scholarly journals Inhibition of matrix metalloproteinase-9 secretion by dimethyl sulfoxide and cyclic adenosine monophosphate in human monocytes

2021 ◽  
Vol 12 (1) ◽  
pp. 1-14
Author(s):  
Darcy R Denner ◽  
Maria LD Udan-Johns ◽  
Michael R Nichols
2009 ◽  
Vol 385 (2) ◽  
pp. 241-246 ◽  
Author(s):  
Chi-Jen Chang ◽  
Lung-An Hsu ◽  
Yu-Hsein Ko ◽  
Pei-Ling Chen ◽  
Yi-Ting Chuang ◽  
...  

1997 ◽  
Vol 273 (3) ◽  
pp. C826-C833 ◽  
Author(s):  
G. Egidy ◽  
J. Friedman ◽  
M. Viswanathan ◽  
L. M. Wahl ◽  
J. M. Saavedra

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.


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