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Related Concept Videos

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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...
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The pancreatic islets comprising only 1%-2% of the volume are highly vascularized and innervated mini-organs. They contain five endocrine cell types, including β cells that secrete insulin, which is synthesized as a single polypeptide chain, preproinsulin, processed to proinsulin, and finally to insulin and C-peptide. This process is complex and regulated, involving the Golgi complex, the endoplasmic reticulum, and the secretory granules of the β cell.
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Incretins include glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), which stimulate insulin secretion post-meals. In type 2 diabetes, GIP's efficacy is reduced, making GLP-1 a viable drug target. GIP originates from preproGIP.
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Insulin: The Receptor and Signaling Pathways01:28

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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...
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cAMP-dependent Protein Kinase Pathways01:25

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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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Insulin is released by beta cells of the pancreas when blood glucose levels are high. It facilitates glucose absorption and utilization in insulin-dependent cells with insulin receptors on their plasma membranes. Insulin promotes glucose uptake by increasing the number of glucose transport proteins in the cell membrane, allowing glucose to enter the cell. As a result, glucose utilization and ATP production are enhanced.
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Updated: Aug 11, 2025

Imaging Calcium Dynamics in Subpopulations of Mouse Pancreatic Islet Cells
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Ca2+-Responsive Glyco-insulin.

Shunliang Wu1,2, Mads Østergaard2, Freja Fredholt3,4

  • 1Biomolecular Nanoscale Engineering Center, University of Copenhagen, Thorvaldsensvej 40, 1871 Frederiksberg, Denmark.

Bioconjugate Chemistry
|February 9, 2023
PubMed
Summary
This summary is machine-generated.

Oligogalacturonic acids (OGAs) conjugated to human insulin (HI) form Ca2+-responsive nanostructures. This glyco-insulin conjugate demonstrates prolonged glucose reduction in vivo, offering a novel stimuli-responsive therapeutic approach.

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Area of Science:

  • Bioconjugation Chemistry
  • Materials Science
  • Nanotechnology

Background:

  • Chemical modification of peptides and proteins, like PEGylation, yields conjugates with altered properties.
  • Existing modifications often lack dynamic or stimuli-responsive characteristics.
  • Stimuli-controlled self-assembly offers a method to dynamically adjust conjugate properties.

Purpose of the Study:

  • To create novel stimuli-responsive glyco-insulin conjugates using oligogalacturonic acids (OGAs).
  • To investigate the self-assembly behavior of OGA-peptide conjugates.
  • To evaluate the in vivo efficacy of OGA-conjugated insulin for glucose regulation.

Main Methods:

  • Conjugation of plant-derived OGAs to human insulin (HI) and model peptides.
  • Characterization of self-assembly using dynamic light scattering (DLS), small-angle X-ray scattering (SAXS), and circular dichroism (CD).
  • In vivo subcutaneous administration studies in a glucose regulation model.

Main Results:

  • OGA-HI conjugates exhibited Ca2+-responsive self-assembly into nanostructures.
  • Self-assembly was dependent on OGA sequence length and divalent cation (Zn2+, Ca2+) concentrations.
  • Subcutaneous administration of OGA12-HI with Zn2+ achieved prolonged blood glucose reduction compared to unmodified HI, despite lower receptor binding affinity.

Conclusions:

  • Oligogalacturonic acid conjugation creates stimuli-responsive glyco-insulin conjugates.
  • These novel conjugates self-assemble into nanostructures modulated by divalent cations.
  • OGA-HI conjugates represent a promising platform for sustained glucose-lowering therapies.