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The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3.

Abstract:

We investigated whether the affinity of tissue inhibitor of metalloproteinases (TIMP)-3 for adamalysins with thrombospondin motifs (ADAMTS)-4 and ADAMTS-5 is affected by the non-catalytic ancillary domains of the enzymes. For this purpose, we first established a novel method of purifying recombinant FLAG-tagged TIMP-3 and its inhibitory N-terminal domain (N-TIMP-3) by treating transfected HEK293 cells with sodium chlorate to prevent heparan sulfate proteoglycan-mediated TIMP-3 internalization...

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Publication status:
Published

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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
Fushimi, K More by this author
Scilabra, SD More by this author
Nakamura, H More by this author
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Journal:
Matrix biology : journal of the International Society for Matrix Biology
Volume:
28
Issue:
8
Pages:
463-469
Publication date:
2009-10-05
DOI:
EISSN:
1569-1802
ISSN:
0945-053X
URN:
uuid:a068a4b3-3b45-4c46-9e6a-0ae87431962b
Source identifiers:
226351
Local pid:
pubs:226351

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