Activation of Human Neutrophil Procollagenase by Nitrogen Dioxide and Peroxynitrite: A Novel Mechanism for Procollagenase Activation Involving Nitric Oxide

Okamoto, Tatsuya; Akaike, Takaaki; Nagano, Tetsuo; Miyajima, Seiya; Suga, Moritaka; Ando, Masayuki; Ichimori, Kohji; Maeda, Hiroshi

doi:10.1006/abbi.1997.0127

Cited by 218 publications

(147 citation statements)

References 55 publications

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“…In vitro, a number of proMMPs are activated by reactive oxygen species (ROS), which can modify the cysteine thiol group and activate proMMPs via autolytic cleavage. For example, hypochlorous acid (HOCl), a product of neutrophil myeloperoxidase (MPO), and hydroxyl radicals activate proMMPs-1, -7, and -9 (Fu et al, 2001;Michaelis et al, 1992;Peppin and Weiss, 1986;Weiss et al, 1985), and peroxynitrate can activate proMMPs-1, -2, and -9 (Okamoto et al, 1997). However, a role for most ROS as in vivo activators of MMPs has not been established.…”

Section: Oxidative Control Of Mmp Activitymentioning

confidence: 99%

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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Section: Oxidative Control Of Mmp Activitymentioning

confidence: 99%

Control of matrix metalloproteinase catalytic activity

2007

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“…Activation may be achieved in vitro by proteinases (plasmin, tryptase, stromelysin, CG, and bacterial proteinases), reactive oxygen species, and chemicals including organomercurials and SH-modifying agents [87][88][89][90]. These activators disrupt the interaction between zinc, coordinated within the catalytic domain, and a conserved cysteine within the proenzyme domain [91].…”

Section: Metalloproteinasesmentioning

confidence: 99%

The cell biology of leukocyte-mediated proteolysis

Owen

Campbell

1999

Journal of Leukocyte Biology

383

399

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Leukocyte-derived proteinases have the capacity to degrade every component of the extracellular matrix, and thereby play fundamental roles in physiological processes. However, if the activity of these proteinases is uncontrolled or dysregulated, they have the capacity to contribute to tissue injury that potentially affects every organ in the body. Although there is a substantial literature on structure and activity of these proteinases when they are free in solution, until recently there has been little information about the cell biology of proteinases and their inhibitors. Recent studies, however, have identified several mechanisms by which inflammatory cells can degrade extracellular proteins in a milieu that contains high-affinity proteinase inhibitors. J. Leukoc. Biol. 65: 137-150; 1999.

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“…The immunoreactive band was visualized with 5-bromo-4-chloro-3-indolyl phosphate/nitro blue tetrazolium as substrates for alkaline phosphatase. Immunoblots were quantified by a densitometrical analysis, as compared with the immunoreactive band of standard purified CP (34).…”

Section: Rs-no Production By Cells Inmentioning

confidence: 99%

Nitrosothiol Formation Catalyzed by Ceruloplasmin

Inoue¹,

Akaike²,

Miyamoto³

et al. 1999

Journal of Biological Chemistry

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187

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Ceruloplasmin (CP) is a major multicopper-containing plasma protein that is not only involved in iron metabolism through its ferroxidase activity but also functions as an antioxidant. However, physiological substrates for CP have not been fully identified nor has the role of CP been fully understood. The reaction of nitric oxide (NO) with CP was investigated in view of nitrosothiol (RS-NO) formation. First, formation of heavy metal-or CP-catalyzed RS-NO was examined with physiologically relevant concentrations of NO and various thiol compounds (RSH) such as glutathione (GSH). Among the various heavy metal ions and copper-containing enzymes and proteins examined, only copper ion (Cu 2؉ ) and CP showed potent RS-NO (S-nitrosoglutathione)-producing activity. Also, RS-NO-forming catalytic activity was evident for CP added exogenously to RAW264 cells expressing inducible NO synthase in culture, but this was not the case for copper ion. Similarly, CP produced endogenously by HepG2 cells showed potent RS-NO-forming activity in the cell culture. One-electron oxidation of NO appears to be operative for RS-NO production via electron transfer from type 1 copper to a cluster of types 2 and 3 copper in CP. Neurological disorders are associated with aceruloplasminemia; besides RS-NO, S-nitrosoglutathione particularly has been shown to have neuroprotective effect against oxidative stress induced by iron overload. Thus, we suggest that CP plays an important catalytic role in RS-NO formation, which may contribute to its potent antioxidant and cytoprotective activities in vivo in mammalian biological systems.

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Activation of Human Neutrophil Procollagenase by Nitrogen Dioxide and Peroxynitrite: A Novel Mechanism for Procollagenase Activation Involving Nitric Oxide

Cited by 218 publications

References 55 publications

Control of matrix metalloproteinase catalytic activity

Control of matrix metalloproteinase catalytic activity

The cell biology of leukocyte-mediated proteolysis

Nitrosothiol Formation Catalyzed by Ceruloplasmin

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