The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
The Hemopexin and O-Glycosylated Domains Tune Gelatinase B/MMP-9 Bioavailability via Inhibition and Binding to Cargo Receptors
Open accessAbstract
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 cargo receptor low density lipoprotein receptor-related protein-1 (LRP-1). Furthermore, megalin/LRP-2 is identified as a new functional receptor for the hemopexin domain of MMP-9, able to mediate the endocytosis and catabolism of the enzyme. The OG domain is required to correctly orient the hemopexin domain for inhibition by TIMP-1 and internalization by LRP-1 and megalin. Therefore, the OG and hemopexin domains down-regulate the bioavailability of active MMP-9 and the interactions with the cargo receptors are proposed to be the original function of hemopexin domains in MMPs.
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Citations
Cites
Matrix metalloproteinases as modulators of inflammation and innate immunity
Parks, W. C., Wilson, C. L., & López-Boado, Y. S. (2004) · Nature Reviews Immunology · doi:10.1038/nri1418 · Cited by 1,929
Identification of the receptor scavenging hemopexin-heme complexes
Hvidberg, V., Maniecki, M. B., Jacobsen, C., Højrup, P., Møller, H. J., & Moestrup, S. K. (2005) · Blood · doi:10.1182/blood-2005-03-1185 · Cited by 473
Self-citation
Cited by
Progress in matrix metalloproteinase research
MURPHY, G., & NAGASE, H. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.05.002 · Cited by 759
Chakraborty, S., Kaur, S., Guha, S., & Batra, S. K. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.03.008 · Cited by 503
Zymography methods for visualizing hydrolytic enzymes
Vandooren, J., Geurts, N., Martens, E., Van den Steen, P. E., & Opdenakker, G. (2013) · Nature Methods · doi:10.1038/nmeth.2371 · Cited by 320
Self-citationCauwe, B., & Opdenakker, G. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.501783 · Cited by 299
Self-citationInfluence of matrix metalloproteinase MMP-9 on dendritic spine morphology
Michaluk, P., Wawrzyniak, M., Alot, P., Szczot, M., Wyrembek, P., Mercik, K., Medvedev, N., Wilczek, E., De Roo, M., Zuschratter, W., et al. (2011) · Journal of Cell Science · doi:10.1242/jcs.090852 · Cited by 214
Metadata
- Authors
- Van den Steen, P. E., Van Aelst, I., Hvidberg, V., Piccard, H., Fiten, P., Jacobsen, C., Moestrup, S. K., Fry, S., Royle, L., Wormald, M. R., Wallis, R., Rudd, P. M., Dwek, R. A., & Opdenakker, G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-07
- Volume
- 281
- Issue
- 27
- Pages
- 18626-18637
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2136124678
- Cited by
- 189
- References
- 2
- FWCI
- 4.81
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Van den Steen, P. E., Van Aelst, I., Hvidberg, V., Piccard, H., Fiten, P., Jacobsen, C., Moestrup, S. K., Fry, S., Royle, L., Wormald, M. R., Wallis, R., Rudd, P. M., Dwek, R. A., & Opdenakker, G. (2006). The Hemopexin and O-Glycosylated Domains Tune Gelatinase B/MMP-9 Bioavailability via Inhibition and Binding to Cargo Receptors. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m512308200
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
