scholarly journals Polarization of PI3K Activity Initiated by Ooplasmic Segregation Guides Nuclear Migration in the Mesendoderm

2015 ◽  
Vol 35 (3) ◽  
pp. 333-343 ◽  
Author(s):  
Naohito Takatori ◽  
Kouhei Oonuma ◽  
Hiroki Nishida ◽  
Hidetoshi Saiga
Genetics ◽  
1976 ◽  
Vol 82 (3) ◽  
pp. 423-428
Author(s):  
Celia Dubovoy

ABSTRACT Twelve mutations affecting nuclear migration, a major developmental phase in Schizophyllum commune, display a complex pattern of complementation and recombination. They are expressed only when a genetic factor controlling this phase of development, the B incompatibility factor, is operative. All twelve mutations are linked to the B factor, nine in a cluster and three in distinct loci outside the cluster. A linear map cannot be constructed from the frequency of recombination. Complementation maps are not linear. There is little correlation between the complementation groups and the groups based on recombination. Many pairs of mutations that do not complement recombine with frequencies of 1.1% to 26.9%. The genes represented by the twelve mutations are located in a linked group of about 18 known genes involved in the specific phase of development controlled by the B factor.


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Samir Sissaoui ◽  
Stuart Egginton ◽  
Ling Ting ◽  
Asif Ahmed ◽  
Peter W. Hewett

AbstractPlacenta growth factor (PlGF) is a pro-inflammatory angiogenic mediator that promotes many pathologies including diabetic complications and atherosclerosis. Widespread endothelial dysfunction precedes the onset of these conditions. As very little is known of the mechanism(s) controlling PlGF expression in pathology we investigated the role of hyperglycaemia in the regulation of PlGF production in endothelial cells. Hyperglycaemia stimulated PlGF secretion in cultured primary endothelial cells, which was suppressed by IGF-1-mediated PI3K/Akt activation. Inhibition of PI3K activity resulted in significant PlGF mRNA up-regulation and protein secretion. Similarly, loss or inhibition of Akt activity significantly increased basal PlGF expression and prevented any further PlGF secretion in hyperglycaemia. Conversely, constitutive Akt activation blocked PlGF secretion irrespective of upstream PI3K activity demonstrating that Akt is a central regulator of PlGF expression. Knock-down of the Forkhead box O-1 (FOXO1) transcription factor, which is negatively regulated by Akt, suppressed both basal and hyperglycaemia-induced PlGF secretion, whilst FOXO1 gain-of-function up-regulated PlGF in vitro and in vivo. FOXO1 association to a FOXO binding sequence identified in the PlGF promoter also increased in hyperglycaemia. This study identifies the PI3K/Akt/FOXO1 signalling axis as a key regulator of PlGF expression and unifying pathway by which PlGF may contribute to common disorders characterised by endothelial dysfunction, providing a target for therapy.


2008 ◽  
Vol 377 (1) ◽  
pp. 181-186 ◽  
Author(s):  
Daniel Sagan ◽  
Friederike Eckardt-Schupp ◽  
Hedda Eichholtz-Wirth

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