scholarly journals In Vitro Analysis of Light-Induced Transcription in the Wheat psbD/C Gene Cluster Using Plastid Extracts from Dark-Grown and Short-Term-Illuminated Seedlings

1994 ◽  
Vol 104 (4) ◽  
pp. 1259-1267 ◽  
Author(s):  
T. Wada ◽  
Y. Tunoyama ◽  
T. Shiina ◽  
Y. Toyoshima
Keyword(s):  
Gene Cluster ◽  
Short Term ◽  
Vitro Analysis ◽  
In Vitro Analysis

scholarly journals Comparative short-term in vitro analysis of mutans streptococci adhesion on esthetic, nickel-titanium, and stainless-steel arch wires

2014 ◽  
Vol 84 (4) ◽  
pp. 680-686 ◽  
Author(s):  
In-Hye Kim ◽  
Hyo-Sang Park ◽  
Young Kyung Kim ◽  
Kyo-Han Kim ◽  
Tae-Yub Kwon
Keyword(s):  
Stainless Steel ◽  
Nickel Titanium ◽  
Mutans Streptococci ◽  
Short Term ◽  
Vitro Analysis ◽  
In Vitro Analysis

scholarly journals The Effect of Different Cleaning Methods on Protein Deposition and Optical Characteristics of Orthokeratology Lenses

Polymers ◽  
2021 ◽  
Vol 13 (24) ◽  
pp. 4318
Author(s):  
Chen-Ying Su ◽  
Lung-Kun Yeh ◽  
Yi-Fei Tsao ◽  
Wen-Pin Lin ◽  
Chiun-Ho Hou ◽  
...  
Keyword(s):  
Optical Characteristics ◽  
Short Term ◽  
Protein Deposition ◽  
Tear Proteins ◽  
Cleaning Methods ◽  
Vitro Analysis ◽  
In Vitro Analysis ◽  
Myopia Control

Orthokeratology lenses are commonly used for myopia control, especially in children. Tear lipids and proteins are immediately adsorbed when the lens is put on the cornea, and protein deposition may cause discomfort or infection. Therefore, we established an in vitro protein deposition analysis by mimicking the current cleaning methods for orthokeratology lens wearers for both short-term and long-term period. The results showed that the amounts of tear proteins accumulated daily and achieved a balance after 14 days when the lens was rubbed to clean or not. Protein deposition also affected the optical characteristics of the lens regardless of cleaning methods. Our results provided an in vitro analysis for protein deposition on the lens, and they may provide a potential effective method for developing care solutions or methods that can more effectively remove tear components from orthokeratology lenses.

scholarly journals Crosstalk of Endothelial and Mesenchymal Stromal Cells under Tissue-Related O2

2021 ◽  
Vol 1 (2) ◽  
pp. 116-136
Author(s):  
Olga Zhidkova ◽  
Elena Andreeva ◽  
Mariia Ezdakova ◽  
Ludmila Buravkova
Keyword(s):  
Mesenchymal Stromal Cells ◽  
Stromal Cells ◽  
Reciprocal Effects ◽  
Hypoxic Stress ◽  
Protective Effects ◽  
Short Term ◽  
Tnf Α ◽  
Vitro Analysis ◽  
In Vitro Analysis

Mesenchymal stromal cells (MSCs) are considered a valuable tool for cell therapy. After systemic administration, the outcome of MSCs and endothelial cells (ECs) interactions strongly depend on the local microenvironment and tissue O2 levels in particular. In vitro analysis of EC effects on MSC regenerative potential in co-culture was performed after short-term interaction at “physiological” hypoxia (5% O2) and acute hypoxic stress (0.1% O2). At 5% O2, MSCs retained stromal phenotype and CFU-f numbers, osteogenic RUNX2 was upregulated. A shift in the expression of adhesion molecules, and an increase in transcription/synthesis of IL-6, IL-8 contributed to facilitation of directed migration of MSCs. In the presence of MSCs, manifestations of oxidative stress in ECs were attenuated, and a decrease in adhesion of PBMCs to TNF-α-activated ECs was observed. Under 0.1% O2, reciprocal effects of ECs and MSCs were similar to those at 5% O2. Meanwhile, upregulation of RUNX2 was canceled, IL-6 decreased, and IL-8 significantly increased. “Protective” effects of MSCs on TNF-α-ECs were less pronounced, manifested as NOS3 downregulation and intracellular NO elevation. Therefore, interaction with ECs at “physiological” hypoxia enhanced pro-regenerative capacities of MSCs including migration and anti-inflammatory modulation of ECs. Under acute hypoxic stress, the stimulating effects of ECs on MSCs and the “protective” potential of MSCs towards TNF-α-ECs were attenuated.

scholarly journals C-Methylation of S-adenosyl-L-Methionine Occurs Prior to Cyclopropanation in the Biosynthesis of 1-Amino-2-Methylcyclopropanecarboxylic Acid (Norcoronamic Acid) in a Bacterium

Biomolecules ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 775
Author(s):  
Chitose Maruyama ◽  
Yukiko Chinone ◽  
Shusuke Sato ◽  
Fumitaka Kudo ◽  
Kosuke Ohsawa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Gene Cluster ◽  
Acc Synthase ◽  
Building Blocks ◽  
The Other ◽  
Recombinant Enzymes ◽  
Radical Sam ◽  
Vitro Analysis ◽  
In Vitro Analysis

Many pharmacologically important peptides are bacterial or fungal in origin and contain nonproteinogenic amino acid (NPA) building blocks. Recently, it was reported that, in bacteria, a cyclopropane-containing NPA 1-aminocyclopropanecarboxylic acid (ACC) is produced from the L-methionine moiety of S-adenosyl-L-methionine (SAM) by non-canonical ACC-forming enzymes. On the other hand, it has been suggested that a monomethylated ACC analogue, 2-methyl-ACC (MeACC), is derived from L-valine. Therefore, we have investigated the MeACC biosynthesis by identifying a gene cluster containing bacterial MeACC synthase genes. In this gene cluster, we identified two genes, orf29 and orf30, which encode a cobalamin (B12)-dependent radical SAM methyltransferase and a bacterial ACC synthase, respectively, and were found to be involved in the MeACC biosynthesis. In vitro analysis using their recombinant enzymes (rOrf29 and rOrf30) further revealed that the ACC structure of MeACC was derived from the L-methionine moiety of SAM, rather than L-valine. In addition, rOrf29 was found to catalyze the C-methylation of the L-methionine moiety of SAM. The resulting methylated derivative of SAM was then converted into MeACC by rOrf30. Thus, we demonstrate that C-methylation of SAM occurs prior to cyclopropanation in the biosynthesis of a bacterial MeACC (norcoronamic acid).

The native structure of the eukaryotic ribosome

1983 ◽  
Vol 41 ◽  
pp. 432-433
Author(s):  
R.A. Milligan ◽  
P.N.T. Unwin
Keyword(s):  
Ribosomal Proteins ◽  
Crystal Form ◽  
Native Structure ◽  
X Ray Diffraction ◽  
Eukaryotic Ribosome ◽  
Vitro Analysis ◽  
In Vitro Analysis ◽  
Resolution Structure ◽  
Stable Unit

A detailed understanding of the mechanism of protein synthesis will ultimately depend on knowledge of the native structure of the ribosome. Towards this end we have investigated the low resolution structure of the eukaryotic ribosome embedded in frozen buffer, making use of a system in which the ribosomes crystallize naturally.The ribosomes in the cells of early chicken embryos form crystalline arrays when the embryos are cooled at 4°C. We have developed methods to isolate the stable unit of these arrays, the ribosome tetramer, and have determined conditions for the growth of two-dimensional crystals in vitro, Analysis of the proteins in the crystals by 2-D gel electrophoresis demonstrates the presence of all ribosomal proteins normally found in polysomes. There are in addition, four proteins which may facilitate crystallization. The crystals are built from two oppositely facing P4 layers and the predominant crystal form, accounting for >80% of the crystals, has the tetragonal space group P4212, X-ray diffraction of crystal pellets demonstrates that crystalline order extends to ~ 60Å.

1163: Radial Dilation of Ureteral Balloons: A Comparative in-Vitro Analysis

2005 ◽  
Vol 173 (4S) ◽  
pp. 315-316
Author(s):  
Kari Hendlin ◽  
Brynn Lund ◽  
Manoj Monga
Keyword(s):  
Vitro Analysis ◽  
In Vitro Analysis
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