Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact.

By P. Steen, P. Proost, A. Wuyts, J. Damme, G. Opdenakker. Blood, 2000

736 citations recorded by the source corpus.

Subfields: Cancer Research, Immunology, Oncology

View Paper: https://www.semanticscholar.org/paper/090c806ec3c6df76ba0f82c3a426f642a494ae20

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cancer Research

1. J. McGuire
2. A. Manicone
3. Christopher M. Overall
4. G. Opdenakker
5. Zena Werb
6. P. E. Van den Steen
7. V. Plaks
8. K. Kessenbrock

In Immunology

1. V. Plaks
2. J. Wong
3. I. Clark‐Lewis
4. J. Van Damme
5. J. Wallace
6. Christopher M. Overall
7. G. A. McQuibban
8. J. Gong

In Oncology

1. J. McGuire
2. A. Manicone
3. Christopher M. Overall
4. Zena Werb
5. G. Opdenakker
6. V. Plaks
7. K. Kessenbrock
8. P. E. Van den Steen

Citations in the corpus

• Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): The next decade (2013, background): “However, multimers produced by cells are reduction-sensitive and will be converted in vitro to monomers in the presence of reducing chemicals (Van den Steen et al., 2000).”
• Matrix metalloproteinases as modulators of inflammation. (2008, background): “The N-terminal domain of the mature CXC chemokine CXCL8 (IL-8) and LIX (the mouse equivalent of human CXCL5 and CXCL6) are processed by MMP9 and MMP8 respectively, resulting in products that have more potent chemoattractant activities that the full-length molecules [37,38].”
• Matrix metalloproteinase-9: Many shades of function in cardiovascular disease. (2013, background): “A partial list of ECM, chemokines, cytokines, and substrates degraded, activated or inactivated by MMP-9 MMP-9 Substrate Degrades Collagen type I, II, III, IV, V, XI, XVI, fibronectin, laminin, osteopontin, thrombospondin-1, tenascin-C, galectin-3, decorin Activates CXCL5, CXCL8, TNF- , IL-1 , TGFIn”
• Gelatinase B functions as regulator and effector in leukocyte biology (2001, background): “The dimers may be dissociated by the addition of b-mercaptoethanol [18].”
• Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. (2002, methodology): “Figure 2 shows that MCP-1 is cleaved at Ala4-Ile5, designated MCP-1(5-76); by MMP-1; to a lesser extent (20% of total by densitometric analysis) by MMP-3; and to a very minor extent (5% of total) by MMP-8.”
• Matrix Metalloproteinases: Regulators of the Tumor Microenvironment (2010, background): “In a comparable manner, N-terminal processing of neutrophil-attracting CXCL8/interleukin-8 (IL-8) by MMP-9 leads to 10-fold increased chemotactic activity on neutrophils compared to full-length CXCL8 (Van den Steen et al., 2000).”
• Biochemistry and Molecular Biology of Gelatinase B or Matrix Metalloproteinase-9 (MMP-9) (2002, background): “Other CXC chemokines, such as connective tissue activating peptide-III (CTAP-III), growth-related oncogene-α (GRO-α), platelet factor-4 (PF-4) (Van den Steen et al., 2000), and stromal-cell derived factor-1 (SDF-1) (McQuibban et al., 2001) are inactivated.”