We-P14:422 Olive oil phenols modulate TNF-alpha-induced matrix metalloproteinase-9 in THP-1 cells

2006 ◽  
Vol 7 (3) ◽  
pp. 439-440
Author(s):  
R. Fagnani ◽  
M. Dell'Agli ◽  
S. Bellosta ◽  
G.V. Galli ◽  
R. Parente ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Olive Oil ◽  
Matrix Metalloproteinase 9 ◽  
Tnf Alpha ◽  
Metalloproteinase 9

scholarly journals The cross-talk between matrix metalloproteinase-9, RANKL/OPG system and cardiovascular risk factors in ovariectomized rat model of postmenopausal osteoporosis

PLoS ONE ◽  
2021 ◽  
Vol 16 (10) ◽  
pp. e0258254
Author(s):  
Maha Sabry ◽  
Seham Mostafa ◽  
Samaa Kamar ◽  
Laila Rashed ◽  
Suzanne Estaphan
Keyword(s):  
Risk Factors ◽  
Matrix Metalloproteinase ◽  
Inflammatory Markers ◽  
Matrix Metalloproteinase 9 ◽  
Female Rats ◽  
Tnf Alpha ◽  
Cvd Risk ◽  
Turnover Markers ◽  
Metalloproteinase 9 ◽  
Control Sham

Epidemiology and pathogenesis of cardiovascular diseases (CVD) and osteoporosis are strikingly overlapping. This study presents matrix metalloproteinase-9 (MMP-9), as a simple molecular link more consistently associated with the pathophysiology of both osteoporosis and CVD risk factors. 40 adult female rats were randomly distributed into 4 groups [control sham-operated, untreated osteoporosis, carvedilol-treated osteoporosis and alendronate-treated osteoporosis]. After 8 weeks, blood samples were collected to estimate Lipid profile (Total cholesterol, HDL, Triglycerides), inflammatory markers (IL-6, TNF alpha, CRP and NO), and Bone turnover markers (BTM) (Alkaline phosphatase, osteocalcin and pyridinoline). The tibias were dissected to estimate MMP-9 and NF-kB gene expression, OPG, RANKL levels and for histological examination. Induction of osteoporosis resulted in a significant elevation in BTM, inflammatory markers and dyslipidemia. MMP-9 was significantly elevated and positively correlated with BTM, inflammation and dyslipidemia markers. Carvedilol and alendronate exerted a bone preservative role and attenuated dyslipidaemia and inflammation in accordance with their respective effect on MMP-9.

Anetoderma with lesional infiltration of TNF-alpha-expressing basophils and matrix metalloproteinase-9-secreting M2 macrophages

2021 ◽  
Vol 31 (2) ◽  
pp. 258-259
Author(s):  
Takashi Hashimoto ◽  
Kayo Awatani ◽  
Takahiro Satoh
Keyword(s):  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 9 ◽  
Tnf Alpha ◽  
M2 Macrophages ◽  
Metalloproteinase 9

CGP-42112 partially activates human monocytes and reduces their stimulation by lipopolysaccharides

1997 ◽  
Vol 273 (3) ◽  
pp. C826-C833 ◽  
Author(s):  
G. Egidy ◽  
J. Friedman ◽  
M. Viswanathan ◽  
L. M. Wahl ◽  
J. M. Saavedra
Keyword(s):  
Angiotensin Ii ◽  
Matrix Metalloproteinase ◽  
Transforming Growth Factor ◽  
Matrix Metalloproteinase 9 ◽  
Tnf Alpha ◽  
Dependent Manner ◽  
Human Monocytes ◽  
Binding Studies ◽  
Metalloproteinase 9 ◽  
At2 Receptors

CGP 42112, a high-affinity ligand for angiotensin II AT2 receptors, binds to rat macrophage/microglia lacking AT2 receptors. Here we report that CGP-42112 binds to human monocytes and exerts specific effects. Binding studies revealed a single site, highly specific for CGP-42112, not displaceable by angiotensin II, angiotensin fragments, tumor necrosis factor-alpha (TNF-alpha), interleukin (IL)-4, IL-10, transforming growth factor-beta, or lipopolysaccharide (LPS). Incubation of purified human monocytes in serum-free medium with CGP-42112 enhanced, in a dose-dependent manner, cell attachment to fibronectin and collagen-coated dishes as well as matrix metalloproteinase-9 secretion. CGP-42112 did not promote cytokine secretion. In contrast, when added in the presence of low doses of LPS, CGP-42112 reduced the LPS-stimulated secretion of TNF-alpha, IL-1 alpha, IL-1 beta, and IL-6 without affecting IL-10 and decreased the LPS-stimulated matrix metalloproteinase-9 activity. Additionally, CGP-42112 inhibited the increase in protein kinase A activity produced by LPS. Our results indicate that CGP-42112 may modulate monocyte activation through binding to a novel receptor.

Matrix metalloproteinase-9 (92 kDa gelatinase/type IV collagenase) from U937 monoblastoid cells: correlation with cellular invasion

1993 ◽  
Vol 104 (4) ◽  
pp. 991-999 ◽  
Author(s):  
H. Watanabe ◽  
I. Nakanishi ◽  
K. Yamashita ◽  
T. Hayakawa ◽  
Y. Okada
Keyword(s):  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 9 ◽  
Mononuclear Phagocytes ◽  
Cathepsin G ◽  
Tnf Alpha ◽  
U937 Cells ◽  
Type Iv Collagenase ◽  
Leukocyte Elastase ◽  
Type Iv ◽  
Metalloproteinase 9

The role of matrix metalloproteinase-9 (MMP-9, 92 kDa gelatinase/type IV collagenase) in invasion of mononuclear phagocytes was studied with U937 monoblastoid cells. 12-o-tetradecanoyl 13-phorbol acetate (TPA) differentiated them to macrophage-like cells with induction of MMP-9, and tumor necrosis factor alpha (TNF alpha) and interleukin-1 alpha (IL-1 alpha) stimulated the production of MMP-9 by TPA-treated cells. TNF alpha also induced the production of MMP-9 by TPA-untreated U937 cells without morphological differentiation. Other agents including dimethyl sulfoxide (DMSO), all-trans-retinoic acid (all-trans-RA), platelet-derived growth factor and 3′;5′-cyclic monophosphate had no effects on MMP-9 production by TPA-treated or -untreated cells, but all-trans-RA and DMSO did have a morphological effect on the differentiation of the cells. These data suggest that MMP-9 production by U937 cells is regulated by a mechanism independent of the differentiation to macrophage-like cells. MMP-9 was purified to homogeneity as an inactive zymogen with M(r) 92,000 (proMMP-9) from TPA-differentiated U937 cells treated with TNF alpha. ProMMP-9 was activated by p-aminophenylmercuric acetate (APMA) generating an active species of M(r) 67,000. Trypsin and cathepsin G also attained activation of the zymogen to its full activity obtained by APMA activation, but plasmin, leukocyte elastase, thrombin and plasma kallikrein had no ability to activate it. APMA-activated MMP-9 degraded type I gelatin readily and cleaved native collagen types III, IV and V. Invasion assays using reconstituted basement membrane coupled with a type IV collagenolysis assay showed good correlations between invasiveness, type IV collagenolysis and proMMP-9 production. Invasion was significantly inhibited by EDTA, alpha 2-macroglobulin and tissue inhibitor of metalloproteinases-1, but not by inhibitors of cathepsin G and leukocyte elastase. These data suggest that MMP-9 plays an important role in the invasion of mononuclear phagocytes through basement membranes.

364 Adenosine inhibits matrix metalloproteinase-9 secretion by activated neutrophils through a cAMP/PKA/Ca2+ pathway

2006 ◽  
Vol 5 (1) ◽  
pp. 79-80
Author(s):  
I ERNENS ◽  
D ROUY ◽  
Y DEVAUX ◽  
C JEANTY ◽  
D WAGNER
Keyword(s):  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 9 ◽  
Activated Neutrophils ◽  
Metalloproteinase 9

473 Adenosine stimulates matrix metalloproteinase-9 secretion by THP-1-derived macrophages

2007 ◽  
Vol 6 (1) ◽  
pp. 102-102
Author(s):  
E VELOT ◽  
I ERNENS ◽  
B HAAS ◽  
C JEANTY ◽  
D ROUY ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 9 ◽  
Metalloproteinase 9

Increase of matrix metalloproteinase-9 in peripheral blood of multiple sclerosis patients treated with high doses of methylprednisolone

2004 ◽  
Vol 36 (05) ◽  
Author(s):  
D Mirowska ◽  
W Wicha ◽  
A Członkowski ◽  
A Członkowska ◽  
F Holsboer ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Matrix Metalloproteinase ◽  
Peripheral Blood ◽  
Matrix Metalloproteinase 9 ◽  
High Doses ◽  
Multiple Sclerosis Patients ◽  
Metalloproteinase 9
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