scholarly journals Analysis of Protein-Protein Interactions in Cross-talk Pathways Reveals CRKL Protein as a Novel Prognostic Marker in Hepatocellular Carcinoma

2013 ◽  
Vol 12 (5) ◽  
pp. 1335-1349 ◽  
Author(s):  
Chia-Hung Liu ◽  
Tzu-Chi Chen ◽  
Gar-Yang Chau ◽  
Yi-Hua Jan ◽  
Chun-Houh Chen ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Prognostic Marker ◽  
Cross Talk ◽  
Protein Interactions ◽  
Protein Protein Interactions

Protein-protein interactions of the p53 family with the Bcl-2 family in hepatocellular carcinoma

2011 ◽  
Vol 49 (08) ◽  
Author(s):  
LC König ◽  
M Meinhard ◽  
C Sandig ◽  
MH Bender ◽  
A Lovas ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
P53 Family

scholarly journals Insulin signalling: putting the G- in protein-protein interactions

2004 ◽  
Vol 380 (1) ◽  
pp. e11-e12 ◽  
Author(s):  
Craig C. MALBON
Keyword(s):  
Insulin Receptor ◽  
Cross Talk ◽  
Protein Interactions ◽  
Tyrosine Kinases ◽  
Cell Biology ◽  
Receptor Tyrosine Kinases ◽  
Insulin Signalling ◽  
Cell Signalling ◽  
Protein Protein Interactions ◽  
Proximal Point

Cell signalling via receptor tyrosine kinases, such as the insulin receptor, and via heterotrimeric G-proteins, such as Gαi, Gαs and Gαq family members, constitute two of most avidly studied paradigms in cell biology. That elements of these two populous signalling pathways must cross-talk to achieve proper signalling in the regulation of cell proliferation, differentiation and metabolism has been anticipated, but the evolution of our thinking and the analysis of such cross-talk have lagged behind the ever-expanding troupe of players and the recognition of multivalency as the rule, rather than the exception, in signalling biology. New insights have been provided by Kreuzer et al. in this issue of the Biochemical Journal, in which insulin is shown to provoke recruitment of Gαi-proteins to insulin-receptor-based complexes that can regulate the gain of insulin-receptor-catalysed autophosphorylation, a proximal point in the insulin-sensitive cascade of signalling. Understanding the convergence and cross-talk of signals from the receptor tyrosine kinases and G-protein-coupled receptor pathways in physical, spatial and temporal contexts will remain a major challenge of cell biology.

scholarly journals Pathway Analysis Based on Attractor and Cross Talk in Colon Cancer

2016 ◽  
Vol 2016 ◽  
pp. 1-7 ◽  
Author(s):  
Yanxia Liu ◽  
Lin Wang ◽  
Bingping Wang ◽  
Meng Yue ◽  
Yufeng Cheng
Keyword(s):  
Colon Cancer ◽  
Cross Talk ◽  
Protein Interactions ◽  
Microarray Data ◽  
Molecular Mechanisms ◽  
Linear Models ◽  
Impact Factors ◽  
Protein Protein Interactions ◽  
Common Cancer ◽  
Differential Expressed Genes

Colon cancer is the third and second most common cancer form in men and women worldwide. It is generally accepted that colon cancer mainly results from diet. The aim of this study was to identify core pathways which elucidated the molecular mechanisms in colon cancer. The microarray data of E-GEOD-44861 was downloaded from ArrayExpress database. All human pathways were obtained from Kyoto Encyclopedia of Genes and Genomes database. In total, 135 differential expressed genes (DEG) were identified using Linear Models for Microarray Data package. Differential pathways were identified with the method of attractor after overlapping with DEG. Pathway cross talk network (PCN) was constructed by combining protein-protein interactions and differential pathways. Cross talks of all pathways were obtained in PCN. There were 65 pathways with RankProd (RP) values < 0.05 and 16 pathways with Impact Factors (IF) values > 100. Five pathways were satisfied withPvalue < 0.05, RP values < 0.05, and IF values > 100, which were considered to be the most important pathways in colon cancer. In conclusion, the five pathways were identified in the center status of colon cancer, which may contribute to understanding the mechanism and development of colon cancer.

scholarly journals Differential modulation of transcriptional activity of oestrogen receptors by direct protein–protein interactions with retinoid receptors

1998 ◽  
Vol 336 (3) ◽  
pp. 711-717 ◽  
Author(s):  
Mi-Ryoung SONG ◽  
Soo-Kyung LEE ◽  
Young-Woo SEO ◽  
Hueng-Sik CHOI ◽  
Jae Woon LEE ◽  
...  
Keyword(s):  
Cross Talk ◽  
Protein Interactions ◽  
Oestrogen Receptors ◽  
Differential Modulation ◽  
Protein Protein Interactions ◽  
Glutathione S Transferase ◽  
Retinoid Receptors ◽  
Binding Domains ◽  
X Receptors

Control of oestradiol-responsive gene regulation by oestrogen receptors (ERs) may involve complex cross-talk with retinoic acid receptors (RARs) and retinoid X receptors (RXRs). Recently, we have shown that ERα directly interacts with RARα and RXRα through their ligand binding domains (LBDs). In the present work, we extend these results by showing that ERβ binds similarly to RARα and RXRα but not to the glucocorticoid receptor, as demonstrated by the yeast two-hybrid tests and glutathione S-transferase pull-down assays. These direct interactions were also demonstrated in gel-shift assays, in which the oestrogen response element (ERE) binding by ERα was enhanced by the RXRα LBD but was abolished by the RARα LBD. In addition, we showed that RARα and RXRα bound the ERE as efficiently as ERα, suggesting that competition for DNA binding may affect the transactivation function of the ER. In transient transfection experiments, co-expression of RARα or RXRα, along with ERα or ERβ, revealed differential modulation of the ERE-dependent transactivation, which was distinct from the results when each receptor alone was co-transfected. Importantly, when the LBD of RARα was co-expressed with ERα, transactivation of ERα on the ERE was repressed as efficiently as when wild-type RARα was co-expressed. Furthermore, liganded RARα or unliganded RXRα enhanced the ERα transactivation, suggesting the formation of transcriptionally active heterodimer complexes between the ER and retinoid receptors. Taken together, these results suggest that direct protein–protein interactions may play major roles in the determination of the biological consequences of cross-talk between ERs and RARα or RXRα.

scholarly journals Stat1-Vitamin D Receptor Interactions Antagonize 1,25-Dihydroxyvitamin D Transcriptional Activity and Enhance Stat1-Mediated Transcription

2002 ◽  
Vol 22 (8) ◽  
pp. 2777-2787 ◽  
Author(s):  
Marcos Vidal ◽  
Chilakamarti V. Ramana ◽  
Adriana S. Dusso
Keyword(s):  
Vitamin D ◽  
Vitamin D Receptor ◽  
Cross Talk ◽  
Protein Interactions ◽  
Nuclear Accumulation ◽  
Protein Protein Interactions ◽  
Dihydroxyvitamin D ◽  
1,25 Dihydroxyvitamin D ◽  
Key Enzyme ◽  
Ifn Γ

ABSTRACT The cytokine gamma interferon (IFN-γ) and the calcitropic steroid hormone 1,25-dihydroxyvitamin D (1,25D) are activators of macrophage immune function. In sarcoidosis, tuberculosis, and several granulomatoses, IFN-γ induces 1,25D synthesis by macrophages and inhibits 1,25D induction of 24-hydroxylase, a key enzyme in 1,25D inactivation, causing high levels of 1,25D in serum and hypercalcemia. This study delineates IFN-γ-1,25D cross talk in human monocytes-macrophages. Nuclear accumulation of Stat1 and vitamin D receptor (VDR) by IFN-γ and 1,25D promotes protein-protein interactions between Stat1 and the DNA binding domain of the VDR. This prevents VDR-retinoid X receptor (RXR) binding to the vitamin D-responsive element, thus diverting the VDR from its normal genomic target on the 24-hydroxylase promoter and antagonizing 1,25D-VDR transactivation of this gene. In contrast, 1,25D enhances IFN-γ action. Stat1-VDR interactions, by preventing Stat1 deactivation by tyrosine dephosphorylation, cooperate with IFN-γ/Stat1-induced transcription. This novel 1,25D-IFN-γ cross talk explains the pathogenesis of abnormal 1,25D homeostasis in granulomatous processes and provides new insights into 1,25D immunomodulatory properties.

Partial Purification of a Specific Plasminogen Activator from Porcine Parotid Glands

1974 ◽  
Vol 31 (03) ◽  
pp. 403-414 ◽  
Author(s):  
Terence Cartwright
Keyword(s):  
Nucleic Acid ◽  
Salivary Glands ◽  
Plasminogen Activator ◽  
Protein Interactions ◽  
Partial Purification ◽  
Protein Protein Interactions ◽  
Parotid Glands ◽  
Two Stage ◽  
Preliminary Characterization ◽  
Specific Inhibitors

SummaryA method is described for the extraction with buffers of near physiological pH of a plasminogen activator from porcine salivary glands. Substantial purification of the activator was achieved although this was to some extent complicated by concomitant extraction of nucleic acid from the glands. Preliminary characterization experiments using specific inhibitors suggested that the activator functioned by a similar mechanism to that proposed for urokinase, but with some important kinetic differences in two-stage assay systems. The lack of reactivity of the pig gland enzyme in these systems might be related to the tendency to protein-protein interactions observed with this material.

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