Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II

Suzuki, Ko; Lees, M; Newlands, G. F. J.; Nagase, Hideaki; Woolley, David

doi:10.1042/bj3050301

Cited by 80 publications

(61 citation statements)

References 55 publications

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“…In contrast, the N-terminal sequence of the MMP-1 activated by trypsin showed that proMMP-1 is cleaved at Phe 81 -Val 82 , which is one amino acid upstream of the bacterial proteinase cleavage site. Thus, these bacterial proteinase processing sites were different from those of other activators such as PCMB, APMA, plasmin, stromelysin, and trypsin, as was reported previously (6,31,33) and was confirmed in the present experiment. DISCUSSION A series of MMPs secreted from connective tissue cells and inflammatory cells play an important role in degradation and remolding of extracellular matrixes under physiological and pathological conditions (6 -8, 10 -12, 34 -36).…”

Section: Proteolytic Activation Of Prommp-8 By Various Bacterial Protsupporting

confidence: 89%

“…To determine the N-terminal sequence of proMMP-derived fragments, each protein fragment was separated by SDS-PAGE and transferred to the Immobilon™ polyvinylidene difluoride transfer membrane (Millipore Co., Ltd., Bedford, MA) according to the procedure reported previously (30,31). The proteins transferred to the polyvinylidene difluoride membrane were visualized by staining with Coomassie Brilliant Blue R250, and bands of interest were excised and placed on a Polybrene-treated glass filter, and sequence analysis was performed.…”

Section: N-terminal Sequence Analysis Of the Bacterial Proteinase Promentioning

confidence: 99%

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Activation of Human Matrix Metalloproteinases by Various Bacterial Proteinases

Okamoto¹,

Akaike²,

Suga³

et al. 1997

Journal of Biological Chemistry

145

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Matrix metalloproteinases (MMPs) are zinc-containing proteinases that participate in tissue remodeling under physiological and pathological conditions. To test the involvement of bacterial proteinases in tissue injury during bacterial infections, we investigated the activation potential of various bacterial proteinases against precursors of MMPs (proMMPs) purified from human neutrophils (proMMP-8 and -9) and from human fibrosarcoma cells (proMMP-1). Each proMMP was subjected to treatment with a series of bacterial proteinases at molar ratios of 0.01-0.1 (bacterial proteinase to proMMP), and activities of MMPs generated were determined. Among six different bacterial proteinases, thermolysin family enzymes (family M4) such as Pseudomonas aeruginosa elastase, Vibrio cholerae proteinase, and thermolysin strongly activated all three proMMPs via limited proteolysis to generate active forms of the MMPs. N-terminal sequence analysis of the active MMPs revealed that cleavage occurred at the Val 82 -Leu 83 and Thr 90 -Phe 91 bonds of proMMP-1 and proMMP-9, respectively, which are located near the N terminus of the catalytic domain of MMPs. In contrast, Serratia 56-kDa proteinase and Pseudomonas alkaline proteinase, both of which are classified as members of the serralysin subfamily of zinc metalloproteinases (family M10), and Serratia 73-kDa thiol proteinase did not evidence proteolytic processing or activation of proMMP-1, -8, and -9 under these experimental conditions. These results indicate that bacterial proteinases may play an important role in tissue destruction and disintegration of extracellular matrix at the site of infections.Collagen, one of the major structural components of the extracellular matrix, has a triple-helical structure and exhibits resistance to proteolytic cleavage by endogenous and exogenous proteinases (1) except for matrix metalloproteinases (MMPs) 1 such as human neutrophil collagenase (MMP-8). Bacterial proteinases have been suggested to mediate direct tissue destruction, resulting in impairment of host defense mechanisms in septic foci (2-4). Most bacterial proteinases, however, have weak degradative activity against collagen (1, 5). Thus, the mechanism of extracellular matrix destruction at the site of bacterial infection is poorly understood.MMPs, a family of zinc neutral endopeptidases, are secreted by a variety of cells as inactive precursors (proMMPs) and degrade a series of collagens (6). Two distinct proMMPs (proMMP-8 and neutrophil progelatinase, proMMP-9) are synthesized and secreted extracellularly from specific granules of human neutrophils after membrane stimulation (7, 8). Macrophages and fibroblasts produce interstitial procollagenase (proMMP-1) (6, 9) and 92-kDa progelatinase (proMMP-9), whose expressions vary constitutively or inducibly after stimulation with proinflammatory cytokines and lipopolysaccharide (10 -12). MMP-8 and -1 specifically cleave native triplehelical type I collagen into two major fragments, one-fourth and three-fourths the size of native collagen, respect...

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Section: Proteolytic Activation Of Prommp-8 By Various Bacterial Protsupporting

confidence: 89%

Section: N-terminal Sequence Analysis Of the Bacterial Proteinase Promentioning

confidence: 99%

Activation of Human Matrix Metalloproteinases by Various Bacterial Proteinases

Okamoto¹,

Akaike²,

Suga³

et al. 1997

Journal of Biological Chemistry

145

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“…Tryptase can process prothrombin (74), generate C3a from complement C3 (75), and degrade ECM components including fibrinogen (76,77), denatured type I collagen (78), and fibronectin (79). Tryptase and chymase can further promote ECM degradation by activating proMMPs (80)(81)(82)(83)(84) and pro-uPA (85). Mast cell tryptase is important in activating PAR-2 on synovial fibroblasts and inducing proinflammatory cytokine release (86,87).…”

Section: Immune Cell-derived Serine Proteinasesmentioning

confidence: 99%

“…Thus, cartilage resorption involves both metalloproteinases and serine proteinases, which are likely to function through a series of interacting cascades (Figure 2). A large number of serine proteinases have been shown to activate proMMPs, especially proMMP-3 (trypsin, chymotrypsin, tryptase, chymase, plasmin, plasma kallikrein, NE, CTG, trypsinogen 2, thrombin, and matriptase) (38,81,84,(189)(190)(191)(192). However, the precise activation mechanisms for many of the proMMPs that occur in vivo in both cartilage and other matrices are unknown (175).…”

Section: Serine Proteinases and Activation Of Procollagenases In Cartmentioning

confidence: 99%

Emerging roles of serine proteinases in tissue turnover in arthritis

Milner

Patel

Rowan

2008

Arthritis & Rheumatism

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“…In addition to blood pressure regulation, both Ang II and endothelin-1 are involved in the stimulation of vascular smooth muscle cell (SMC) growth and proliferation, vascular remodeling, and cardiac hypertrophy (8,9). Chymases also can influence structural remodeling through their ability to degrade extracellular matrix proteins, including fibronectin and collagen type IV, possibly through activation of matrix metalloproteinases (MMPs) (MMP-1, MMP-3, and MMP-9) (10)(11)(12). Chymases also stimulate collagen fibirillogenesis by cleavage of type I procollagen (13).…”

mentioning

confidence: 99%

Conditional and targeted overexpression of vascular chymase causes hypertension in transgenic mice

Gros²,

You³

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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We cloned a rat vascular chymase (RVCH) from smooth muscle cells (SMCs) that converts angiotensin I to II and is up-regulated in SMC from spontaneously hypertensive vs. normotensive rats. To determine whether increased activity of RVCH is sufficient to cause hypertension, transgenic mice were generated with targeted conditional expression of RVCH to SMC, with the use of the tetracyclinecontrolled transactivator (tTA). We confirmed conditional expression of RVCH by mRNA, protein, and chymase activity in the absence, but not in the presence, of dietary doxycycline. The systolic blood pressure (mmHg), measured by carotid artery cannulation at 10 -12 weeks of age, was higher in tTA؉͞RVCH؉ mice than in nonbinary transgenic littermates (136 ؎ 4 vs. 109 ؎ 3) (P < 0.05), as were the diastolic and mean pressures. Hypertension was completely reversed by doxycycline, suggesting a causal link with chymase expression. Medial thickening of mesenteric arteries from tTA؉͞RVCH؉ mice vs. littermates (0.82 ؎ 0.1 vs. 0.42 ؎ 0.02) (P < 0.05) was associated with increased SMC proliferation, as judged by positive immunoreactivity, with the use of an antibody to the proliferating cell nuclear antigen. These structural changes were prevented by doxycycline. Perfusion myography of mesenteric arteries from tTA؉͞RVCH؉ mice also revealed increased vasoconstriction in response to phenylephrine and impaired metacholine-induced vasodilatation when compared with littermate controls or with the doxycyline-treated group. Our studies suggest that up-regulation of this vascular chymase is sufficient to cause a hypertensive arteriopathy, and that RVCH may be a candidate gene and a therapeutic target in patients with high blood pressure.smooth muscle cells C hymases are serine proteinases that were thought to be produced exclusively by mast cells in blood vessels and the myocardium. These enzymes generate angiotensin (Ang) II in large and resistance vessels (1-3) and in the heart (4) and also can convert big-endothelin-1 to endothelin-1 in vitro (5) and inactivate the vasodilator bradykinin (6). That chymase-dependent Ang II formation can occur in the intact animal is evident from studies in the baboon, where it was shown that Ang-converting enzyme inhibitors could not prevent the hemodynamic response to [Pro11, Da1a12]Ang I, which produces Ang II upon incubation with chymase (7). In addition to blood pressure regulation, both Ang II and endothelin-1 are involved in the stimulation of vascular smooth muscle cell (SMC) growth and proliferation, vascular remodeling, and cardiac hypertrophy (8, 9). Chymases also can influence structural remodeling through their ability to degrade extracellular matrix proteins, including fibronectin and collagen type IV, possibly through activation of matrix metalloproteinases (MMPs) (MMP-1, MMP-3, and MMP-9) (10-12). Chymases also stimulate collagen fibirillogenesis by cleavage of type I procollagen (13).Several studies have provided compelling data to suggest that chymases could play a central role in cardiovascular di...

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Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II

Cited by 80 publications

References 55 publications

Activation of Human Matrix Metalloproteinases by Various Bacterial Proteinases

Activation of Human Matrix Metalloproteinases by Various Bacterial Proteinases

Emerging roles of serine proteinases in tissue turnover in arthritis

Conditional and targeted overexpression of vascular chymase causes hypertension in transgenic mice

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