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Related Concept Videos

Insulin: The Receptor and Signaling Pathways01:28

Insulin: The Receptor and Signaling Pathways

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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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Insulin Secretory Vesicles01:05

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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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Glucagon-like Receptor Agonists01:24

Glucagon-like Receptor Agonists

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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.
GLP-1, when administered in high doses intravenously, triggers insulin secretion, inhibits glucagon release, slows gastric emptying, reduces food intake, and restores normal insulin secretion. However, its rapid inactivation by...
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TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

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The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
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Insulin: Biosynthesis, Chemistry, and Preparation01:25

Insulin: Biosynthesis, Chemistry, and Preparation

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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...
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PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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Related Experiment Video

Updated: Mar 26, 2026

Precise Visualization of Insulin Receptors A and B in Murine Brain with an RNA In Situ Hybridization Assay
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Precise Visualization of Insulin Receptors A and B in Murine Brain with an RNA In Situ Hybridization Assay

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Insulin-Like Growth Factor Binding Proteins--an Update.

Leon A Bach

    Pediatric Endocrinology Reviews : PER
    |February 5, 2016
    PubMed
    Summary

    Insulin-like growth factor binding proteins (IGFBPs) regulate growth and development by modulating insulin-like growth factor (IGF) actions. Understanding IGFBP functions offers insights into diseases and potential therapeutics.

    Area of Science:

    • Endocrinology
    • Molecular Biology
    • Cell Biology

    Background:

    • The insulin-like growth factor (IGF) system is crucial for growth and development.
    • Dysregulation of the IGF system is linked to various diseases.
    • IGF activity is modulated by six high-affinity IGF binding proteins (IGFBPs).

    Purpose of the Study:

    • To elucidate the multifaceted roles of IGFBPs.
    • To explore both IGF-dependent and IGF-independent functions of IGFBPs.
    • To highlight the regulatory mechanisms governing IGFBP activity.

    Main Methods:

    • Review of existing literature on IGFBP functions.
    • Analysis of IGFBP interactions with IGF and non-IGF ligands.
    • Examination of regulatory mechanisms including transcription, post-translational modification, and proteolysis.

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    Main Results:

    • IGFBPs primarily inhibit IGF actions but can enhance them contextually.
    • IGFBPs exert significant IGF-independent effects on cell proliferation, survival, and migration.
    • IGFBP activity is controlled through complex transcriptional and post-translational pathways.

    Conclusions:

    • A comprehensive understanding of IGFBP actions in vivo is essential.
    • Investigating the balance of IGFBP functions may reveal disease mechanisms.
    • IGFBPs represent promising targets for novel therapeutic strategies.