Decreased allergic lung inflammatory cell egression and increased susceptibility to asphyxiation in MMP2-deficiency

Corry, David B.; Rishi, Kirtee; Kanellis, John; Kiss, Attila; Li, Song; Xu, Jie; Li, Feng; Werb, Zena; Kheradmand, Farrah

doi:10.1038/ni773

Cited by 240 publications

(223 citation statements)

References 49 publications

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“…The increase in cells and myeloperoxidase activity in BAL suggests that neutrophils are actively recruited in the airway in this model of injury. In opposite, lack of MMP-2 is related to the sequestration of neutrophils inside the interstitium, without invasion of the air spaces (9). It is known that MMP-9 can cleave different cytoand chemokines, like IL-1␤ (23).…”

Section: Discussionmentioning

confidence: 99%

Lack of matrix metalloproteinase-9 worsens ventilator-induced lung injury

Albaiceta¹,

Gutiérrez‐Fernández²,

Parra³

et al. 2008

American Journal of Physiology-Lung Cellular and Molecular Phys

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Section: Discussionmentioning

confidence: 99%

Lack of matrix metalloproteinase-9 worsens ventilator-induced lung injury

Albaiceta¹,

Gutiérrez‐Fernández²,

Parra³

et al. 2008

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…The role for MMP-14 in activation of MMP-2 is further questioned by a lack of phenocopy between null mouse lines. Whereas MMP-2 null mice reveal mild phenotypes, mostly related to neovascularization and inflammation (Berglin et al, 2003;Corry et al, 2002;Itoh et al, 2002;Itoh et al, 1998;Kato et al, 2001;Ohno-Matsui et al, 2003), MMP-14 knock-out mice have severe defects in skeletal development and turnover of type I collagen (Holmbeck et al, 1999;Holmbeck et al, 2003;Zhou et al, 2000). Overall, the in vivo data indicate that MMP-14 is not required for activation of MMP-2, but they do not rule the possibility that other membrane-type MMPs might be involved.…”

Section: Activation Of Prommps By Mmpsmentioning

confidence: 96%

Control of matrix metalloproteinase catalytic activity

2007

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SummaryAs their name implies, MMPs were first described as proteases that degrade extracellular matrix proteins, such as collagens, elastin, proteoglycans, and laminins. However, studies of MMP function in vivo have revealed that these proteinases act on a variety of extracellular protein substrates, often to activate latent forms of effector proteins, such as antimicrobial peptides and cytokines, or to alter protein function, such as shedding of cell-surface proteins. Because their substrates are diverse, MMPs are involved in variety of homeostatic functions, such as bone remodeling, wound healing, and several aspects of immunity. However, MMPs are also involved in a number of pathological processes, such as tumor progression, fibrosis, chronic inflammation, tissue destruction, and more. A key step in regulating MMP proteolysis is the conversion of the zymogen into an active proteinase. Several proMMPs are activated in the secretion pathway by furin proprotein convertases, but for most the activation mechanisms are largely not known. In this review, we discuss both authentic and potential mechanisms of proMMP activation.

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“…MMP9 cleaves and activates CXCL6 and CXCL8 (also known as interleukin-8 (IL8)), whereas it inactivates CXCL1 and CXCL4 (REFS 93,94 ). In asthma models, eosinophils from Mmp2-or Mmp9-deficient mice fail to migrate into the airways and accumulate in the interstitium, thereby predisposing the animals to asphyxiation 95,96 . MMP2 and MMP9 participate in a regulatory loop that dampens allergic inflammation.…”

Section: Pro-inflammatory and Anti-inflammatory Mmp Functionsmentioning

confidence: 99%

Matrix metalloproteinases and the regulation of tissue remodelling

Page-McCaw

Ewald

Werb

2007

Nat Rev Mol Cell Biol

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2,554

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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Decreased allergic lung inflammatory cell egression and increased susceptibility to asphyxiation in MMP2-deficiency

Cited by 240 publications

References 49 publications

Lack of matrix metalloproteinase-9 worsens ventilator-induced lung injury

Lack of matrix metalloproteinase-9 worsens ventilator-induced lung injury

Control of matrix metalloproteinase catalytic activity

Matrix metalloproteinases and the regulation of tissue remodelling

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