Effects of taurine acute intake on cortical excitability and post-exercise facilitation: A TMS study.

Taurine (TAU) is one of the most abundant amino acids in the brain. It has many important physiological functions. The effects of TAU supplementation on brain function need to be further characterized in humans. The purpose of this study was to investigate whether a single dose of Taurine (TAU) intake would modulate corticospinal excitability and post-exercise facilitation (PEF) of the motor evoked potentials (MEP).

Vitamin D deficiency in patients with intestinal malabsorption syndromes--think in and outside the gut.

There is a very high prevalence of vitamin D deficiency, which is defined by a serum level of 25-hydroxyvitamin D [25(OH)D] of lower than 20 ng/mL, in all populations of the world. Unfortunately, the prevalence of vitamin D deficiency in patients with intestinal malabsorption syndromes, including cystic fibrosis (CF), celiac disease (CD), short bowel syndrome and inflammatory bowel disease (IBD), is higher than that in the general population, indicating the presence of disease-specific causative factors. In this review, we aimed to present clinical findings to highlight the roles of insufficient exposure to sunlight and inflammation in the development of vitamin D deficiency in patients with intestinal malabsorption syndromes. Furthermore, we aimed to present experimental evidence that supported a role of vitamin D deficiency in the pathogenesis of IBD. Finally, we reviewed clinical intervention strategies aiming to normalize vitamin D status in and even to improve the conditions of patients and to discuss certain issues that needed to be addressed in future research.

Induction of apoptosis in human colon cancer HCT116 cells treated with an extract of the plant product, Chios mastic gum.

A hexane extract of the plant product Chios mastic gum (He-CMG) is demonstrated to kill human colon cancer cells in vitro via the process of anoikis. Specifically, the sequence of events includes He-CMG-induced GI-arrest of the cells, detachment of the cells from the substrate and subsequent apoptosis. Anoikis is dependent on the concentration and duration of treatment with He-CMG. Presence of the pan-caspase inhibitor, Z-VAD-fmk, did not prevent cell detachment, but it did prevent apoptosis of the detached cells indicating that the process of cell detachment, but not apoptosis, is independent of caspase activation. He-CMG-induced apoptosis is associated with activation of the initiator caspases-8, and -9 and the effector caspase-3. Caspases are activated in cells at a relatively long time after detachment, and caspase-3 activation may require caspase-8 or caspase-9 activation, as determined by using HCT116 isogenic clones impaired in apoptosis mechanisms that involve these two caspases. Finally, electron microscopy observations indicated a time-dependent appearance of morphological features both typical and non-typical of apoptosis in cells treated with He-CMG for various periods of time. Taken together, the results demonstrated that He-CMG induces apoptosis in HCT116 cells and, therefore, further in vivo and in vitro studies of the anticancer activities of this plant product are warranted.

SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei.

Signal transducer and activator of transcription (STAT) proteins are both tyrosine- and serine-phosphorylated, mediating signal transduction and gene regulation. Following gene regulation, STAT activity in the nucleus is then terminated by a nuclear protein phosphatase(s), which remains unidentified. Using novel antibody arrays to screen the Stat1-specific protein phosphatase(s), we identified a SHP-2-Stat1 interaction in the A431 cell nucleus. SHP-2 and Stat1 nuclear localization and their association in response to either epidermal growth factor or interferon-gamma (IFNgamma) were confirmed by immunofluorescent staining and affinity precipitation assays. The SHP-2 C-terminal region containing protein-tyrosine phosphatase activity interacted with the C-terminal SH2 transcriptional activation domain of Stat1. In SHP-2-/- mouse fibroblast cells, Stat1 phosphorylation at both the tyrosine residue Tyr(701) and the serine residue Ser(727) by IFNgamma was enhanced and prolonged. Consistently, purified GST-SHP-2 dephosphorylated Stat1 at both tyrosine and serine residues when immunoprecipitated phospho-Stat1 or a peptide corresponding to the sequence surrounding Tyr(P)(701) or Ser(P)(727) of Stat1 was used as the substrate. Overexpression of SHP-2 in 293T cells inhibited IFNgamma-dependent Stat1 phosphorylation and suppressed Stat1-dependent induction of luciferase activity. Our findings demonstrate that SHP-2 is a dual-specificity protein phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues and plays an important role in modulating STAT function in gene regulation.