GPR3 accelerates neurite outgrowth and neuronal polarity formation via PI3 kinase-mediating signaling pathway in cultured primary neurons

2021 ◽  
pp. 103691
Author(s):  
Shigeru Tanaka ◽  
Naoto Shimada ◽  
Hiroko Shiraki ◽  
Tatsuhiro Miyagi ◽  
Kana Harada ◽  
...  
Keyword(s):  
Neurite Outgrowth ◽  
Signaling Pathway ◽  
Pi3 Kinase ◽  
Neuronal Polarity ◽  
Primary Neurons

scholarly journals PI3 kinase signaling pathway in hematopoietic cancers: A glance in miRNA's role

2021 ◽  
Vol 35 (4) ◽  
Author(s):  
Elham Roshandel ◽  
Leila Noorazar ◽  
Behrouz Farhadihosseinabadi ◽  
Mahshid Mehdizadeh ◽  
Mohammad Hossein Kazemi ◽  
...  
Keyword(s):  
Signaling Pathway ◽  
Pi3 Kinase ◽  
Kinase Signaling ◽  
Kinase Signaling Pathway ◽  
Hematopoietic Cancers

scholarly journals Role of the PI3-kinase signaling pathway in trafficking of the surfactant protein A receptor P63 (CKAP4) on type II pneumocytes

2010 ◽  
Vol 299 (6) ◽  
pp. L794-L807 ◽  
Author(s):  
Altaf S. Kazi ◽  
Jian-Qin Tao ◽  
Sheldon I. Feinstein ◽  
Li Zhang ◽  
Aron B. Fisher ◽  
...  
Keyword(s):  
Signaling Pathway ◽  
Protein A ◽  
Surfactant Protein ◽  
Pi3 Kinase ◽  
Surfactant Protein A ◽  
Type Ii Cells ◽  
Type Ii ◽  
Type Ii Pneumocytes ◽  
Kinase Signaling Pathway ◽  
Stimulation Of

Surfactant protein A (SP-A) plays an important role in the maintenance of lung lipid homeostasis. Previously, an SP-A receptor, P63 (CKAP4), on type II pneumocyte plasma membranes (PM) was identified by chemical cross-linking techniques. An antibody to P63 blocked the specific binding of SP-A to pneumocytes and the ability of SP-A to regulate surfactant secretion. The current report shows that another biological activity of SP-A, the stimulation of surfactant uptake by pneumocytes, is inhibited by P63 antibody. cAMP exposure resulted in enrichment of P63 on the cell surface as shown by stimulation of SP-A binding, enhanced association of labeled P63 antibody with type II cells, and promotion of SP-A-mediated liposome uptake, all of which were inhibited by competing P63 antibody. Incubation of A549 and type II cells with SP-A also increased P63 localization on the PM. The phosphatidylinositol 3-kinase (PI3-kinase) signaling pathway was explored as a mechanism for the transport of this endoplasmic reticulum (ER)-resident protein to the PM. Treatment with LY-294002, an inhibitor of the PI3-kinase pathway, prevented the SP-A-induced PM enrichment of P63. Exposure of pneumocytes to SP-A or cAMP activated Akt (PKB). Blocking either PI3-kinase or Akt altered SP-A-mediated lipid turnover. The data demonstrate an important role for the PI3-kinase-Akt pathway in intracellular transport of P63. The results add to the growing body of evidence that P63 is critical for SP-A receptor-mediated interactions with type II pneumocytes and the resultant regulation of surfactant turnover.

Insulin attenuates arsenic-induced neurite outgrowth impairments by activating the PI3K/Akt/SIRT1 signaling pathway

2015 ◽  
Vol 236 (3) ◽  
pp. 138-144 ◽  
Author(s):  
Apichaya Niyomchan ◽  
Piyajit Watcharasit ◽  
Daranee Visitnonthachai ◽  
Benjaporn Homkajorn ◽  
Apinya Thiantanawat ◽  
...  
Keyword(s):  
Neurite Outgrowth ◽  
Signaling Pathway

NADPH-dependent oxidation of CRMP2 through a MICAL1-Prx1 redox relay controls neurite outgrowth

2021 ◽  
Author(s):  
Clara Ortegón Salas ◽  
Yana Bodnar ◽  
Dennis Uhlenkamp ◽  
Katharina Schneider ◽  
Lara Knaup ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Neurite Outgrowth ◽  
Signaling Pathway ◽  
Molecular Oxygen ◽  
Effector Protein ◽  
Post Translational Modifications ◽  
Signal Transducers ◽  
Extracellular Signals ◽  
Cytoskeletal Dynamics ◽  
Redox Switch

Abstract CRMP2/DPYL2 is an effector protein in the semaphorin signaling pathway that controls cytoskeletal dynamics, linking extracellular signals to the formation of axonal networks. CRMP2 is regulated by post-translational modifications including a dithiol-disulfide redox switch. The mechanisms of reduction of this switch were established, the signal-induced oxidation, however, remained unclear. Here, we show that CRMP2 is oxidized through a redox relay involving the flavin-mooxygenase MICAL1 and the peroxidase Prx1 as specific signal transducers. Using molecular oxygen and electrons provided by NADPH, MICAL produces hydrogen peroxide and specifically oxidizes Prx1 through direct interactions between the proteins. Subsequently, Prx1 oxidizes CRMP2. The lack of any components of this redox relay dysregulates neurite outgrowth. Consequently, both oxidation and reduction of CRMP2 require reducing equivalents in the form of NADPH.

Alpha-synuclein promotes early neurite outgrowth in cultured primary neurons

2013 ◽  
Vol 120 (9) ◽  
pp. 1331-1343 ◽  
Author(s):  
Guangwei Liu ◽  
Peng Wang ◽  
Xin Li ◽  
Yaohua Li ◽  
Shengli Xu ◽  
...  
Keyword(s):  
Neurite Outgrowth ◽  
Alpha Synuclein ◽  
Primary Neurons
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