MMP‐2 plays an essential role in producing epithelial‐mesenchymal transformations in the avian embryo

Duong, Tuan D.; Erickson, Carol A.

doi:10.1002/dvdy.10465

Cited by 129 publications

(113 citation statements)

References 74 publications

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“…It is likely that this profile varies with cell type, microenvironment and specific time point within the EMT process. For example, during development, MMP2 is expressed while neural crest cells undergo EMT but is rapidly downregulated as they disperse (Duong and Erickson 2004). It is possible that different concentrations of BMP4, the presence of additional signals, or a longer exposure time would result in further EMT-related changes in BEAS-2B cells.…”

Section: Discussionmentioning

confidence: 99%

BMP4 induces an epithelial–mesenchymal transition-like response in adult airway epithelial cells

et al. 2008

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Section: Discussionmentioning

confidence: 99%

BMP4 induces an epithelial–mesenchymal transition-like response in adult airway epithelial cells

et al. 2008

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“…• Epithelial-mesenchymal transition (EMT) [134][135][136][137][138] • Invasion and metastasis 29,138,139 • Vasoconstriction 140…”

Section: Box 2 Biological Consequences Of Mmp Proteolysismentioning

confidence: 99%

Matrix metalloproteinases and the regulation of tissue remodelling

Page-McCaw

Ewald

Werb

2007

Nat Rev Mol Cell Biol

2,560

2,180

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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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“…In addition to the structural rearrangements, delamination of NC cells and active migration throughout the whole embryo involves penetration of the basement membranes and invading extracellular matrices (ECM) (Fig.1 (Cai et al, 2000;Cantemir et al, 2004;Duong and Erickson, 2004). Also expression of several members of the novel metalloproteinase/disintegrin family ADAM identified in cancer have been reported in Xenopus cranial NC cells (Alfandari et al, 2001;Gaultier et al, 2002;Smith et al, 2002;Harrison et al, 2004).…”

Section: Modulation Of Extracellular Matrixmentioning

confidence: 99%

Controlled levels of canonical Wnt signaling are required for neural crest migration

Maj

Künneke

Loresch

et al. 2016

Developmental Biology

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MMP‐2 plays an essential role in producing epithelial‐mesenchymal transformations in the avian embryo

Cited by 129 publications

References 74 publications

BMP4 induces an epithelial–mesenchymal transition-like response in adult airway epithelial cells

BMP4 induces an epithelial–mesenchymal transition-like response in adult airway epithelial cells

Matrix metalloproteinases and the regulation of tissue remodelling

Controlled levels of canonical Wnt signaling are required for neural crest migration

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