Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

TGF - β Signaling Pathway

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...

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...

Activation and Inactivation of G Proteins

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...

General Transcription Factors

General Transcription Factors

Tissue-specific transcription factors contribute to diverse cellular functions in mammals. For example, the gene for beta globin, a major component of hemoglobin, is present in all cells of the body. However, it is only expressed in red blood cells because the transcription factors that can bind to the promoter sequences of the beta globin gene are only expressed in these cells. Tissue-specific transcription factors also ensure that mutations in these factors may impair only the function of...

NF-κB-dependent Signaling Pathway

NF-κB-dependent Signaling Pathway

The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
The...

Transcription Factors

Transcription Factors

Tissue-specific transcription factors contribute to diverse cellular functions in mammals. For example, the gene for beta globin, a major component of hemoglobin, is present in all cells of the body. However, it is only expressed in red blood cells because the transcription factors that can bind to the promoter sequences of the beta globin gene are only expressed in these cells. Tissue-specific transcription factors also ensure that mutations in these factors may impair only the function of...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Single-Cell Proteomics Reveals Novel Cell Phenotypes in Marfan Mouse Aneurysm.

Molecular & cellular proteomics : MCP·2026

Same author

Hypercalcemic Crisis in Pregnancy With Acute Respiratory Distress Syndrome Requiring Extracorporeal Membrane Oxygenation.

JCEM case reports·2025

Same author

Collagen type VI regulates TGF-β bioavailability in skeletal muscle in mice.

The Journal of clinical investigation·2025

Same author

Single Cell Proteomics Reveals Novel Cell Phenotypes in Marfan Mouse Aneurysm.

bioRxiv : the preprint server for biology·2025

Same author

Neurological prognosis prediction for cardiac arrest patients using quantitative imaging biomarkers from brain computed tomography.

Physica medica : PM : an international journal devoted to the applications of physics to medicine and biology : official journal of the Italian Association of Biomedical Physics (AIFB)·2024

Same author

Binding requirements for latent transforming growth factor Beta2 activation.

Matrix biology plus·2024

Search research articles

Related Experiment Video

Updated: Apr 12, 2026

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

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

Published on: October 27, 2020

Latent TGF-β-binding proteins.

Ian B Robertson¹, Masahito Horiguchi¹, Lior Zilberberg¹

¹The Department of Cell Biology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.

Matrix Biology : Journal of the International Society for Matrix Biology

|May 12, 2015

Summary

This summary is machine-generated.

Latent transforming growth factor beta binding proteins (LTBPs) are crucial extracellular matrix components. This review details their roles in TGFβ latency, activation, and TGFβ-independent functions in microfibril biology.

Keywords:

Extracellular matrix Latency associated protein Latent TGFβ binding proteins TGFβ activation

More Related Videos

Analysis of Transforming Growth Factor ß Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos

Analysis of Transforming Growth Factor ß Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos

Published on: July 21, 2021

Analysis of the c-KIT Ligand Promoter Using Chromatin Immunoprecipitation

Analysis of the c-KIT Ligand Promoter Using Chromatin Immunoprecipitation

Published on: June 27, 2017

Related Experiment Videos

Last Updated: Apr 12, 2026

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

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

Published on: October 27, 2020

Analysis of Transforming Growth Factor ß Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos

Analysis of Transforming Growth Factor ß Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos

Published on: July 21, 2021

Analysis of the c-KIT Ligand Promoter Using Chromatin Immunoprecipitation

Analysis of the c-KIT Ligand Promoter Using Chromatin Immunoprecipitation

Published on: June 27, 2017

Area of Science:

Biochemistry
Cell Biology
Extracellular Matrix Biology

Background:

Latent transforming growth factor beta binding proteins (LTBPs) are key extracellular matrix (ECM) proteins.
LTBPs interact with fibrillin microfibrils, influencing microfibril biology.
Four LTBP isoforms exist in the human genome: LTBP-1, -2, -3, and -4.

Purpose of the Study:

To review the biology and functions of the four LTBP isoforms.
To explore LTBP roles in transforming growth factor beta (TGFβ) latency and activation.
To highlight TGFβ-independent functions of LTBPs.

Main Methods:

Literature review of studies on LTBP isoforms.
Analysis of LTBP interactions with fibrillin and TGFβ.
Examination of LTBP roles in cellular processes and development.

Main Results:

LTBPs form large latent complexes (LLCs) with TGFβ, maintaining its latency.
LTBP-1 is implicated in TGFβ activation via integrins and other factors.
LTBP-3 plays a role in skeletal and tooth development.
LTBP-2 and LTBP-4 exhibit TGFβ-independent functions in microfibril and elastic fiber assembly.

Conclusions:

LTBPs are multifunctional ECM proteins with diverse roles.
Understanding LTBP functions is crucial for comprehending TGFβ regulation and ECM dynamics.
Further research into LTBP-independent activities may reveal novel therapeutic targets.