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Related Experiment Video

Updated: May 27, 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

Designer TGFβ superfamily ligands with diversified functionality.

George P Allendorph¹, Jessica D Read, Yasuhiko Kawakami

¹Joint Center for Biosciences at Lee Gil Ya Cancer and Diabetes Institute, Gachon University for Medicine and Science, Incheon, Korea.

|November 11, 2011

Summary

This summary is machine-generated.

We engineered novel Transforming Growth Factor-beta (TGFβ) superfamily ligands using the RASCH strategy. These chimeric proteins offer unique signaling properties and improved therapeutic potential for various biological applications.

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Published on: July 21, 2021

Area of Science:

Biochemistry
Molecular Biology
Protein Engineering

Background:

Transforming Growth Factor-beta (TGFβ) superfamily ligands are crucial in development and cellular processes.
These ligands, including Activins, GDFs, and BMPs, are promising targets for protein-based therapeutics.

Purpose of the Study:

To develop a strategy (RASCH) for engineering chemically-refoldable TGFβ superfamily ligands with novel signaling properties.
To create and characterize new chimeric TGFβ ligands for expanded biological and clinical applications.

Main Methods:

Development of the RASCH (Random Assembly of Segmental Chimera and Heteromer) strategy.
Engineering of chimeric ligands (e.g., AB208 from Activin-βA and BMP-2).
Assessment of refolding characteristics and signaling pathways (e.g., Smad1) of engineered ligands.

Main Results:

The engineered ligand AB208 demonstrated BMP-2 refolding with Activin-like signaling.
New ligands (AB204, AB211, AB215) showed enhanced Smad1 pathway activation and Noggin insensitivity.
Incorporation of a BMP-2 N-terminal segment enabled refolding of BMP-9.

Conclusions:

The RASCH strategy successfully generates chemically-refoldable chimeric TGFβ ligands.
Engineered ligands possess unique signaling profiles, expanding the functional repertoire of TGFβ superfamily proteins.
These novel ligands hold potential for diverse biological and clinical applications.