The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Biochemistry and Molecular Biology of Gelatinase B or Matrix Metalloproteinase-9 (MMP-9)
Abstract
The matrix metalloproteinases (MMPs) form an enzyme family of which gelatinase B (MMP-9) represents the largest and most complex member. We focus here on the biochemical properties, regulation, and functions of gelatinase B. The tight regulation of gelatinase B activity is highly complex and is established at five different levels. The transcription of the gelatinase B-gene depends on various cis-elements in its gene promotor and is induced or repressed by a large variety of soluble factors, including cytokines, growth factors, and hormones and by cellular contacts acting through specific signaling pathways. The specific regulation of its secretion occurs in cells storing gelatinase B in granules. After secretion, progelatinase B must be activated through an activation network. The enzyme activity is further regulated by inhibition and by other mechanisms, such as fine-tuning and stabilization by glycosylation. The ability of gelatinase B to degrade components of the extracellular matrix and to regulate the activity of a number of soluble proteins confers an important role in various physiological and pathological processes. These include reproduction, growth, development, inflammation, and vascular and proliferative diseases.
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Cites
Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis
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Cited by
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“[20] Van den Steen PE, Dubois B, Nelissen I, Rudd P M, Dwek RA, Opdenakker G.”
BackgroundCell-laden microengineered gelatin methacrylate hydrogels
Nichol, J. W., Koshy, S. T., Bae, H., Hwang, C. M., Yamanlar, S., & Khademhosseini, A. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.03.064 · Cited by 2,377
Inflammatory and immune pathways in the pathogenesis of periodontal disease
Cekici, A., Kantarci, A., Hasturk, H., & Van Dyke, T. E. (2014) · Periodontology 2000 · doi:10.1111/prd.12002 · Cited by 1,415
“involves tissue and plasma proteinases and bacterial proteinases, together with oxidative stress (174, 242).”
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Tuberculous Granuloma Induction via Interaction of a Bacterial Secreted Protein with Host Epithelium
Volkman, H. E., Pozos, T. C., Zheng, J., Davis, J. M., Rawls, J. F., & Ramakrishnan, L. (2010) · Science · doi:10.1126/science.1179663 · Cited by 448
Metadata
- Authors
- Van den Steen, P. E., Dubois, B., Nelissen, I., Rudd, P. M., Dwek, R. A., & Opdenakker, G.
- Venue
- Critical Reviews in Biochemistry and Molecular Biology
- Publisher
- Informa UK Limited
- Published
- 2002-01
- Volume
- 37
- Issue
- 6
- Pages
- 375-536
- ISSN
- 0045-6411 (ISSN-L)
- 1040-9238
- 1549-7798
- OpenAlex
- W2073259535
- Cited by
- 946
- References
- 5
- FWCI
- 7.88
- Type
- journal article
- Language
- en
- Open access
- closed
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- Van den Steen, P. E., Dubois, B., Nelissen, I., Rudd, P. M., Dwek, R. A., & Opdenakker, G. (2002). Biochemistry and Molecular Biology of Gelatinase B or Matrix Metalloproteinase-9 (MMP-9). Critical Reviews in Biochemistry and Molecular Biology. https://doi.org/10.1080/10409230290771546
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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