scholarly journals Alternative Splicing and Promoter Usage Generates an Intracellular Stromelysin 3 Isoform Directly Translated as an Active Matrix Metalloproteinase

2002 ◽  
Vol 277 (28) ◽  
pp. 25527-25536 ◽  
Author(s):  
Daochun Luo ◽  
Bernard Mari ◽  
Isabelle Stoll ◽  
Patrick Anglard
1999 ◽  
Vol 16 (1) ◽  
pp. 76-83 ◽  
Author(s):  
Rama Kannan ◽  
Marc Ruff ◽  
John G. Kochins ◽  
Susan P. Manly ◽  
Isabelle Stoll ◽  
...  

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Liza L. Ramenzoni ◽  
Deborah Hofer ◽  
Alex Solderer ◽  
Daniel Wiedemeier ◽  
Thomas Attin ◽  
...  

Abstract Background Pathologically elevated levels of matrix metalloproteinase-8 (MMP-8) and Lactoferrin in oral fluids have been associated with the presence of gingivitis/periodontitis. This study aimed to assess the origin of MMP-8 and Lactoferrin in periodontitis patients and to identify the degree to which conventional clinical parameters correlate with their presence. Methods A total of ten periodontitis and ten healthy patients were included in this study. Whole saliva (stimulated and unstimulated), parotid/sublingual glandular fluid and gingival crevicular fluid from pockets and sulci were tested for MMP-8 and Lactoferrin and protein concentrations were quantified using an ELISA assay. Clinical parameters were checked for potential associations with MMP-8 and Lactoferrin levels. Results Periodontal patients presented higher concentrations of MMP-8 and Lactoferrin in pockets than other sources (P = 0.03). Lactoferrin measurement was higher in the parotid compared to sublingual glandular fluid in periodontitis patients (P = 0.03). Increased probing pocket depth was positively correlated with high MMP-8 and Lactoferrin levels. Conclusions Periodontal pockets appear to be the major source of active matrix metalloproteinase and Lactoferrin, which also may also enter the oral cavity through the salivary glands. Since clinically healthy sites in periodontitis patients also had elevated biomarker levels, gingival crevicular fluid biomarker testing may be more predictive of future tissue breakdown than conventional clinical parameters.


Author(s):  
Mutlu Keskin ◽  
Hanna Lähteenmäki ◽  
Nilminie Rathnayake ◽  
Ismo T. Räisänen ◽  
Taina Tervahartiala ◽  
...  

2000 ◽  
Vol 275 (4) ◽  
pp. 2661-2668 ◽  
Author(s):  
Matthew W. Olson ◽  
M. Margarida Bernardo ◽  
Martin Pietila ◽  
David C. Gervasi ◽  
Marta Toth ◽  
...  

2009 ◽  
Vol 29 (7) ◽  
pp. 966-978 ◽  
Author(s):  
Stephen N. Hartland ◽  
Frank Murphy ◽  
Rebecca L. Aucott ◽  
Armand Abergel ◽  
Xiaoying Zhou ◽  
...  

2021 ◽  
Vol 10 (5) ◽  
Author(s):  
Corey S. Moran ◽  
Erik Biros ◽  
Smriti M. Krishna ◽  
Susan K. Morton ◽  
Daniel J. Sexton ◽  
...  

Background Abdominal aortic aneurysm (AAA) is an important cause of mortality in older adults. The kinin B2 receptor agonist, bradykinin, has been implicated in AAA pathogenesis through promoting inflammation. Bradykinin is generated from high‐ and low‐molecular‐weight kininogen by the serine protease kallikrein‐1. The aims of this study were first to examine the effect of neutralizing kallikrein‐1 on AAA development in a mouse model and second to test how blocking kallikrein‐1 affected cyclooxygenase‐2 and prostaglandin E 2 in human AAA explants. Methods and Results Neutralization of kallikrein‐1 in apolipoprotein E‐deficient ( ApoE −/− ) mice via administration of a blocking antibody inhibited suprarenal aorta expansion in response to angiotensin (Ang) II infusion. Kallikrein‐1 neutralization decreased suprarenal aorta concentrations of bradykinin and prostaglandin E 2 and reduced cyclooxygenase‐2 activity. Kallikrein‐1 neutralization also decreased protein kinase B and extracellular signal‐regulated kinase 1/2 phosphorylation and reduced levels of active matrix metalloproteinase 2 and matrix metalloproteinase 9. Kallikrein‐1 blocking antibody reduced levels of cyclooxygenase‐2 and secretion of prostaglandin E 2 and active matrix metalloproteinase 2 and matrix metalloproteinase 9 from human AAA explants and vascular smooth muscle cells exposed to activated neutrophils. Conclusions These findings suggest that kallikrein‐1 neutralization could be a treatment target for AAA.


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