Secretory phospholipase A2 is released from pancreatic β-cells and stimulates insulin secretion via inhibition of ATP-dependent K+ channels

2003 ◽  
Vol 310 (2) ◽  
pp. 274-279 ◽  
Author(s):  
Kirstine Juhl ◽  
Alexander M Efanov ◽  
Hervør L Olsen ◽  
Jesper Gromada
Keyword(s):  
Insulin Secretion ◽  
Phospholipase A2 ◽  
Secretory Phospholipase A2 ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
K Channels ◽  
Secretory Phospholipase

scholarly journals The dual role of group V secretory phospholipase A2 in pancreatic β-cells

Endocrine ◽  
2017 ◽  
Vol 58 (1) ◽  
pp. 47-58 ◽  
Author(s):  
Preetha Shridas ◽  
Victoria P. Noffsinger ◽  
Andrea C. Trumbauer ◽  
Nancy R. Webb
Keyword(s):  
Phospholipase A2 ◽  
Dual Role ◽  
Secretory Phospholipase A2 ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Group V ◽  
Secretory Phospholipase

Inhibition of voltage-gated K+ channels mediates docosahexaenoic acid-stimulated insulin secretion in rat pancreatic β-cells

2020 ◽  
Vol 11 (10) ◽  
pp. 8893-8904
Author(s):  
Tao Bai ◽  
Huanhuan Yang ◽  
Hui Wang ◽  
Linping Zhi ◽  
Tao Liu ◽  
...  
Keyword(s):  
Insulin Secretion ◽  
Docosahexaenoic Acid ◽  
Signaling Pathway ◽  
Vital Role ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
K Channels ◽  
Voltage Gated ◽  
Kv Channels

Kv channels play a vital role in DHA-augmented insulin secretion through GPR40/AC/cAMP/PLC signaling pathway in rat pancreatic β-cells.

scholarly journals Somatostatin Inhibits Oxidative Respiration in Pancreatic β-Cells

Endocrinology ◽  
2006 ◽  
Vol 147 (3) ◽  
pp. 1527-1535 ◽  
Author(s):  
Mathew Daunt ◽  
Oliver Dale ◽  
Paul A. Smith
Keyword(s):  
Insulin Secretion ◽  
Glucose Metabolism ◽  
Somatostatin Receptor ◽  
Katp Channels ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
K Channels ◽  
Min6 Cells ◽  
Voltage Gated ◽  
Mouse Islets

Somatostatin potently inhibits insulin secretion from pancreatic β-cells. It does so via activation of ATP-sensitive K+-channels (KATP) and G protein-regulated inwardly rectifying K+-channels, which act to decrease voltage-gated Ca2+-influx, a process central to exocytosis. Because KATP channels, and indeed insulin secretion, is controlled by glucose oxidation, we investigated whether somatostatin inhibits insulin secretion by direct effects on glucose metabolism. Oxidative metabolism in β-cells was monitored by measuring changes in the O2 consumption (ΔO2) of isolated mouse islets and MIN6 cells, a murine-derived β-cell line. In both models, glucose-stimulated ΔO2, an effect closely associated with inhibition of KATP channel activity and induction of electrical activity (r > 0.98). At 100 nm, somatostatin abolished glucose-stimulated ΔO2 in mouse islets (n = 5, P < 0.05) and inhibited it by 80 ± 28% (n = 17, P < 0.01) in MIN6 cells. Removal of extracellular Ca2+, 5 mm Co2+, or 20 μm nifedipine, conditions that inhibit voltage-gated Ca2+ influx, did not mimic but either blocked or reduced the effect of the peptide on ΔO2. The nutrient secretagogues, methylpyruvate (10 mm) and α-ketoisocaproate (20 mm), also stimulated ΔO2, but this was unaffected by somatostatin. Somatostatin also reversed glucose-induced hyperpolarization of the mitochondrial membrane potential monitored using rhodamine-123. Application of somatostatin receptor selective agonists demonstrated that the peptide worked through activation of the type 5 somatostatin receptor. In conclusion, somatostatin inhibits glucose metabolism in murine β-cells by an unidentified Ca2+-dependent mechanism. This represents a new signaling pathway by which somatostatin can inhibit cellular functions regulated by glucose metabolism.

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