Matrix metalloproteinase 2 secretion in WEHI 164 fibrosarcoma cells is nitric oxide-related and modified by morphine

2006 ◽  
Vol 530 (1-2) ◽  
pp. 33-39 ◽  
Author(s):  
Ahmad Shariftabrizi ◽  
Artemissia-Phoebe Nifli ◽  
Mohammad Ansari ◽  
Farshid Saadat ◽  
Mohammad Reza Ebrahimkhani ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 2 ◽  
Fibrosarcoma Cells

scholarly journals Hesperidin Prevents Nitric Oxide Deficiency-Induced Cardiovascular Remodeling in Rats via Suppressing TGF-β1 and MMPs Protein Expression

2018 ◽  
Author(s):  
Putcharawipa Maneesai ◽  
Sarawoot Bunbupha ◽  
Prapassorn Potue ◽  
Thewarid Berkban ◽  
Upa Kukongviriyapan ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Tumor Necrosis Factor ◽  
Matrix Metalloproteinase ◽  
Protein Expression ◽  
Wall Thickness ◽  
Tumor Necrosis ◽  
Left Ventricular ◽  
Matrix Metalloproteinase 2 ◽  
Cardiovascular Remodeling ◽  
Necrosis Factor

Hesperidin is a major flavonoid isolated from citrus fruits that exhibits several biological activities. This study aims to evaluate the effect of hesperidin on cardiovascular remodeling induced by N-nitro L-arginine methyl ester (L-NAME) in rats.  Male Sprague-Dawley rats were treated with L-NAME (40 mg/kg); L-NAME plus hesperidin (15 mg/kg), or hesperidin (30 mg/kg), or captopril (2.5 mg/kg) for five weeks (n = 8/group). Hesperidin or captopril significantly prevented the development of hypertension in L-NAME rats.  Moreover, hesperidin or captopril alleviated L-NAME-induced cardiac remodeling; increases in wall thickness, cross sectional area (CSA) and fibrosis of left ventricular (LV), and vascular remodeling; increases in wall thickness, CSA, vascular smooth muscle cells and collagen deposition in the aorta. These were associated with reduced oxidative stress markers, tumor necrosis factor-alpha (TNF-α), transforming growth factor-beta 1 (TGF-β1) and enhancing plasma nitric oxide metabolite (NOx) in L-NAME treated groups. Furthermore, up-regulation of tumor necrosis factor receptor type 1 (TNF-R1) and TGF-β1 protein expression and the over-expression of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) were suppressed in L-NAME rats treated with hesperidin or captopril. These data suggested that hesperidin had cardioprotective effects in L-NAME hypertensive rats. The possible mechanism may involve its antioxidant and anti-inflammatory effects.

Staurosporine-induced cleavage of apoptosis-inducing factor in human fibrosarcoma cells is independent of matrix metalloproteinase-2

2021 ◽  
Author(s):  
Wesam Bassiouni ◽  
John M. Seubert ◽  
Richard Schulz
Keyword(s):  
Matrix Metalloproteinase ◽  
Gelatin Zymography ◽  
Matrix Metalloproteinase 2 ◽  
Cell Necrosis ◽  
Calpain Activity ◽  
Fibrosarcoma Cells ◽  
Proteolytic Activities ◽  
Human Fibrosarcoma Cells ◽  
Apoptosis Inducing Factor ◽  
Calpain Inhibitors

Apoptosis-inducing factor (AIF) is a mitochondrial flavoprotein which mediates staurosporine (STS)-induced cell death. AIF cleavage and translocation to the cytosol is thought to be calpain-1-dependent as calpain inhibitors reduced AIF proteolysis. However, many calpain inhibitors also inhibit matrix metalloproteinase-2 (MMP-2) activity, an intracellular and extracellular protease implicated in apoptosis. Here we investigated whether MMP-2 activity is affected in response to STS and if contributes to AIF cleavage. Human fibrosarcoma HT1080 cells were treated with STS (0.1 µM, 0.25-24 hr). A significant increase in cellular MMP-2 activity was seen by gelatin zymography after 6 hr STS treatment, prior to induction of cell necrosis. Western blot showed the time-dependent appearance of two forms of AIF (~60 and 45 kDa) in the cytosol which were significantly increased at 6 hr. Surprisingly, knocking down MMP-2 or inhibiting its activity with MMP-2 preferring inhibitors ARP-100 or ONO-4817, or inhibiting calpain activity with ALLM or PD150606, did not prevent the STS-induced increase in cytosolic AIF. These results show that although STS rapidly increases MMP-2 activity, the cytosolic release of AIF may be independent of the proteolytic activities of MMP-2 or calpain.

Carbohydrate-Mediated Regulation of Matrix Metalloproteinase-2 Activation in Normal Human Fibroblasts and Fibrosarcoma Cells

1996 ◽  
Vol 228 (2) ◽  
pp. 530-538 ◽  
Author(s):  
David C. Gervasi ◽  
Avraham Raz ◽  
Marie Dehem ◽  
Maozhou Yang ◽  
Markku Kurkinen ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Human Fibroblasts ◽  
Matrix Metalloproteinase 2 ◽  
Fibrosarcoma Cells ◽  
Normal Human

Abstract 665: Endothelial Nitric Oxide Negatively Modulates Phenylephrine-induced Contraction In Matrix Metalloproteinase 2 (mmp-2)-filled Rabbit Aortic Rings

Hypertension ◽  
2012 ◽  
Vol 60 (suppl_1) ◽  
Author(s):  
Alejandro F Prado ◽  
Laena Pernomian ◽  
Lusiane M Bendhack ◽  
Raquel F Gerlach
Keyword(s):  
Nitric Oxide ◽  
Matrix Metalloproteinase ◽  
Muscle Activity ◽  
Vascular Function ◽  
Vascular Reactivity ◽  
Selective Inhibitor ◽  
Matrix Metalloproteinase 2 ◽  
Maximum Effect ◽  
Endothelial Nitric Oxide

Endothelial nitric oxide negatively modulates Phenylephrine-induced contraction in Matrix metalloproteinase 2 (MMP-2)-filled rabbit aortic rings The present study aimed to evaluate the vascular function of aortic rings after intraluminal injection of matrix metalloproteinase 2 (MMP-2) and contribution of endothelial nitric oxide (NO) in this response. METHODS: thoracic aorta isolated from New Zealand rabbits (3.0 Kg) was isolated and were performed in situ gelatinolytic assay (intraluminal exposure with Krebs solution or MMP-2 1.2 μg/mL, at 37° C for 30 minutes, with measure of fluorescence intensity - FI) or vascular reactivity. Cumulative concentration-effect curves for phenylephrine (PE, 0.1 nM - 10 μM/L) were performed in endothelium-intact (E+) or denuded (E-) aortic rings, in the absence or presence of L-NAME (non-selective inhibitor of NOS, 100 μM) or Hydroxycobalamine (scavenger of intracellular NO), 30 min before the PE curves on E+ rings. The vascular contraction was normalized by grams of tension by dry tissue (g/g) and were analyzed the agonist maximum effect (Emax) and potency (pD2). Data represent mean ± S.E.M and the results were statistically analyzed using Student t test, one-way or two-way ANOVA with Bonferroni pos-hoc (p<0,05). Results: In situ gelatinolytic activity was increased in the vessels filled with MMP-2 (19.19+0.93U,n=5) compared to vehicle (10.75+0.45U,n=5). In the vascular reactivity, E- aortic rings filled with MMP-2 increased Emax of PE (1893,28+122,40g/g,n=9) versus vehicle E- (1485.73+76.82g/g,n=9), but no differences were observed on Emax of E+ aortic rings (vehicle: 1416.13+120.87g/g,n=7; MMP-2: 1893.28+122.40g/g,n=9). The presence of L-NAME induced an increase in Emax of E+ aortic rings filled with vehicle (1817.60+76.37g/g,n=7) or MMP-2 (2340.50+130.43g/g,n=5). Hydroxycobalamine also increased the Emax of E+ aortic rings with vehicle (1889,81+129,17,n=6) or MMP-2 (2480,12+192,57,n=5). No difference of pD2 value was observed in this study. Conclusion: Data suggest this protease cross the aorta layers from the lumen. An increased vasoconstriction in E- vessels suggests a vascular smooth muscle activity of MMP-2. In the presence of L-NAME and Hydroxycobalamine, vessels filled with MMP-2 shows a greater maximum effect suggesting that NO exerts a negative modulation of the PE-induced vasoconstriction on MMP-2 aortic rings.

Nitric oxide induces gelatinase A (matrix metalloproteinase 2) during rat embryo implantation

2002 ◽  
Vol 78 (6) ◽  
pp. 1278-1287 ◽  
Author(s):  
Virginia Novaro ◽  
Carolina Pustovrh ◽  
Alejandro Colman-Lerner ◽  
Derek Radisky ◽  
Fabiana Lo Nostro ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Matrix Metalloproteinase ◽  
Embryo Implantation ◽  
Matrix Metalloproteinase 2 ◽  
Gelatinase A ◽  
Rat Embryo
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