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Related Experiment Video

Updated: Jul 14, 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

The bone morphogenetic protein 1/Tolloid-like metalloproteinases.

Delana R Hopkins¹, Sunduz Keles, Daniel S Greenspan

¹Program in Molecular and Cellular Pharmacology, University of Wisconsin, Madison, WI 53706, USA.

Matrix Biology : Journal of the International Society for Matrix Biology

|June 15, 2007

Summary

Bone morphogenetic protein 1 (BMP1) processes collagen precursors and, with related proteinases, regulates extracellular matrix formation and embryonic development by activating TGFbeta-like proteins.

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Site-Directed Immobilization of Bone Morphogenetic Protein 2 to Solid Surfaces by Click Chemistry

Site-Directed Immobilization of Bone Morphogenetic Protein 2 to Solid Surfaces by Click Chemistry

Published on: March 29, 2018

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Last Updated: Jul 14, 2026

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

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Published on: July 21, 2021

Site-Directed Immobilization of Bone Morphogenetic Protein 2 to Solid Surfaces by Click Chemistry

Site-Directed Immobilization of Bone Morphogenetic Protein 2 to Solid Surfaces by Click Chemistry

Published on: March 29, 2018

Area of Science:

Biochemistry
Developmental Biology
Molecular Biology

Background:

Bone morphogenetic protein 1 (BMP1) cleaves C-propeptides from procollagens I-III.
BMP1 is the prototype of extracellular metalloproteinases regulating extracellular matrix (ECM) formation.
Related Drosophila proteinase Tolloid (TLD) is crucial for dorsal-ventral axis formation.

Purpose of the Study:

To elucidate the broader roles of BMP1/TLD-like proteinases in ECM formation and developmental signaling.
To understand the activation mechanisms of TGFbeta superfamily proteins by these metalloproteinases.

Main Methods:

Literature review of genetic and biochemical studies on BMP1 and TLD.
Analysis of conserved functions across species from Drosophila to humans.
Investigation of proteinase activity in activating growth factors.

Main Results:

BMP1/TLD-like proteinases are conserved and essential for dorsal-ventral patterning.
These proteinases activate BMP2, BMP4, and decapentaplegic via transforming growth factor beta (TGFbeta) signaling.
Evidence suggests these proteinases activate a wider range of TGFbeta superfamily members.

Conclusions:

BMP1/TLD-like proteinases are key regulators of ECM assembly.
They play critical roles in orchestrating ECM formation with growth factor activation.
These proteinases are central to BMP signaling and morphogenetic processes during development.