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

Abstract:

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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Publisher:
Elsevier Ltd
Journal:
Chemistry and Biology
Volume:
21
Issue:
10
Pages:
1300-1309
Publication date:
2014-10-23
DOI:
ISSN:
1074-5521
URN:
uuid:1aba8269-e902-40c6-8d2b-bff13dc78c9a
Source identifiers:
489653
Local pid:
pubs:489653
Language:
English

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