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Journal article

The hemopexin and O-glycosylated domains tune gelatinase B/MMP-9 bioavailability via inhibition and binding to cargo receptors.

Abstract:

Gelatinase B/matrix metalloproteinase-9 (MMP-9), a key regulator and effector of immunity, contains a C-terminal hemopexin domain preceded by a unique linker sequence of approximately 64 amino acid residues. This linker sequence is demonstrated to be an extensively O-glycosylated (OG) domain with a compact three-dimensional structure. The OG and hemopexin domains have no influence on the cleavage efficiency of MMP-9 substrates. In contrast, the hemopexin domain contains a binding site for the...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m512308200

Authors


Van den Steen, PE More by this author
Van Aelst, I More by this author
Hvidberg, V More by this author
Piccard, H More by this author
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Journal:
The Journal of biological chemistry
Volume:
281
Issue:
27
Pages:
18626-18637
Publication date:
2006-07-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:d92bb35d-c1d8-4e60-a158-fc3d8941f606
Source identifiers:
100224
Local pid:
pubs:100224

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