting the effective concentration of the HA component.     

The TRH-like peptide pGlu-Glu-ProNH2 is present in the porcine pituitary but not in reproductive tissues.

The peptide pGlu-Glu-ProNH2, which differs from thyrotrophin-releasing hormone (TRH) by only one amino acid, was initially detected and characterised in the rabbit prostate complex and more recently in human semen and rat pituitary. A previous study reported that TRH and a homologous peptide were present in a range of porcine tissues and it was of interest to further characterise these peptides. In this study, high levels of TRH-immunoreactivity have been demonstrated in the porcine pituitary, the majority of which was authentic TRH; although 9% was found to be chromatographically identical to pGlu-Glu-ProNH2. In contrast, TRH-immunoreactivity was not detected in follicular fluid, ovary or prostate. The unexpected finding that pGlu-Glu-ProNH2 is present in the porcine pituitary but absent from regions of the reproductive tract may be of biological significance.     

Deletion of pgi alters tryptophan biosynthesis in a genetically engineered strain of Escherichia coli.

Deletion of the structural gene for phosphoglucose isomerase (pgi) of Escherichia coli dramatically alters the path of glucose catabolism by diverting carbon into the hexose monophosphate shunt. The effect of this genetic alteration on the conversion of glucose to tryptophan by strains optimized for the biosynthesis of this amino acid was determined by using 13C-nuclear magnetic resonance spectroscopy in vivo. Pgi- strains converted glucose to tryptophan almost twice as efficiently as did their Pgi+ counterparts.