Open Access. Powered by Scholars. Published by Universities.®
- Institution
- Keyword
-
- 2D Gels (1)
- Adenine (1)
- Agonists (1)
- Colorectal Neoplasms (1)
- DNA (1)
-
- Experimental Design (1)
- False Discovery Rate (1)
- Gene Expression Profiling (1)
- HCT116 Cells (1)
- HMGB (1)
- Human (1)
- Laser Capture (1)
- Mass Spectrometry (1)
- Neoplastic drug effects (1)
- PPAR gamma physiology (1)
- Peptides (1)
- Pharmacology (1)
- Progesterone (1)
- Prostaglandin D2 (1)
- Proteins (1)
- Proteomics (1)
- Randomization (1)
- Receptors (1)
- Regulation (1)
- Reverse Transcriptase Polymerase Chain Reaction (1)
- Signal Transduction (1)
- Thiazolidinediones (1)
- Thymine (1)
- Transcriptional Activation (1)
Articles 1 - 4 of 4
Full-Text Articles in Molecular Biology
Gene Alterations By Peroxisome Proliferator-Activated Receptor Gamma Agonists In Human Colorectal Cancer Cells, Maria Cekanova, J Yuan, X Li, K B. Kim, Seung J. Baek
Gene Alterations By Peroxisome Proliferator-Activated Receptor Gamma Agonists In Human Colorectal Cancer Cells, Maria Cekanova, J Yuan, X Li, K B. Kim, Seung J. Baek
Maria Cekanova MS, RNDr, PhD
The peroxisome proliferator-activated receptor gamma (PPARgamma) is a nuclear transcription factor that controls the genes involved in metabolism and carcinogenesis. In the present study, we examined the alteration of gene expression in HCT-116 human colorectal cancer cells by PPARgamma agonists: MCC-555 (5 microM), rosiglitazone (5 microM), and 15-deoxy-Delta12,14-prostaglandin J2 (1 microM). The long-oligo microarray data revealed a list of target genes commonly induced (307 genes) and repressed (32 genes) by tested PPARgamma agonists. These genes were analyzed by Onto-Express software and KEGG pathway analysis and revealed that PPARgamma agonists are involved in cell proliferation, focal adhesion, and several signaling pathways. …
Microproteomics: Analysis Of Protein Diversity In Small Samples, Howard B. Gutstein, Jeffrey S. Morris, Suresh P. Annangudi, Jonathan V. Sweedler
Microproteomics: Analysis Of Protein Diversity In Small Samples, Howard B. Gutstein, Jeffrey S. Morris, Suresh P. Annangudi, Jonathan V. Sweedler
Jeffrey S. Morris
Proteomics, the large-scale study of protein expression in organisms, offers the potential to evaluate global changes in protein expression and their post-translational modifications that take place in response to normal or pathological stimuli. One challenge has been the requirement for substantial amounts of tissue in order to perform comprehensive proteomic characterization. In heterogeneous tissues, such as brain, this has limited the application of proteomic methodologies. Efforts to adapt standard methods of tissue sampling, protein extraction, arraying, and identification are reviewed, with an emphasis on those appropriate to smaller samples ranging in size from several microliters down to single cells. The …
Analogy Of Issr And Rapd Markers For Comparative Analysis Of Genetic Diversity Among Different Jatropha Curcas Genotypes, Shailesh K. Tiwari Dr.
Analogy Of Issr And Rapd Markers For Comparative Analysis Of Genetic Diversity Among Different Jatropha Curcas Genotypes, Shailesh K. Tiwari Dr.
Shailesh K Tiwari Dr.
The phylogenetic relationships of 13 Jatropha genotypes from different parts of the India were analysed using 34 polymerase chain reaction (PCR) markers (20 random amplified polymorphic DNAs (RAPDs) and 14 inter simple sequence repeats (ISSRs)). Amplification of genomic DNA of the 13 genotypes, using RAPD analysis, yielded 107 fragments that could be scored, of which 91 were polymorphic, with an average of 4.55 polymorphic fragments per primer. Number of amplified fragments ranged from one (OPA20, OPB19, OPD13) to nine (OPA18) and which varied in size from 200 to 2,500 bp. Percentage of polymorphism ranged from 40% (OPB18) to a maximum …
Mechanism Of High-Mobility Group Protein B Enhancement Of Progesterone Receptor Sequence-Specific Dna Binding, James S. Adelman, Sarah C. Roemer, Mair E.A. Churchill, Dean P. Edwards
Mechanism Of High-Mobility Group Protein B Enhancement Of Progesterone Receptor Sequence-Specific Dna Binding, James S. Adelman, Sarah C. Roemer, Mair E.A. Churchill, Dean P. Edwards
James S. Adelman
The DNA-binding domain (DBD) of progesterone receptor (PR) is bipartite containing a zinc module core that interacts with progesterone response elements (PRE), and a short flexible carboxyl terminal extension (CTE) that interacts with the minor groove flanking the PRE. The chromosomal high-mobility group B proteins (HMGB), defined as DNA architectural proteins capable of bending DNA, also function as auxiliary factors that increase the DNA-binding affinity of PR and other steroid receptors by mechanisms that are not well defined. Here we show that the CTE of PR contains a specific binding site for HMGB that is required for stimulation of PR-PRE …