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Related Experiment Video

Updated: May 11, 2026

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

Proteolytic processing regulates placental growth factor activities.

Daniel C Hoffmann¹, Sebastian Willenborg, Manuel Koch

¹Department of Dermatology, University of Cologne, Cologne, Germany.

The Journal of Biological Chemistry

|May 7, 2013

Summary

This summary is machine-generated.

Proteolytic processing by plasmin regulates placental growth factor (PlGF) activity. This study reveals how plasmin digestion of PlGF-2 impacts its interaction with Neuropilin-1, affecting blood vessel formation.

Keywords:

Angiogenesis Mechanism of Growth Factor Regulation PlGF Plasmin Protease Vascular Biology Vascular Endothelial Growth Factor (VEGF)

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Published on: August 2, 2017

Area of Science:

Biochemistry
Molecular Biology
Angiogenesis Research

Background:

Placental growth factor (PlGF) is crucial for blood vessel formation.
The precise mechanisms regulating PlGF's action and biological activity remain unclear.

Purpose of the Study:

To investigate the role of proteolytic processing in regulating PlGF's biological activity.
To elucidate the functional consequences of plasmin-mediated PlGF processing on angiogenesis.

Main Methods:

Plasmin digestion of PlGF-2 to generate a core fragment.
Generation of a truncated PlGF118 isoform.
Comparative analysis of PlGF-1, PlGF-2, and PlGF118 in angiogenic assays.
Investigation of PlGF/Neuropilin-1 binding and function.

Main Results:

Plasmin processing of PlGF-2 yields a core fragment lacking the heparin-binding domain.
The processed PlGF fragment exhibits altered biological activity compared to native PlGF-2.
PlGF-2 promotes endothelial cell chemotaxis and vascular sprouting, which are reduced after plasmin digestion.
Heparin-binding domain interaction with Neuropilin-1 is critical and modulated by plasmin processing.

Conclusions:

Proteolytic processing is a key regulatory mechanism for PlGF biological activity.
Plasmin digestion significantly alters PlGF-mediated angiogenesis by affecting its interaction with Neuropilin-1.
These findings provide new insights into the regulation of PlGF-2/Neuropilin-1 signaling in tissue vascularization.