scholarly journals Sustained Stimulation of β2AR Inhibits Insulin Signaling in H9C2 Cardiomyoblast Cells Through the PKA-Dependent Signaling Pathway

2020 ◽  
Vol Volume 13 ◽  
pp. 3887-3898
Author(s):  
Jinli Pei ◽  
Zhengpan Xiao ◽  
Ziyi Guo ◽  
Yechun Pei ◽  
Shuangshuang Wei ◽  
...  
2013 ◽  
Vol 288 (13) ◽  
pp. 9313-9320 ◽  
Author(s):  
Xuefeng Yang ◽  
Shuang Mei ◽  
Xiaolei Wang ◽  
Xiang Li ◽  
Rui Liu ◽  
...  

Diabetes ◽  
1996 ◽  
Vol 45 (12) ◽  
pp. 1798-1804 ◽  
Author(s):  
D. E. Estrada ◽  
H. S. Ewart ◽  
T. Tsakiridis ◽  
A. Volchuk ◽  
T. Ramlal ◽  
...  

Blood ◽  
2009 ◽  
Vol 113 (15) ◽  
pp. 3577-3584 ◽  
Author(s):  
Lurong Lian ◽  
Yanfeng Wang ◽  
Matthew Flick ◽  
John Choi ◽  
Edward W. Scott ◽  
...  

AbstractPleckstrin, the platelet and leukocyte C kinase substrate, is a prominent substrate of PKC in platelets, monocytes, macrophages, lymphocytes, and granulocytes. Pleckstrin accounts for 1% of the total protein in these cells, but it is best known for containing the 2 prototypic Pleckstrin homology, or PH, domains. Overexpressed pleckstrin can affect polyphosphoinositide second messenger–based signaling events; however, its true in vivo role has been unknown. Here, we describe mice containing a null mutation within the pleckstrin gene. Platelets lacking pleckstrin exhibit a marked defect in exocytosis of δ and α granules, αIIbβ3 activation, actin assembly, and aggregation after exposure to the PKC stimulant, PMA. Pleckstrin-null platelets aggregate normally in response to thrombin, but they fail to aggregate in response to thrombin in the presence of PI3K inhibitors, suggesting that a PI3K-dependent signaling pathway compensates for the loss of pleckstrin. Although pleckstrin-null platelets merged their granules in response to stimulation of PKC, they failed to empty their contents into the open canalicular system. This might be attributable to impaired actin assembly present in cells lacking pleckstrin. These data show that pleckstrin regulates the fusion of granules to the cell membrane and is an essential component of PKC-mediated exocytosis.


Diabetes ◽  
2018 ◽  
Vol 67 (Supplement 1) ◽  
pp. 1730-P
Author(s):  
RASHEED AHMAD ◽  
NADEEM AKHTER ◽  
SHIHAB P. KOCHUMON ◽  
AREEJ ABU ALROUB ◽  
REEBY S. THOMAS ◽  
...  

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