Characterization of ADAMTS9 proteoglycanase activity: Comparison with ADAMTS1, ADAMTS4, and ADAMTS5.

ABSTRACT: A Disintegrin-like And Metalloprotease domain with Thrombospondin type I motifs (ADAMTS) 9 has essential, non-redundant roles during embryogenesis. Adamts9 null murine embryos die prior to completing gastrulation. Unusually, for a protease, Adamts9 haploinsufficiency results in cardiovascular and ocular anomalies. ADAMTS9 is required for proteostasis of versican, a widely distributed large aggregating proteoglycan abundant in the provisional extracellular matrix during embryogenesis. Despite its importance, ADAMTS9 proteoglycanase activity has undergone limited characterization, especially in comparison to ADAMTS1, ADAMTS4, and ADAMTS5, due to difficulties in expressing and purifying the >200 kDa full-length form of ADAMTS9. Like ADAMTS1, ADAMTS4, and ADAMTS5, ADAMTS9 cleaves versican V1 i

SUBMITTER: Martin DR 

PROVIDER: S-EPMC12226136 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature