Related Experiment Video

Updated: Aug 6, 2026

Molecular Analysis of Endothelial-mesenchymal Transition Induced by Transforming Growth Factor-β Signaling
07:49

Molecular Analysis of Endothelial-mesenchymal Transition Induced by Transforming Growth Factor-β Signaling

Published on: August 3, 2018

Transforming growth factor-beta isoform expression in insulin-like growth factor stimulated myogenesis

W J Bosche1, D Z Ewton, J R Florini

  • 1Biology Department, Syracuse University, New York 13244, USA.

Journal of Cellular Physiology
|August 1, 1995
PubMed

Insights

Insulin-like growth factors (IGFs) modulate transforming growth factor beta (TGF-beta) gene expression in myoblasts. IGFs downregulate TGF-beta 3 and TGF-beta 1, impacting myogenic differentiation.

Area of Science:

  • Cell Biology
  • Developmental Biology
  • Molecular Biology

Background:

  • Transforming growth factor betas (TGF-beta) regulate development and morphogenesis.
  • TGF-beta can inhibit or induce myoblast differentiation.
  • Insulin-like growth factors (IGFs) also play a role in myogenesis.

Purpose of the Study:

  • To investigate the effect of IGF treatment on TGF-beta expression and secretion in L6A1 myoblasts.
  • To understand the role of IGFs in modulating TGF-beta gene expression during myogenesis.

Main Methods:

  • Treatment of L6A1 myoblasts with varying concentrations of IGFs.
  • Analysis of TGF-beta 1 and TGF-beta 3 mRNA expression at 24 and 48 hours.
  • Investigation of the involvement of the type 1 IGF receptor and IGF binding proteins.

Main Results:

  • IGF treatment downregulated TGF-beta 3 expression in a concentration-dependent manner.
  • TGF-beta 1 expression was downregulated by IGFs at 48 hours but not at 24 hours.
  • Downregulation was mediated by the type 1 IGF receptor and modulated by secreted IGF binding proteins.
  • Reexpression of TGF-beta 1 and TGF-beta 3 mRNAs occurred after significant morphological differentiation.

Conclusions:

  • IGFs, via the IGF type I receptor, modulate TGF-beta gene expression.
  • This modulation is part of a coordinated mechanism during terminal myogenic differentiation.
  • IGFs and TGF-betas interact to regulate the complex process of myogenesis.

More Related Videos

Suppression of Pro-fibrotic Signaling Potentiates Factor-mediated Reprogramming of Mouse Embryonic Fibroblasts into Induced Cardiomyocytes09:16

Suppression of Pro-fibrotic Signaling Potentiates Factor-mediated Reprogramming of Mouse Embryonic Fibroblasts into Induced Cardiomyocytes

Published on: June 3, 2018

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells06:54

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells

Published on: October 27, 2020

Related Concept Videos

mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
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...
Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

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 rapamycin-insensitive companion...
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

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 are of three kinds RI, RII, and RIII. The RI...
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...