Bacterial Expression and in Vitro Assay of Cell Cycle Kinases

1996 ◽  
pp. 157-168 ◽  
Author(s):  
Lisa Connell-Crowley ◽  
Wade Harper
Keyword(s):  
Cell Cycle ◽  
In Vitro Assay ◽  
Bacterial Expression ◽  
Vitro Assay

Growth factors and pattern formation

Development ◽  
1981 ◽  
Vol 65 (Supplement) ◽  
pp. 187-207
Author(s):  
J. C. Smith
Keyword(s):  
Cell Cycle ◽  
Growth Factors ◽  
Pattern Formation ◽  
Positional Information ◽  
In Vitro Assay ◽  
Vitro Assay ◽  
Produce Cell ◽  
Morphogenetic Factors ◽  
Positional Value

Growth and pattern formation occur simultaneously in many epimorphic fields and it has been suggested that specification of positional information is somehow linked to cell division. It is possible, therefore, that boundary regions responsible for the specification of positional information produce cell growth factors. In this paper I review the properties of some known growth factors, describe their effects on the cell cycle and discuss how they might act. In developing a convenient in vitro assay for morphogenetic factors it will be much easier to measure incorporation of [3H]thymidine into responding cells than to estimate changes in positional value.

scholarly journals Cell cycle expression of RNA duplex unwindase activity in mammalian cells.

1988 ◽  
Vol 8 (2) ◽  
pp. 770-777 ◽  
Author(s):  
R W Wagner ◽  
K Nishikura
Keyword(s):  
Cell Cycle ◽  
Burkitt Lymphoma ◽  
Mammalian Cells ◽  
Somatic Cells ◽  
Mouse Fibroblast ◽  
In Vitro Assay ◽  
3T3 Cells ◽  
Vitro Assay ◽  
Gel Retardation Assay

An RNA duplex unwindase activity has been found by using an in vitro assay with various types of mammalian, somatic cells, including HeLa, mouse plasmacytoma, and Burkitt lymphoma. The unwindase activity is very low in mouse fibroblast 3T3 cells arrested into quiescence, but increases when the cells are released into renewed growth by serum. In addition, a gel retardation assay proved to be specific and sensitive for detection of RNA duplex-unwindase complexes.

Cell cycle expression of RNA duplex unwindase activity in mammalian cells

1988 ◽  
Vol 8 (2) ◽  
pp. 770-777
Author(s):  
R W Wagner ◽  
K Nishikura
Keyword(s):  
Cell Cycle ◽  
Burkitt Lymphoma ◽  
Mammalian Cells ◽  
Somatic Cells ◽  
Mouse Fibroblast ◽  
In Vitro Assay ◽  
3T3 Cells ◽  
Vitro Assay ◽  
Gel Retardation Assay

An RNA duplex unwindase activity has been found by using an in vitro assay with various types of mammalian, somatic cells, including HeLa, mouse plasmacytoma, and Burkitt lymphoma. The unwindase activity is very low in mouse fibroblast 3T3 cells arrested into quiescence, but increases when the cells are released into renewed growth by serum. In addition, a gel retardation assay proved to be specific and sensitive for detection of RNA duplex-unwindase complexes.

scholarly journals The localization and phosphorylation of p47 are important for Golgi disassembly–assembly during the cell cycle

2003 ◽  
Vol 161 (6) ◽  
pp. 1067-1079 ◽  
Author(s):  
Keiji Uchiyama ◽  
Eija Jokitalo ◽  
Mervi Lindman ◽  
Mark Jackman ◽  
Fumi Kano ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Mammalian Cells ◽  
In Vitro Assay ◽  
Inhibitory Mechanism ◽  
Vitro Assay ◽  
Daughter Cells ◽  
Golgi Membranes ◽  
Golgi Fragmentation ◽  
Mitotic Phosphorylation

In mammalian cells, the Golgi apparatus is disassembled at the onset of mitosis and reassembled at the end of mitosis. This disassembly–reassembly is generally believed to be essential for the equal partitioning of Golgi into two daughter cells. For Golgi disassembly, membrane fusion, which is mediated by NSF and p97, needs to be blocked. For the NSF pathway, the tethering of p115-GM130 is disrupted by the mitotic phosphorylation of GM130, resulting in the inhibition of NSF-mediated fusion. In contrast, the p97/p47 pathway does not require p115-GM130 tethering, and its mitotic inhibitory mechanism has been unclear. Now, we have found that p47, which mainly localizes to the nucleus during interphase, is phosphorylated on Serine-140 by Cdc2 at mitosis. The phosphorylated p47 does not bind to Golgi membranes. An in vitro assay shows that this phosphorylation is required for Golgi disassembly. Microinjection of p47(S140A), which is unable to be phosphorylated, allows the cell to keep Golgi stacks during mitosis and has no effect on the equal partitioning of Golgi into two daughter cells, suggesting that Golgi fragmentation-dispersion may not be obligatory for equal partitioning even in mammalian cells.

In Vitro Assay of Platelet Adhesiveness with Washed and Tanned Human Red Cells

1968 ◽  
Vol 20 (03/04) ◽  
pp. 384-396 ◽  
Author(s):  
G Zbinden ◽  
S Tomlin
Keyword(s):  
Platelet Adhesion ◽  
Sodium Citrate ◽  
Blood Platelets ◽  
In Vitro Assay ◽  
Red Cells ◽  
Platelet Adhesiveness ◽  
Vitro Assay ◽  
In Vitro System ◽  
Human Red Cells

SummaryAn in vitro system is described in which adhesion of blood platelets to washed and tannic acid-treated red cells was assayed quantitatively by microscopic observation. ADP, epinephrine and TAME produced a reversible increase in platelet adhesiveness which was antagonized by AMP. With Evans blue, polyanetholsulfonate, phthalanilide NSC 38280, thrombin and heparin at concentrations above 1-4 u/ml the increase was irreversible. The ADP-induced increase in adhesiveness was inhibited by sodium citrate, EDTA, AMP, ATP and N-ethylmaleimide. EDTA, AMP and the SH-blocker N-ethylmaleimide also reduced spontaneous platelet adhesion to red cells. No significant effects were observed with adenosine, phenprocoumon, 5-HT, phthalanilide NSC 57155, various estrogens, progestogens and fatty acids, acetylsalicylic acid and similarly acting agents, hydroxylamine, glucose and KCN. The method may be useful for the screening of thrombogenic and antithrombotic properties of drugs.

A comparative study on adhesion and recovery of potential probiotic strains ofLactobacillusspp. by in vitro assay and analysis of human colon biopsies

2009 ◽  
Vol 21 (2) ◽  
Author(s):  
Nadja Larsen ◽  
Kim F. Michaelsen ◽  
Anders Pærregaard ◽  
Finn K. Vogensen ◽  
Mogens Jakobsen
Keyword(s):  
Comparative Study ◽  
Human Colon ◽  
In Vitro Assay ◽  
Vitro Assay ◽  
Probiotic Strains

Angiogenic Effect of Pravastatin Alone and with Sera from Healthy and Complicated Pregnancies Studied by in vitro Vasculogenesis/Angiogenesis Assay

2021 ◽  
pp. 1-9
Author(s):  
Anita Virtanen ◽  
Outi Huttala ◽  
Kati Tihtonen ◽  
Tarja Toimela ◽  
Tuula Heinonen ◽  
...  
Keyword(s):  
Direct Effect ◽  
Late Onset ◽  
Maternal Serum ◽  
In Vitro Assay ◽  
Serum Samples ◽  
Therapeutic Concentration ◽  
Tubule Formation ◽  
Vitro Assay ◽  
Angiogenesis Assay

<b><i>Objective:</i></b> To determine the direct effect of pravastatin on angiogenesis and to study the interaction between pravastatin and maternal sera from women with early- or late-onset pre-eclampsia (PE), intrauterine growth restriction, or healthy pregnancy. <b><i>Methods:</i></b> We collected 5 maternal serum samples from each group. The effect of pravastatin on angiogenesis was assessed with and without maternal sera by quantifying tubule formation in a human-based in vitro assay. Pravastatin was added at 20, 1,000, and 8,000 ng/mL concentrations. Concentrations of angiogenic and inflammatory biomarkers in serum and in test medium after supplementation of serum alone and with pravastatin (1,000 ng/mL) were measured. <b><i>Results:</i></b> Therapeutic concentration of pravastatin (20 ng/mL) did not have significant direct effect on angiogenesis, but the highest concentrations inhibited angiogenesis. Pravastatin did not change the levels of biomarkers in the test media. There were no changes in angiogenesis when therapeutic dose of pravastatin was added with maternal sera, but there was a trend to wide individual variation towards enhanced angiogenesis, particularly in the early-onset PE group. <b><i>Conclusions:</i></b> At therapeutic concentration, pravastatin alone or with maternal sera has no significant effect on angiogenesis, but at high concentrations the effect seems to be anti-angiogenic estimated by in vitro assay.

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