Biocompatibility of Polysulfone II. Platelet Adhesion and CHO Cell Growth

1995 ◽  
Vol 5 (4) ◽  
pp. 259-273 ◽  
Author(s):  
Gilson Khang ◽  
Bong Jin Jeong ◽  
Hai Bang Lee ◽  
Joon B. Park
Keyword(s):  
Cell Growth ◽  
Platelet Adhesion ◽  
Cho Cell

Effects Of Aspirin And Sulfinpyrazone On Platelets, Vascular Cells And Their Interactions

1981 ◽  
Author(s):  
M R Buchanan ◽  
M J Vazquez ◽  
M A Gimbrone
Keyword(s):  
Growth Rate ◽  
Cell Growth ◽  
Dna Synthesis ◽  
Vessel Wall ◽  
Culture Medium ◽  
Platelet Adhesion ◽  
Thymidine Incorporation ◽  
Inhibitory Effect ◽  
Human Platelets ◽  
Final Density

Sulfinpyrazone (SUL) and aspirin (ASA) are potentially useful antithrombotic drugs. Both drugs are thought to exert this effect by inhibiting the platelet enzyme, cyclooxygenase (C-0), thus preventing thromboxane A2 synthesis. Recent data, however, suggest that these drugs also may affect vessel wall cells. To study this further, we examined the effects of SUL and ASA on i) the adhesion of 3H-adenine-labelled washed human platelets to cultured bovine endothelial (EC) and smooth muscle cells (SMC), ii) EC and SMC DNA synthesis (3H-thymidine incorporation) and iii) cell growth. Pretreatment of platelets with 100μM ASA or 250μM SUL (concentrations sufficient to inhibit C-0), did not affect platelet adhesion to untreated EC or SMC. However, adhesion of untreated, ASA- and SUL-platelets was increased 25,28 and 44% resp. when EC were pretreated with 650μM SUL for 24 hr. In contrast, adhesion of ASA-platelets to EC pretreated with lOOμM ASA (sufficient to inhibit prostacyclin), was unaffected. Platelet adhesion to SMC pretreated with 650μM SUL for 24 hr was decreased when platelets also were pretreated with ASA (20%, p<0.05) or SUL (27%, pc 0.02). Pretreatment of SMC with SUL for only 2 hr had no effect. DNA synthesis in EC and SMC treated with 62.5 and 250μM SUL for 24 hr, was inhibited >35% and >95% resp. Preliminary data suggest that this inhibitory effect may last longer in SMC. To study the effect of SUL on cell growth, EC and SMC were plated at 2 × 104 cells/ cm2 and fed with culture medium containing 0, 62.5 or 625uM SUL on day 0, 1, 3 and 4.5. EC growth rate and final density were unaffected over 7 days. SMC growth rate also was unaffected, but the final density of SMC treated with 650μM SUL was 31 μ 2% less than untreated SMC at 7 days (p<0.01). These data indicate that SUL has direct effects on EC and SMC that may influence i) platelet-vessel wall interactions and ii) vascular cell proliferation.

Effect of surfactant pluronic F-68 on CHO cell growth, metabolism, production, and glycosylation of human recombinant IFN-γ in mild operating conditions

2010 ◽  
Vol 27 (1) ◽  
pp. 181-190 ◽  
Author(s):  
Marie-Françoise Clincke ◽  
Emmanuel Guedon ◽  
Frances T. Yen ◽  
Virginie Ogier ◽  
Olivier Roitel ◽  
...  
Keyword(s):  
Cell Growth ◽  
Operating Conditions ◽  
Cho Cell ◽  
Ifn Γ ◽  
Growth Metabolism

Dependence on glucose limitation of thepCO2 influences on CHO cell growth, metabolism and IgG production

2007 ◽  
Vol 97 (6) ◽  
pp. 1479-1488 ◽  
Author(s):  
Shinya Takuma ◽  
Chikashi Hirashima ◽  
James M. Piret
Keyword(s):  
Cell Growth ◽  
Cho Cell ◽  
Glucose Limitation ◽  
Growth Metabolism

scholarly journals Engineering CHO cell growth by stable manipulation of miRNA expression

2011 ◽  
Vol 5 (S8) ◽  
Author(s):  
Noëlia Sanchez ◽  
Nga Lao ◽  
Clair Gallagher ◽  
Martin Clynes ◽  
Niall Barron
Keyword(s):  
Cell Growth ◽  
Mirna Expression ◽  
Cho Cell

CRGT Peptide In Cytoplasm Regulates Thrombus Formation Via Dissociating c-Src-β3 Interaction

Blood ◽  
2013 ◽  
Vol 122 (21) ◽  
pp. 3501-3501
Author(s):  
Jiansong Huang ◽  
Xiaofeng Shi ◽  
Wenda Xi ◽  
Ping Liu ◽  
Xiaodong Xi
Keyword(s):  
Molecular Mechanisms ◽  
Platelet Adhesion ◽  
Thrombus Formation ◽  
Human Platelets ◽  
Flow Conditions ◽  
Cho Cell ◽  
Integrin Αiibβ3 ◽  
Shear Rates ◽  
Platelet Adhesion And Aggregation

Abstract The RGT sequences of the integrin β3 tail directly and constitutively bind the inactive c-Src, regulating integrin αIIbβ3 signaling and platelet function. Previous work has shown that disrupting the interaction of c-Src with β3 via myristoylated RGT peptide or deletion of the RGT sequences in β3 selectively inhibits integrin αIIbβ3 outside-in signaling in platelets. However, the precise molecular mechanisms by which the Src-β3 association regulates integrin αIIbβ3 signaling need to be clarified. We found that active c-Src phosphoylated the Y747 and Y759 residues of β3 directly at the in vitro protein/protein level or in CHO cell models bearing Tac-β3 chimeras, which were devoid of the intact β3 signal transduction. Furthermore, data from mass spectrometry, [γ-32P] ATP incorporation assays and CHO cell/Tac-β3 chimeras demonstrated that the direct phosphorylation of Y747 and Y759 by active c-Src did not depend on the binding of c-Src to the RGT sequences of the β3 tail. To further investigate the biological functions of Src-β3 association in signal transduction we employed a cell-permeable and reduction-sensitive peptide (myr-AC∼CRGT), which disrupted the Src-β3 association in platelets independent of membrane-anchorage, and found that when platelets were stimulated by thrombin the c-Src activation and the phosphorylation of the tyrosine residues of the β3 tail were substantially inhibited by the presence of the peptide. These results suggest that one of the crucial biological functions of Src-β3 association is to serve as a “bridge” linking integrin signaling with the c-Src full activation and phosphorylation of the tyrosines of the β3 tail. To answer whether the RGT peptide binding to Src is able to alter the enzymatic activity of c-Src, we examined the Src-Csk association, the phosphorylation status of Y416 and Y527 of c-Src and the c-Src kinase catalytic activity. Results showed that myr-AC∼CRGT did not dissociate Csk from c-Src in resting platelets and the phosphorylation level of Y416 and Y527 of c-Src remained unaltered. Consistent data were also obtained from in vitro analysis of the c-Src kinase catalytic activity in the presence of CRGT peptide. These results suggest that myr-AC∼CRGT peptide per se does not fully activate c-Src. Myr-AC∼CRGT was also found to inhibit integrin αIIbβ3 outside-in signaling in human platelets. To examine the effect of the myr-AC∼CRGT on platelet adhesion and aggregation under flow conditions, we measured the platelet thrombus formation under different shear rates. Myr-AC∼CRGT did not affect the platelet adhesion at a wall shear rate of 125 s-1. The inability of myr-AC∼CRGT to affect platelet adhesion and aggregation remained at 500 s-1 shear rates. At 1,500 s-1, or 5,000 s-1 rates, myr-AC∼CRGT partially inhibited platelet adhesion and aggregation. These observations indicate that the Src-regulated outside-in signaling plays a pivotal role in the stable thrombus formation and the thrombus growth under flow conditions. The present study reveals novel insights into the molecular mechanisms by which c-Src regulates integrin αIIbβ3 signaling, particularly the phorsphorylation of the β3 cytoplasmic tyrosines, and provides first evidence in human platelets that the RGT peptide or derivatives regulate thrombus formation through dissociating the Src-β3 interaction. The data of this work allow us to anticipate that intracellular delivery of the RGT peptide or its analogues may have potential in the development of a new antithrombotic strategy where only the Src-β3 interaction is specifically interrupted so as to provide an effective inhibition on thrombosis together with a decent hemostasis. Disclosures: No relevant conflicts of interest to declare.

Optimization of microencapsulated recombinant CHO cell growth, endostatin production, and stability of microcapsulein vivo

2007 ◽  
Vol 84B (1) ◽  
pp. 79-88 ◽  
Author(s):  
Ying Zhang ◽  
Wei Wang ◽  
Yubing Xie ◽  
Weiting Yu ◽  
Guojun Lv ◽  
...  
Keyword(s):  
Cell Growth ◽  
Cho Cell

The Influence of pH on Cell Growth and Specific Productivity of Two CHO Cell Lines Producing Human Anti Rh D IgG

2001 ◽  
pp. 197-199 ◽  
Author(s):  
Maria J. De Jesus ◽  
M. Bourgeois ◽  
G. Baumgartner ◽  
P. Tromba ◽  
Martin Jordan ◽  
...  
Keyword(s):  
Cell Growth ◽  
Cell Lines ◽  
Specific Productivity ◽  
Cho Cell ◽  
Influence Of Ph

Influence of the rapeseed protein hydrolysis process on CHO cell growth

2008 ◽  
Vol 99 (15) ◽  
pp. 7143-7151 ◽  
Author(s):  
G. Chabanon ◽  
L. Alves da Costa ◽  
B. Farges ◽  
C. Harscoat ◽  
S. Chenu ◽  
...  
Keyword(s):  
Cell Growth ◽  
Protein Hydrolysis ◽  
Cho Cell ◽  
Rapeseed Protein ◽  
Hydrolysis Process

scholarly journals Combination of yeast hydrolysates to improve CHO cell growth and IgG production

2012 ◽  
Vol 65 (4) ◽  
pp. 629-641 ◽  
Author(s):  
Mathilde Mosser ◽  
Isabelle Chevalot ◽  
Eric Olmos ◽  
Fabrice Blanchard ◽  
Romain Kapel ◽  
...  
Keyword(s):  
Cell Growth ◽  
Cho Cell

Effects of laser-modified polystyrene substrate on CHO cell growth and alignment

2004 ◽  
Vol 70B (1) ◽  
pp. 43-48 ◽  
Author(s):  
Bangshang Zhu ◽  
Qinhua Lu ◽  
Jie Yin ◽  
Jun Hu ◽  
Zongguang Wang
Keyword(s):  
Cell Growth ◽  
Cho Cell ◽  
Modified Polystyrene
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