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Insulin Secretory Vesicles01:05

Insulin Secretory Vesicles

Insulin secretory vesicles release insulin to stimulate blood glucose uptake and regulate carbohydrate metabolism. When the blood glucose levels increase, glucose enters the pancreatic β-islet cells through glucose transporters. Once inside, glucose is metabolized through glycolysis, the citric acid cycle, and the electron transport chain, producing ATP. This increase in ATP concentration closes ATP-sensitive potassium channels, leading to depolarization of the membrane and the opening of...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Insulin: The Receptor and Signaling Pathways01:28

Insulin: The Receptor and Signaling Pathways

Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but this inhibition is released...
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...

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Related Experiment Video

Updated: May 20, 2026

Imaging Calcium Dynamics in Subpopulations of Mouse Pancreatic Islet Cells
08:03

Imaging Calcium Dynamics in Subpopulations of Mouse Pancreatic Islet Cells

Published on: November 26, 2019

Calcium-sensing receptor activation increases cell-cell adhesion and β-cell function.

Claire E Hills1, Mustafa Y G Younis, Jeanette Bennett

  • 1Schools of Life Sciences, University of Warwick, Coventry, UK.

Cellular Physiology and Biochemistry : International Journal of Experimental Cellular Physiology, Biochemistry, and Pharmacology
|July 27, 2012
PubMed
Summary
This summary is machine-generated.

Activation of the calcium-sensing receptor (CaR) in pancreatic beta-cells enhances cell-to-cell communication and insulin secretion. CaR activation increases E-cadherin, improving cell tethering and calcium signaling for better secretory function.

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Confocal Laser Scanning Microscopy of Calcium Dynamics in Acute Mouse Pancreatic Tissue Slices

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Last Updated: May 20, 2026

Imaging Calcium Dynamics in Subpopulations of Mouse Pancreatic Islet Cells
08:03

Imaging Calcium Dynamics in Subpopulations of Mouse Pancreatic Islet Cells

Published on: November 26, 2019

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Analysis of Beta-cell Function Using Single-cell Resolution Calcium Imaging in Zebrafish Islets

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Confocal Laser Scanning Microscopy of Calcium Dynamics in Acute Mouse Pancreatic Tissue Slices
10:49

Confocal Laser Scanning Microscopy of Calcium Dynamics in Acute Mouse Pancreatic Tissue Slices

Published on: April 13, 2021

Area of Science:

  • Endocrinology
  • Cell Biology
  • Molecular Biology

Background:

  • The calcium-sensing receptor (CaR) is present in pancreatic beta-cells.
  • CaR is believed to mediate cell-to-cell communication and enhance insulin secretion.
  • The precise mechanisms by which CaR activation improves beta-cell function remain unclear.

Purpose of the Study:

  • To investigate how CaR activation influences pancreatic beta-cell function.
  • To elucidate the molecular mechanisms underlying CaR-mediated improvements in beta-cell communication and secretion.

Main Methods:

  • Utilized immunocytochemistry and western blotting to confirm CaR expression in MIN6 beta-cell lines.
  • Employed the calcimimetic R568 to specifically activate CaR at physiological calcium concentrations.
  • Assessed cell proliferation using BrdU incorporation and cytosolic calcium changes via fura-2 microfluorimetry.
  • Measured E-cadherin expression and functional cell tethering using AFM-single-cell-force spectroscopy.

Main Results:

  • CaR activation for 48 hours significantly increased E-cadherin expression (206±41%) and L-type voltage-dependent calcium channel (VDCC) expression (70%).
  • Observed a 30% enhancement in cell-cell tethering and elevated basal-to-peak amplitude of ATP- and tolbutamide-evoked cytosolic calcium.
  • CaR activation also promoted beta-cell proliferation in a dose-dependent manner with PD98059 and SU1498.

Conclusions:

  • CaR activation enhances functional tethering between beta-cells via E-cadherin.
  • Increased L-type VDCC expression and potentiated secretagogue-evoked calcium signaling contribute to improved beta-cell function.
  • Findings suggest a paracrine mechanism where co-released calcium activates CaR on neighboring cells, ensuring efficient insulin secretion.