Sulfated glycosaminoglycans control the extracellular trafficking and the activity of the metalloprotease inhibitor timp-3

Journal article

Summary Tissue inhibitor of metalloproteinase 3 (TIMP-3) is an important regulator of extracellular matrix (ECM) turnover. TIMP-3 binds to sulfated ECM glycosaminoglycans or is endocytosed by cells via low-density lipoprotein receptor-related protein 1 (LRP-1). Here, we report that heparan sulfate (HS) and chondroitin sulfate E (CSE) selectively regulate postsecretory trafficking of TIMP-3 by inhibiting its binding to LRP-1. HS and CSE also increased TIMP-3 affinity for glycan-binding metallo...

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Authors: Troeberg, L; Lazenbatt, C; Anower-E-Khuda, M; Freeman, C; Federov, O

• Publisher: Elsevier
• Journal: Chemistry and Biology
• Volume: 21
• Issue: 10
• Pages: 1300-1309
• Publication date: 2014-10-23
• DOI: 10.1016/j.chembiol.2014.07.014
• ISSN: 1074-5521
• Language: English