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Updated: Dec 4, 2025

Induction of Endothelial Differentiation in Cardiac Progenitor Cells Under Low Serum Conditions

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Published on: January 7, 2019

Engineering Stem Cell Factor Ligands with Different c-Kit Agonistic Potencies.

Tal Tilayov¹, Tal Hingaly¹, Yariv Greenshpan²

¹Avram and Stella Goldstein-Goren Department of Biotechnology Engineering and the National Institute of Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer-Sheva 8410501, Israel.

Molecules (Basel, Switzerland)

|October 24, 2020

Summary

This summary is machine-generated.

Engineered stem cell factor (SCF) variants with altered self-association demonstrate improved c-Kit receptor tyrosine kinase (RTK) activation. Monomeric SCF variants show superior agonistic potency compared to wild-type dimeric SCF.

Keywords:

agonistic activity angiogenesis binding affinity directed evolution protein engineering protein-protein interactions receptor tyrosine kinases

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Last Updated: Dec 4, 2025

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Published on: January 13, 2023

Area of Science:

Biochemistry
Molecular Biology
Cell Signaling

Background:

Receptor tyrosine kinases (RTKs) are crucial for cellular processes, including regeneration and cancer.
c-Kit, a key RTK, is involved in normal and neoplastic cell functions, making it a therapeutic target.
Stem cell factor (SCF) is the ligand for c-Kit, and its self-association influences c-Kit activation.

Purpose of the Study:

To engineer stem cell factor (SCF) variants with modified self-association properties.
To investigate the impact of SCF self-association on c-Kit binding affinity and activation potency.
To understand the structure-function dynamics between SCF variants and c-Kit.

Main Methods:

Directed evolution was used to create a library of SCF mutants (SCF_M).
Yeast display technology was employed for screening SCF variants.
Structural studies, in vitro binding assays, and functional angiogenesis assays were conducted.

Main Results:

Specific SCF variants exhibited altered dimerization potential and increased affinity for c-Kit.
A monomeric SCF variant demonstrated superior agonistic potency compared to wild-type SCF and high-affinity dimeric variants.
Monomeric SCF ligands effectively induced receptor dimerization and activation, outperforming dimeric ligands.

Conclusions:

SCF self-association significantly impacts c-Kit activation potency.
Monomeric SCF variants can achieve superior c-Kit activation compared to dimeric forms.
These findings offer insights into ligand-receptor interactions and RTK activation mechanisms.