Conserved sequence in the aggrecan interglobular domain modulates cleavage by ADAMTS-4 and ADAMTS-5

• Published in: Biochimica et biophysica acta Vol. 1790; no. 3; pp. 161 - 172
• Main Authors: Miwa, Hazuki E., Gerken, Thomas A., Huynh, Tru D., Duesler, Lori R., Cotter, Meghan, Hering, Thomas M.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.03.2009
• Subjects: ADAM Proteins - genetics; ADAM Proteins - metabolism; ADAMTS-4; ADAMTS-5; ADAMTS4 Protein; ADAMTS5 Protein; Aggrecan; Aggrecanase; Aggrecans - chemistry; Aggrecans - metabolism; Animals; Blotting, Western; Cattle; Conserved Sequence; Exosite; Glycosylation; Hydrolysis; Interglobular domain; Mutagenesis, Site-Directed; Procollagen N-Endopeptidase - genetics; Procollagen N-Endopeptidase - metabolism; Proteinase; Substrate Specificity; Interglobular domain; Proteinase; Exosite; IGD; KS; G2 domain; G3 domain; Aggrecanase; EDTA; GAG; PVDF; ECM; ECL; CS; MMP; SDS-PAGE; G1 domain; ADAMTS-5; ADAMTS-4; HA; Aggrecan

Cleavage of aggrecan by ADAMTS proteinases at specific sites within highly conserved regions may be important to normal physiological enzyme functions, as well as pathological degradation. To examine ADAMTS selectivity, we assayed ADAMTS-4 and -5 cleavage of recombinant bovine aggrecan mutated at am...