Oxidative Stress Key Research Data and Analysis

ULK1 was also tested in vitro in order to determine it could serve as a direct AMPK substrate. A kinase inactive kinase allele was made to remove autophosphorylation properties that ULK1 may have. Also, ULK1 phosphorylation by AMPK was compared to raptor – an established substrate. In addition, the group also created phosphospecific antibodies that acted against Ser 467 and Ser 555. This was done in order to understand phosphorylation under the absence of energy stress.

Would the GFP gene in a pGLO transformed E. coli be activated by a sugar other than arabinose?

Determining the Production of Glucose During Changes in Temperature and pH, and Manipulation of Specificity and Cofactors

Journal of Chemical Education , 81 (5), 702-704. Pohle, T., Brändlein, S., Ruoff, N., Müller-Hermelink, H. K., & Vollmers, H. P. (2004). Lipoptosis Tumor-Specific Cell Death by Antibody-Induced Intracellular Lipid Accumulation. Cancer Research , 64, 3900.

1,2-Dipalmitoyl-sn-glycerol (1,2-DPG) is an analog of the protein kinase C (PKC)-activating second messenger diacylglycerol [1].

Several upstream kinases have been reported to activate AMPK, including liver kinase B 1 (LKB1) [12]. LKB1 is predominately localized in the nucleus under normal physiological condition, and is translocated to cytosol in response to stimulation, which leads to subsequent AMPK phosphorylation and activation [13]. When activated, AMPK decreases fatty acid levels by phosphorylating and thus inhibiting acetyl-CoA carboxylases (ACC), a critical enzyme for controling fatty acid biosynthesis and oxidation [14]. The activation of AMPK also decreases total cholesterol (TC) and triglyceride (TG) levels by inhibiting the activity of glycerol-3-phosphate acyltransferase (GPAT) and HMG-CoA reductase, respectively [15]. AMPK has therefore been proposed as a major therapeutic target for obesity and obesity-linked metabolic disorders such as hyperlipidemia and atherosclerosis [16]. 5-Aminoimidazole-4-carboxamide-1-b-D- ribofuranoside (AICAR) is one of the activators of AMPK

1,2-Dipalmitoyl-sn-glycerol (1,2-DPG) was a weak activator of PKC. 1,2-Dipalmitoyl-sn-glycerol at 25 µM activated 15% of PKC [1].

Annexing V FITIC/PI was used to detect for the involvement of apoptosis based upon externalization of phospholipid phosphatidylserine (PS) and permeabilization of nuclear membrane for staining with PI. PS is a biomarker of early apoptotic stage, Annexin V has specific and high affinity for the anionic PS, when PS is exposed on cell surface Annexing V binds to it. PS indicates intermediate stages of apoptosis. Caspases-3 activation, nuclear fragmentation and mitochondrial membrane flux preceded PS translocation [46]. From Fig.5 sonicated pectin induced dose apoptosis and reduced proportion of viable cells. The 400W sonicated pectin was more potent apoptosis inducer than 200W sonicated pectin. control cells had 89.29% viable cells 3.14% early apoptotic cells and 6.50% late apoptosis, 400W sonicated pectin at 0.1 and 0.5mg/ml induced significant reduction in viable cells to 70.90%, early apoptotic cells were 4.84% and late apoptosis 14.94% in the cells as shown in Fig.5b, on the other hand, 0.5mg/ml led to 50.79% viable cells, 22.65 %early apoptotic cells and 19.56% late apoptotic cells as shown in Fig.

Notably, in congruent with our finding, NAC has been shown to provide cysteine to cells even in the absence of cysteine transport [47, 48]. Interestingly, the present finding also suggests a possibility that oxidative stress can regulate EAAC1 since NAC prevented the E-induced EAAC1 loss (Fig 7C). In support of this finding, under stressful conditions, such as oxidative and chemical stress, regulation and/or alteration of EAAC1 are evident at the level of expression, activity, and its membrane trafficking [49-52]. Clinically, NAC is the widely used Cys prodrug due to its safety, tolerability, and its ability to undergo rapid hydrolysis to deliver Cys immediately following cellular entry [46, 53, 54].

(CDKs) cyclin-dependent kinases are a family of serine/threonine kinases that are controlling progression throughout the cell cycle. In this review the main focus is going to be on cyclin D1 and other similar manner of functions. Cyclin D1 plays one of the most important roles in the cell cycle, because it will lead to progression through association with CDK4 and CDK6. The problem discussed is that within Cyclin D1 the DNA damage response and repairs alarms the chromosome stability. Metastasis has become a major cause of death in cancer patients that resulted in studies of cellular migration making it essential for tumor metastasis. Scientist have figured out that cyclin D1 binding of pk27 contributed to cellular migration. The review very comprehensive it is 9 pages of solid information even though 4 of the 9 pages are references. No, all the references are not related to the problem under

DMBA is an effective chemical used to induce breast tumorigenesis in rats. In this study, DMBA treatment led to the development of tumors by rats as revealed by tumorigenesis analyses and the histopathological examination. Treatment with lycopene reversed the pathological changes showing the efficiency of lycopene in breast tumor treatment. This result was in accordance with previous studies where lycopene alone or in combination with other products was proven to have anti-tumor activity.

Sphingosine 1-phosphate, a product of sphingosine kinases (SphK), mediates various biological processes including cell proliferation, differentiation, motility, and apoptosis. Protein kinase C (PKC), is a family of protein kinase enzymes involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues.

Histone acetylation is regulated by two covalent modifying enzymes, acetylases and deacetylases, and plays a key role in gene expression of eukaryotes. It has been revealed that histone deacetylase (HDAC), which is overexpressed in several tumor cells. plays a critical role in carcinogenesis. Moreover, plenty of studies have showed that the expression of tumor suppressors including p53, p21, and gelsolin, are repressed, whereas, tumor activators including hypoxia-induced factor-1 and vascular endothelial growth factor, are up-regulated in HDAC-overexpressed cells.

(2004) suggests that that the serum- and glucocorticoid-inducible kinase (SGK) acts parallel to the ATK kinases, atk-1 and atk-2, by forming a complex together that is activated by PDK-1. Each of these kinases are able to phosphorylate DAF-16 and prevent dauer arrest. Interestingly, while all three kinases work to suppress DAF-16, the ATK kinases play a larger role of regulating dauer formation, while SGK controls the stress response, development and longevity of the organism. This was discovered by performing rescue experiments on organisms with knockout mutations of sgk-1, akt-1 and akt-2. From these experiments, they found that SGK-1, ATK-1 and ATK-2 form a complex that is activated by PDK-1 and phosphorylated. When all three of these kinases are inactivated, DAF-16 is not phosphorylated and as a result the percentage of larvae entering the dauer stage increases. Thus, they concluded that these kinases act through the same mechanism to prevent dauer arrest. On the other hand, when they supplemented a daf-16 mutant with the triple sgk-1, atk-1 and atk-2 mutant, dauer arrest was only partially blocked. In the supplemented daf-16 mutant, dauer arrest is blocked completely when the DAF-2 receptor is also knocked out. This suggests the presence of another pathway from the DAF-2 receptor that turns off the DAF-16 transcription factor. (Hertwick,

In human HSCs, activation of AMPK inhibits several profibrogenic actions including; cell proliferation and migration, chemokine secretion and collagen production. The processes accompanying HSC activation and particularly cell division are energetically demanding and need sufficient metabolic resources. Because AMPK activity is repressed by a large availability of nutrients, this pathway may be viewed as a mechanism linking the excess of substrates typical of the metabolic syndrome with a faster development of fibrosis. Since pharmacological agents, such as 5-aminoimidazole-4-carboxamide-1-beta-4- ribofuranoside (AICAR) and metformin can activate AMPK, they may also act as antifibrogenic agents (Caligiuri et al.,