Journal article

ADAMTS-9 in mouse cartilage has aggrecanase activity that is distinct from ADAMTS-4 and ADAMTS-5

FM Rogerson, K Last, SB Golub, SJ Gauci, H Stanton, KM Bell, AJ Fosang

International Journal of Molecular Sciences | MDPI | Published : 2019

Open access

Abstract

A disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)-4 and ADAMTS-5 are the principal aggrecanases in mice and humans; however, mice lacking the catalytic domain of both enzymes (TS-4/5∆cat) have no skeletal phenotype, suggesting there is an alternative aggrecanase for modulating normal growth and development in these mice. We previously identified aggrecanase activity that (a) cleaved at E↓G rather than E↓A bonds in the aggrecan core protein, and (b) was upregulated by retinoic acid but not IL-1α. The present study aimed to identify the alternative aggrecanase. Femoral head cartilage explants from TS-4/5∆cat mice were stimulated with IL-1α or retinoic acid and total RNA w..

View full abstract

University of Melbourne Researchers