Effects of retinoic acid on the synthesis of selenoprotein and the antioxidative indices of bovine mammary epithelial cells in vitro
CZECH JOURNAL OF ANIMAL SCIENCE
Authors: Jin, L.; Yan, S.; Shi, B.; Sheng, R.; Shi, H.; Zhao, Y.; Li, J.
Abstract
The present study was conducted to examine the effects of retinoic acid (RA) on the synthesis of selenoprotein and the antioxidative indices of bovine mammary epithelial cells (BMEC) in vitro and to explore the antioxidative mechanisms of RA in the BMEC. The subconfluenced BMEC were divided into six treatments with six replicates per treatment and cultured in a Dulbecco's Modified Eagle's Medium/F12 media (10% fetal bovine serum, 5 mu g/ml ovine prolactin, 10 ng/ml epidermal growth factor, 1 g/ml hydrocortisone, 0.5% insulin-transferrin-selenium) containing different levels of RA (0 (control), 0.05, 0.1, 0.2, 1 or 2 mu g/ml) for 24 h. Addition of RA promoted the proliferation of BMEC, increased the activities of catalase, superoxide dismutase, total antioxidant capacity, glutathione peroxidase (GPX), thioredoxin reductase (TRXR), and the content of selenoprotein P (SELP) in a dose-dependent manner (P < 0.05). The optimal RA dose was 1 mu g/ml. However, positive effect of RA tended to be suppressed when RA was increased to 2 mu g/ml. The expressions of mRNA and protein of GPX in BMEC were up-regulated by RA in a quadratic dose-response relationship (P < 0.01), and the addition of 1 mu g/ml RA showed the best effect. The mRNA expressions of TRXR1 and SELP as well as the protein expression of TRXR1 were higher at 1-2 mu g/ml RA. These results suggested that RA promoted antioxidant function of BMEC by regulating the synthesis of selenoprotein including GPX, TRXR, and SELP in vitro.
Silk-elastinlike protein polymer hydrogels: Influence of monomer sequence on physicochemical properties
POLYMER
Authors: Dandu, Ramesh; Von Cresce, Arthur; Briber, Robert; Dowell, Paul; Cappello, Joseph; Ghandehari, Hamidreza
Abstract
Silk-elastinlike protein polymer, SELP-815K, with eight silk and fifteen elastin units and a lysine (K) modified elastin, was genetically engineered with longer silk and elastin units compared to existing hydrogel forming analogs (SELP-415K and SELP-47K). Hydrogels of the three SELPs (with similar MWs) were investigated for their structure-function relationships. Results indicate that equilibrium swelling ratio in these hydrogels is a function of polymer structure, concentration, cure time and ionic strength of media. Swelling was not influenced by the changes in pH. Storage moduli observed by dynamic mechanical analysis and the Debye-Bueche correlation length obtained from small-angle neutron scattering provided structural insight that suggests the cross-linking densities in these hydrogels follow the order SELP-47K > SELP-815K > SELP-415K. These results allude to the importance of the length of elastin blocks in governing the spacing of the cross-linked hydrogel network and that of silk in governing the stiffness of their 3-dimensional structures. (C) 2008 Elsevier Ltd. All rights reserved.