Proteomics

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A disintegrin-like and metalloproteinase domain with thrombospondin motif 18 (ADAMTS18) cleaves fibronectin and regulates its fibrillogenesis

ABSTRACT: Remodelling of the extracellular matrix (ECM) plays a crucial role in the development, maintenance and repair of all tissues. Therefore, identifying the regulators of this process is essential for understanding the mechanisms of tissue homeostasis. Among these regulators, A disintegrin and metalloproteinase with a thrombospondin motif 18 (ADAMTS18) has been implicated in fibronectin (FN) matrix regulation. However, how ADAMTS18 influences endothelial specific functions and its role in ECM maturation, particularly in the regulation of FN fibrillogenesis, remains unclear. In this study, using mass spectrometry, we identified two sites in FN that are proteolytically cleaved by ADAMTS18, including a cleavage site in the linker FN-I5-6. Cleavage at this site generated FN molecules lacking the N-terminal FN-I1-5 (29kDa) fragment that is known to be essential for FN fibrillogenesis.

ORGANISM(S): Homo Sapiens

SUBMITTER: Mikko Gynther  

PROVIDER: PXD060097 | panorama | Tue Feb 10 00:00:00 GMT 2026

REPOSITORIES: PanoramaPublic

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A disintegrin and metalloproteinase with thrombospondin motifs 18 (ADAMTS18) cleaves fibronectin and negatively regulates its fibrillogenesis.

Barbiera Maria M   Gynther Mikko M   Terasaki Tetsuya T   Jauhiainen Suvi S   Laakkonen Johanna P JP   Jeltsch Michael M   Ylä-Herttuala Seppo S   Laham-Karam Nihay N  

The Journal of biological chemistry 20251022 12

Remodeling of the extracellular matrix (ECM) plays a crucial role in the development, maintenance, and repair of all tissues. Therefore, identifying the regulators of this process is essential. Among these, A disintegrin and metalloproteinase with thrombospondin motifs 18 (ADAMTS18) has been implicated in fibronectin (FN) matrix regulation. Knockout of ADAMTS18, either in mouse models or in vitro, was shown to lead to FN accumulation, mutation in epithelial branching, and reduction in endothelia  ...[more]

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