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Related Concept Videos

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...
Glucose Homeostasis: Pancreatic Islets and Insulin Secretion01:27

Glucose Homeostasis: Pancreatic Islets and Insulin Secretion

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.
Insulin and C-peptide are co-secreted in...
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...
Insulin: Biosynthesis, Chemistry, and Preparation01:25

Insulin: Biosynthesis, Chemistry, and Preparation

The endoplasmic reticulum (ER) of pancreatic β-cells synthesizes preproinsulin, which consists of a signal peptide, A and B chains, and a C-peptide. Preproinsulin is then cleaved and folded into proinsulin, which translocates to the Golgi apparatus for sorting and packaging into secretory granules. In these granules, enzymatic clipping generates insulin and C-peptide.
Damage or functional impairment of β-cells inhibits insulin production, leading to diabetes. Diabetes treatment primarily uses...
Production of Pharmaceuticals01:30

Production of Pharmaceuticals

Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...

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Related Experiment Video

Updated: Jul 10, 2026

Coculture Analysis of Extracellular Protein Interactions Affecting Insulin Secretion by Pancreatic Beta Cells
05:51

Coculture Analysis of Extracellular Protein Interactions Affecting Insulin Secretion by Pancreatic Beta Cells

Published on: June 15, 2013

Insulin-stimulating protein from human plasma.

N Arakaki, T Oribe, A Ueno

    FEBS Letters
    |November 19, 1984
    PubMed
    Summary

    Researchers isolated a novel insulin-stimulating protein from human plasma. This protein enhances insulin

    Area of Science:

    • Biochemistry
    • Endocrinology
    • Metabolic Research

    Background:

    • Insulin is a key hormone regulating glucose metabolism.
    • Understanding factors that modulate insulin action is crucial for metabolic research.
    • The existence of insulin-modulating proteins in plasma requires further investigation.

    Purpose of the Study:

    • To isolate and characterize a protein from human plasma with insulin-stimulating properties.
    • To investigate the functional role of this protein in glucose metabolism.
    • To determine if the isolated protein directly influences insulin signaling pathways.

    Main Methods:

    • Isolation of the protein using Sephadex G-100 chromatography and reverse-phase HPLC.
    • Characterization of the purified protein using SDS-polyacrylamide gel electrophoresis.

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  • Assessment of the protein's effect on glucose metabolism in rat adipose tissue and adipocytes.
  • Main Results:

    • A single-band protein was successfully isolated from human plasma.
    • The isolated protein exhibited no intrinsic insulin-like activity.
    • The protein significantly enhanced insulin's effect on fatty acid synthesis and glucose utilization in adipose tissue and adipocytes.

    Conclusions:

    • A novel insulin-stimulating protein was identified in human plasma.
    • This protein potentiates insulin action, enhancing glucose metabolism.
    • Further research is warranted to elucidate the precise mechanisms and physiological relevance of this protein.