Matrix metalloproteinases as insulin-like growth factor binding protein-degrading proteinases

Fowlkes, John L.; Thrailkill, Kathryn M.; Serra, Delila; Suzuki, Ko; Nagase, Hideaki

doi:10.1016/0955-2235(95)00017-8

Cited by 220 publications

(207 citation statements)

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“…Type I collagen degradation that is mediated by MMP1 is necessary for epithelial cell migration and wound healing in culture models 20 . Cleavage of ECM proteins by MMPs can also release ECM-bound growth factors, including insulin growth factors and fibroblast growth factors 21,22 . Alternative mechanisms of action have also been observed, including functional intermolecular MMP complexes: MMP14 binds to tissue inhibitor of metalloproteinase-2 (TIMP2), which binds to pro-MMP2, thereby positioning it for activation by a second molecule of MMP14 (REF.…”

Section: Functions Of Mmp Proteolysismentioning

confidence: 99%

Matrix metalloproteinases and the regulation of tissue remodelling

Page-McCaw

Ewald

Werb

2007

Nat Rev Mol Cell Biol

2,517

2,148

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Matrix metalloproteinases (MMPs) were discovered because of their role in amphibian metamorphosis, yet they have attracted more attention because of their roles in disease. Despite intensive scrutiny in vitro, in cell culture and in animal models, the normal physiological roles of these extracellular proteases have been elusive. Recent studies in mice and flies point to essential roles of MMPs as mediators of change and physical adaptation in tissues, whether developmentally regulated, environmentally induced or disease associated.The founding member of the matrix metalloproteinase (MMP) family, collagenase, was identified in 1962 by Gross and Lapiere, who found that tadpole tails during metamorphosis contained an enzyme that could degrade fibrillar collagen 1,2 . Subsequently, an interstitial collagenase, collagenase-1 or MMP1, was found in diseased skin and synovium 3 . In vitro, MMP1 initiates degradation of native fibrillar collagens, crucial components of vertebrate extracellular matrix (ECM), by cleaving the peptide bond between Gly775-Ile776 or Gly775-Lys776 in native type I, II or III collagen molecules 3,4 . Further research led to the discovery of a family of structurally related proteinases (23 in human, 24 in mice), now referred to as the MMP family.Interest in MMPs increased in the late 1960s and early 1970s following observations that MMPs are upregulated in diverse human diseases including rheumatoid arthritis and cancer. Importantly, high levels of MMPs often correlated with poor prognosis in human patients (reviewed in REF. 5 ). However, recent clinical data indicate that the relationship between § These authors contributed equally to this paper. Competing interests statementThe authors declare no competing financial interests. DATABASESThe following terms in this article are linked online to: Entrez Genome: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene DmMmp1 | DmMmp2 NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author ManuscriptMMPs and disease is not simple; for example, increased MMP activity can enhance tumour progression or can inhibit it (reviewed in REF. 6 ). This complex relationship between MMP expression and cancer has increased the basic and clinical interest in understanding MMP function in vivo, but it has also focused attention on MMPs and pathology, and relatively less attention has been focused on the normal roles of these enzymes. MMP proteolysisMMPs are members of the metzincin group of proteases, which are named after the zinc ion and the conserved Met residue at the active site 11,12 . Recent work has generated a unified peptidase nomenclature 13 Functions of MMP proteolysisHistorically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. However, MMP proteolysis can create space for cells to migrate, can produce specific substrate-cleavage fragments with independent biological activity, can MMPs in bone modelling and remodellingBone is an important site of ongoing tissue remodelling during development...

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Section: Functions Of Mmp Proteolysismentioning

confidence: 99%

Matrix metalloproteinases and the regulation of tissue remodelling

Page-McCaw

Ewald

Werb

2007

Nat Rev Mol Cell Biol

2,517

2,148

View full text Add to dashboard Cite

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“…For example, degradation of laminin-5 (Ln-5) by MMP-2 results in the exposure of a Ln-5 cryptic site that enhances endothelial cell migration [2,92,96,97]. Besides degradation of ECM, MMPs are also capable of releasing growth factors from ECM and/or inactive complexes, cleaving growth factor receptors and activating growth factors excreted as pre-pro-enzymes, like transforming growth factor (TGF)-␣, TGF-␤, macrophage-colony stimulating factor (M-CSF), insulin like growth factor (IGF) and fibroblast growth factor receptor (FGFR)-1 [4,98,[98][99][100][101][102][103][104][105][106][107][108][109]. As pointed out, above MMPs can directly or indirectly induce tumor angiogenesis through degradation of ECM and release or activation of growth factors, like TNF-␣ and TGF-␤.…”

Section: The Role Of Mmps In Tumor Angiogenesis and Tumor Growthmentioning

confidence: 99%

The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia

Klein

Vellenga

Fraaije

et al. 2004

Critical Reviews in Oncology/Hematology

303

170

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“…Insulin yes (Descamps et al, 2003) Insulin-like growth factor binding proteins (IGFBP) yes yes (Fowlkes et al, 1994;Manes et al, 1999;Thrailkill et al, 1995) Intercellular adhesion molecule (ICAM)-1 yes (Fiore et al, 2002) Interferon (IFN)-β yes (Nelissen et al, 2003) Interferon-inducible protein-10 (IP-10/CXCL-10) yes…”

Section: (Van Den Steen Et Al 2000)mentioning

confidence: 99%