This resulted in an increased DHA/arachidonic acid (AA) ratio in the adipocyte FA secretion profile and in plasma of niacin-treated mice. Interestingly, the DHA metabolite 19,20-dihydroxy docosapentaenoic acid (19,20-diHDPA) was increased in plasma of niacin-treated mice. Both

an increased DHA/AA ratio and increased 19,20-diHDPA are indicative for an anti-inflammatory profile and may indirectly contribute to the atheroprotective lipid and lipoprotein profile associated with prolonged niacin treatment.”
“Neuropsychological studies suggest that patients with left parietal lesions may show impaired localization of parts of either their own or the examiner’s body, despite preserved ability to identify isolated body parts. This deficit, called autotopagnosia, may result from damage to the Body Structural Description (BSD), a representation SYN-117 supplier which codes spatial relationships among body parts. We used functional magnetic resonance imaging to identify the neural mechanisms underlying the BSD. Two human body or building parts (factor: STIMULI) were shown to participants who either identified them or evaluated their distance (factor: TASK). The analysis of the interaction between STIMULI and BYL719 TASK, which isolates the neural mechanism underlying BSD, revealed an activation of left posterior intraparietal sulcus (IPS) when the distance between body parts was evaluated. The results show that

the left IPS processes specifically the information about spatial relationships among body parts and thereby suggest that damage to this area may underlie autotopagnosia.”
“The recently discovered pleckstrin homology (PH) domain leucine-rich repeat protein phosphatase (PHLPP) family is emerging as a central component in suppressing cell survival pathways. Originally discovered in a rational search for a phosphatase that directly dephosphorylates and inactivates Akt,

PHLPP is now known to potently suppress cell survival both by inhibiting proliferative pathways and by promoting apoptotic Crenolanib nmr pathways. In the first instance, PHLPP directly dephosphorylates a conserved regulatory site (termed the hydrophobic motif) on Akt, protein kinase C and S6 kinase, thereby terminating signalling by these pro-survival kinases. In the second instance, PHLPP dephosphorylates and thus activates the pro-apoptotic kinase Mst1, thereby promoting apoptosis. PHLPP is deleted in a large number of cancers and the genetic deletion of one isozyme in a PTEN (phosphatase and tensin homologue located on chromosome 1) +/- (or heterozygous) prostate cancer model results in increased tumourigenesis, underscoring the role of PHLPP as a tumour suppressor. This review summarizes the targets and cellular actions of PHLPP, with emphasis on its role as a tumour suppressor in the oncogenic phosphoinositide 3-kinase (PI3K)/Akt signalling cascade.