The results showed highly similar reaction patterns in all spine positions, regardless of the location of the silicon panel. Between standing and walking, the main differences were in the lumbar spine. The results suggest a relationship between the chewing and the movement system. However, it must be stated

that this study has no direct clinical impact. The study design cannot determine the causality of the observed associations; also the clinical significance of the small postural changes remains unknown. (C) 2014 Elsevier Inc. All rights reserved.”
“Bolger SJ, Gonzales Hurtado PA, Hoffert JD, Saeed F, Pisitkun T, Knepper MA. Quantitative phosphoproteomics in nuclei of vasopressin-sensitive renal collecting duct cells. Am J Physiol Cell Physiol 303: C1006-C1020, 2012. Cyclopamine inhibitor First published September 19, 2012; doi:10.1152/ajpcell.00260.2012.-Vasopressin GSK2879552 in vitro regulates transport across the collecting duct epithelium in part via effects on gene transcription. Transcriptional regulation occurs partially via changes in phosphorylation

of transcription factors, transcriptional coactivators, and protein kinases in the nucleus. To test whether vasopressin alters the nuclear phosphoproteome of vasopressin-sensitive cultured mouse mpkCCD cells, we used stable isotope labeling and mass spectrometry to Prexasertib order quantify thousands of phosphorylation sites in nuclear extracts and nuclear pellet fractions. Measurements were made in the presence and absence of the vasopressin analog dDAVP. Of the 1,251 sites quantified, 39 changed significantly in response to dDAVP. Network analysis of the regulated proteins revealed two major clusters (“cell-cell adhesion” and “transcriptional regulation”) that were connected to known elements of the vasopressin signaling pathway. The hub proteins for these two clusters were the transcriptional coactivator beta-catenin and the transcription factor c-Jun. Phosphorylation

of beta-catenin at Ser552 was increased by dDAVP [log(2)(dDAVP/vehicle) = 1.79], and phosphorylation of c-Jun at Ser73 was decreased [log2(dDAVP/vehicle) = -0.53]. The beta-catenin site is known to be targeted by either protein kinase A or Akt, both of which are activated in response to vasopressin. The c-Jun site is a canonical target for the MAP kinase Jnk2, which is downregulated in response to vasopressin in the collecting duct. The data support the idea that vasopressin-mediated control of transcription in collecting duct cells involves selective changes in the nuclear phosphoproteome. All data are available to users at http://helixweb.nih.gov/ESBL/Database/mNPPD/.