Silylation of layered double hydroxides via an induced hydrolysis method

A series of layered double hydroxides (LDHs) based composites were synthesized by using induced hydrolysis silylation method (IHS), surfactant precursor method, in-situ coprecipitation method, and direct silylation method. Their structures, morphologies, bonding modes and thermal stabilities can be readily adjusted by changing the parameters during preparation and drying processing of the LDHs. The characterization results show that the direct silylation reaction cannot occur between the dried LDHs and 3-aminopropyltriethoxysilane (APS) in an ethanol medium. However, the condensation reaction can proceed with heating process between adsorbed APS and LDHs plates. While using wet state substrates with and without surfactant and ethanol as the solvent, the silylation process can be induced by hydrolysis of APS on the surface of LDHs plates. Surfactants improve the hydrophobicity of the LDHs during the process of nucleation and crystallization, resulting in fluffy shaped crystals; meanwhile, they occupy the surface –OH positions and leave less “free –OH” available for the silylation reaction, favoring formation of silylated products with a higher population in the hydrolyzed bidentate (T2) and tridentate (T3) bonding forms. These bonding characteristics lead to spherical aggregates and tightly bonded particles. All silylated products show higher thermal stability than those of pristine LDHs.

CD73 and CD29 concurrently mediate the mechanically induced decrease of migratory capacity of mesenchymal stromal cells

The assumption that mesenchymal stromal cell (MSC)-based therapies are capable of augmenting physiological regeneration processes has fostered intensive basic and clinical research activities. However, to achieve sustained therapeutic success in vivo, not only the biological, but also the mechanical microenvironment of MSCs during these regeneration processes needs to be taken into account. This is especially important for e.g., bone fracture repair, since MSCs present at the fracture site undergo significant biomechanical stimulation. This study has therefore investigated cellular characteristics and the functional behaviour of MSCs in response to mechanical loading. Our results demonstrated a reduced expression of MSC surface markers CD73 (ecto-5’-nucleotidase) and CD29 (integrin β1) after loading. On the functional level, loading led to a reduced migration of MSCs. Both effects persisted for a week after the removal of the loading stimulus. Specifi c inhibition of CD73/CD29 demonstrated their substrate dependent involvement in MSC migration after loading. These results were supported by scanning electron microscopy images and phalloidin staining of actin fi laments displaying less cell spreading, lamellipodia formation and actin accumulations. Moreover, focal adhesion kinase and Src-family kinases were identified as candidate downstream targets of CD73/CD29 that might contribute to the mechanically induced decrease in MSC migration. These results suggest that MSC migration is controlled by CD73 CD29, which in turn are regulated by mechanical stimulation of cells. We therefore speculate that MSCs migrate into the fracture site, become mechanically entrapped, and thereby accumulate to fulfil their regenerative functions.

Anion induced displacement studies in naphthalene diimide containing interpenetrated and interlocked structures

This article describes investigations into the development of supramolecular systems capable of sensing anions through either displacement type assays or molecular motion. An electron deficient naphthalene diimide thread and electron rich isophthalamide naphthohydroquinone macrocycle was shown to form a coloured pseudorotaxane assembly. Investigations into the ability of such interpenetrated systems to sense anions colorimetrically were undertaken. Anion complexation to the isophthalamide group of the macrocycle causes displacement of the naphthodiimide thread resulting in the loss of colour. The enhanced mechanically bonded binding strength between the naphthodiimide axle and the naphthohydroquinone groups of the macrocycle wheel in the corresponding rotaxane structure however, was found to negate the anion induced displacement process.

Gonadotropin-induced ovarian cancer cell migration and proliferation require extracellular signal-regulated kinase 1/2 activation regulated by calcium and protein kinase Cδ

The gonadotropin hypothesis proposes that elevated serum gonadotropin levels may increase the risk of epithelial ovarian cancer (EOC). We have studied the effect of treating EOC cell lines (OV207 and OVCAR-3) with FSH or LH. Both gonadotropins activated the mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase 1/2 (ERK1/2) pathway and increased cell migration that was inhibited by the MAPK 1 inhibitor PD98059. Both extra- and intracellular calcium ion signalling were implicated in gonadotropin-induced ERK1/2 activation as treatment with either the calcium chelator EGTA or an inhibitor of intracellular calcium release, dantrolene, inhibited gonadotropin-induced ERK1/2 activation. Verapamil was also inhibitory, indicating that gonadotropins activate calcium influx via L-type voltage-dependent calcium channels. The cAMP/protein kinase A (PKA) pathway was not involved in the mediation of gonadotropin action in these cells as gonadotropins did not increase intracellular cAMP formation and inhibition of PKA did not affect gonadotropin-induced phosphorylation of ERK1/2. Activation of ERK1/2 was inhibited by the protein kinase C (PKC) inhibitor GF 109203X as well as by the PKCδ inhibitor rottlerin, and downregulation of PKCδ was inhibited by small interfering RNA (siRNA), highlighting the importance of PKCδ in the gonadotropin signalling cascade. Furthermore, in addition to inhibition by PD98059, gonadotropin-induced ovarian cancer cell migration was also inhibited by verapamil, GF 109203X and rottlerin. Similarly, gonadotropin-induced proliferation was inhibited by PD98059, verapamil, GF 109203X and PKCδ siRNA. Taken together, these results demonstrate that gonadotropins induce both ovarian cancer cell migration and proliferation by activation of ERK1/2 signalling in a calcium- and PKCδ-dependent manner.