Effects of ligustrazine injection on high glucose-induced type Ⅰ collagen, matrix metalloproteinase-1 and tissue inhibitor of metalloproteinase-1 expressions in human peritoneal mesothelial cells in vitro

2009 ◽  
Vol 7 (1) ◽  
pp. 65-69
Author(s):  
GS Zhu
Keyword(s):  
Matrix Metalloproteinase ◽  
High Glucose ◽  
Collagen Matrix ◽  
Mesothelial Cells ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Tissue Inhibitor ◽  
Peritoneal Mesothelial Cells ◽  
Matrix Metalloproteinase 1 ◽  
Human Peritoneal Mesothelial Cells

Pravastatin increases the expression of the tissue inhibitor of matrix metalloproteinase-1 and the oncogeneBaxin human aortic abdominal aneurysms

2008 ◽  
Vol 86 (7) ◽  
pp. 431-437 ◽  
Author(s):  
Petra J. Mateos-Cáceres ◽  
Antonio J. López-Farré ◽  
Pilar C. Morata ◽  
Priscila Ramos-Mozo ◽  
Carlos Macaya ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Apoptotic Index ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Tissue Inhibitor ◽  
Hmg Coa Reductase ◽  
Matrix Metalloproteinase 1 ◽  
Abdominal Aortic ◽  
Coa Reductase ◽  
Metalloproteinase 9

The effect of pravastatin on matrix metalloproteinase-9 (MMP-9) and the level of tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2 was studied in explants of human abdominal aortic aneurysm (AAA) obtained from 13 patients. The effect of pravastatin on the apoptotic status of human AAA explants was also examined. Total MMP-9 content did not differ in human AAA explants incubated in vitro in the presence or absence of pravastatin (10−6mol/L) for 48 h. TIMP-1 levels were significantly increased in pravastatin-incubated AAA explants, but TIMP-2 production was not modified by pravastatin. Western blot experiments showed that, whereas Bax expression was increased in pravastatin-incubated AAA explants, the expression of Bcl-2 was not modified. On the other hand, the ratio of the expression of Bax to Bcl-2, an apoptotic index, was not modified by pravastatin. In the human AAA explants, the increase in Bax expression, but not the increase in TIMP-1 expression elicited by pravastatin, was reversed by l-mevalonate, a downstream HMG-CoA reductase metabolite, suggesting that the expression of Bax and TIMP-1 followed HMG-CoA reductase-dependent and -independent pathways, respectively. In conclusion, pravastatin increases both TIMP-1 and Bax expression in human AAA explants without changes in either MMP-9 activity or the apoptotic status.

Glucose but not N-Acetylglucosamine Accelerates in vitro Senescence of Human Peritoneal Mesothelial Cells

2011 ◽  
Vol 34 (6) ◽  
pp. 489-494 ◽  
Author(s):  
Marta Ciszewicz ◽  
George Wu ◽  
Paul Tam ◽  
Alicja Połubinska ◽  
Andrzej Bręborowicz
Keyword(s):  
Mesothelial Cells ◽  
Peritoneal Mesothelial Cells ◽  
Human Peritoneal Mesothelial Cells

scholarly journals High glucose promotes TGF-β1 production by inducing FOS expression in human peritoneal mesothelial cells

2015 ◽  
Vol 20 (1) ◽  
pp. 30-38 ◽  
Author(s):  
Keiko Kokoroishi ◽  
Ayumu Nakashima ◽  
Shigehiro Doi ◽  
Toshinori Ueno ◽  
Toshiki Doi ◽  
...  
Keyword(s):  
High Glucose ◽  
Mesothelial Cells ◽  
Peritoneal Mesothelial Cells ◽  
Human Peritoneal Mesothelial Cells ◽  
Fos Expression ◽  
Tgf Β1

Catabolism of Newly Synthesized Decorin in vitro by Human Peritoneal Mesothelial Cells

2004 ◽  
Vol 24 (2) ◽  
pp. 147-155 ◽  
Author(s):  
Susan Yung ◽  
Heinz Hausser ◽  
Gareth Thomas ◽  
Liliana Schaefer ◽  
Hans Kresse ◽  
...  
Keyword(s):  
Dermatan Sulfate ◽  
Specific Activity ◽  
Cell Layer ◽  
Mesothelial Cells ◽  
Matrix Assembly ◽  
Peritoneal Mesothelial Cells ◽  
Intracellular Degradation ◽  
Human Peritoneal Mesothelial Cells ◽  
Cell Medium

Objective Previous studies have shown that decorin and biglycan account for over 70% of the proteoglycans (PGs) synthesized by human peritoneal mesothelial cells (HPMCs). Since these PGs are involved in the control of cell growth, cell differentiation, and matrix assembly, we investigated their turnover in cultured HPMCs. Methods Confluent HPMCs were metabolically labeled with [35S]-sulfate and the labeled products isolated from the cell medium and the cell layer characterized by sensitivity to bacterial eliminases. Experiments were undertaken with exogenous labeled decorin, and its metabolic state was studied. Results In a 24-hour labeling period, 75% of the newly synthesized chondroitin sulfate/dermatan sulfate (CS/DS) PGs appeared in the culture medium, the majority of which (90%) was decorin. In the cell layer, protein-free glycosaminoglycan (GAG) chains accounted for 21% of the total CS/DS at 24 hours and exhibited constant specific activity at 12 – 16 hours. The latter material was turned over with a half-life of approximately 2.5 hours. Exogenous decorin underwent receptor-mediated endocytosis and subsequent intracellular degradation. Uptake but not degradation could be inhibited by heparin. Conclusions HPMCs are distinguished by a rapid turnover of decorin. A characteristic metabolic feature is the existence of a large intracellular pool of protein-free DS-GAGs. Understanding the control of decorin turnover in HPMCs might lead to delineation of its potential role in both the physiology and pathophysiology of the membrane in PD patients.

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