Linoleic Acid Activates GPR40/FFA1 and Phospholipase C to Increase [Ca2+]i Release and Insulin Secretion in Islet Beta-Cells

2012 ◽  
Vol 27 (1) ◽  
pp. 18-23 ◽  
Author(s):  
Yi-jun Zhou ◽  
Yu-ling Song ◽  
Hui Zhou ◽  
Yan Li
1991 ◽  
Vol 88 (6) ◽  
pp. 2070-2074 ◽  
Author(s):  
J. Allison ◽  
L. Malcolm ◽  
J. Culvenor ◽  
R. K. Bartholomeusz ◽  
K. Holmberg ◽  
...  

1997 ◽  
Vol 272 (30) ◽  
pp. 18621-18627 ◽  
Author(s):  
Richard J. Noel ◽  
Peter A. Antinozzi ◽  
J. Denis McGarry ◽  
Christopher B. Newgard

2016 ◽  
Vol 237 ◽  
pp. 98-108 ◽  
Author(s):  
Na Wang ◽  
De-yu Guo ◽  
Xiong Tian ◽  
Hao-peng Lin ◽  
Yun-pan Li ◽  
...  

2020 ◽  
Author(s):  
Martin Neukam ◽  
Katharina Ganß ◽  
Jovana Vasiljević ◽  
Johannes Broichhagen ◽  
Kai Johnsson ◽  
...  

AbstractPancreatic islet beta cells employ secretory granules for the storage and glucose-stimulated release of the hormone insulin. The competence of an insulin granule for exocytosis depends on spatial and temporal variables such as its proximity to the plasma membrane as well as its age, with newly-generated granules being preferentially released. The molecular underpinnings for the control of these variables remain largely unknown and their uncovering is of high relevance for the study of diabetes, which results from deficient insulin secretion. However, we still lack a comprehensive view about the molecular composition of the insulin granules and how this may change over their lifetime. Here we report a strategy for the background-free purification of insulin secretory granules of distinct age from insulinoma INS-1 cells. We show that utilization of an immuno-based affinity approach for pulse-chase labeled insulin secretory granules, produces a highly enriched granular fraction. Our approach precludes typical contaminants from the solid phase and may be designed to purify secretory granules of a distinct age.


Sign in / Sign up

Export Citation Format

Share Document