scholarly journals A novel in vitro approach for enhanced production of Musa paradisiaca L. (cv. Nendran) using split sucker explants.

2016 ◽  
Vol 4 (8) ◽  
pp. 696-703
Author(s):  
RadhikaB.J Ravichandran ◽  
◽  
K. Satheeshkumar. ◽  
Keyword(s):  
Musa Paradisiaca ◽  
Enhanced Production

scholarly journals High Frequency Plant Regeneration of Musa paradisiaca cv. Karibale Monthan

2015 ◽  
Vol 3 (2) ◽  
pp. 202-209 ◽  
Author(s):  
R. Shashi Kumar ◽  
V. Krishna ◽  
. Venkatesh
Keyword(s):  
Plant Regeneration ◽  
High Frequency ◽  
Synergetic Effect ◽  
Multiple Shoot ◽  
Coconut Water ◽  
Morphological Variations ◽  
Musa Paradisiaca ◽  
Shoot Initiation

High frequency plant regeneration protocol has been standardized from banana cultivar Musa paradisiaca cv. Karibale Monthan, an endemic cultivar of Malnad region of Karnataka. The fruits are used as glomerular protective to solve kidney problems. To minimize the microbial contamination and to promote healthy growth, explants were treated with 70 % absolute alcohol for 6 min, 0.1 % Mercuric chloride for 10 min and 0.2 % for 10 min, 1 % Sodium hypochlorite for 15 min, 0.1 % Cefotaxime for 5 min and 0.05 % Gentamicin for 5 min. The high frequency shoot initiation (93.33 %) was recorded at 5 mg/l BAP. The synergetic effect of BAP (4 to 6 mg/l), TDZ (0.1 to 1.2 mg/l) and coconut water (0.1 to 0.9 ml/l) induced multiple shoot buds and it was optimized at the concentration of 5 mg/l BAP, 0.5 mg/l TDZ and 0.5 ml/l coconut water with 15.90 ± 1.66 frequency of shoots per propagule. Supplementation of 1.0 mg/l IBA induced 5.33 ± 1.21 numbers of roots with a mean root length of 7.50 ± 1.87 roots. The 99% of plantlets with distinct roots and shoots were successfully acclimatized in the green house and transferred to the field to evaluate the agro-morphological variations. The weight of the bunch (kg), number of hands in a bunch, number of fingers in a hand, length of the finger (cm), girth of the finger (cm) and girth of the pseudostem (cm) exhibited by in vitro plants were higher than the in vivo plants.Int J Appl Sci Biotechnol, Vol 3(2): 202-209 DOI: http://dx.doi.org/10.3126/ijasbt.v3i2.12536 

Carbon dioxide inhalation causes pulmonary inflammation

2009 ◽  
Vol 296 (4) ◽  
pp. L657-L665 ◽  
Author(s):  
Mohammad Abolhassani ◽  
Adeline Guais ◽  
Philippe Chaumet-Riffaud ◽  
Annie J. Sasco ◽  
Laurent Schwartz
Keyword(s):  
Carbon Dioxide ◽  
Nuclear Translocation ◽  
Rnase Protection Assay ◽  
Airway Hyperreactivity ◽  
Cellular Respiration ◽  
Rnase Protection ◽  
Monocyte Chemoattractant Protein 1 ◽  
Enhanced Production

The aim of this study was to assess whether one of the most common poisons of cellular respiration, i.e., carbon dioxide, is proinflammatory. CO2 is naturally present in the atmosphere at the level of 0.038% and involved in numerous cellular biochemical reactions. We analyzed in vitro the inflammation response induced by exposure to CO2 for 48 h (0–20% with a constant O2 concentration of 21%). In vivo mice were submitted to increasing concentrations of CO2 (0, 5, 10, and 15% with a constant O2 concentration of 21%) for 1 h. The exposure to concentrations above 5% of CO2 resulted in the increased transcription (RNase protection assay) and secretion (ELISA) of proinflammatory cytokines [macrophage inflammatory protein-1α (MIP-1α), MIP-1β, MIP-2, IL-8, IL-6, monocyte chemoattractant protein-1, and regulated upon activation, normal T cell expressed, and, presumably, secreted (RANTES)] by epithelial cell lines HT-29 or A549 and primary pulmonary cells retrieved from the exposed mice. Lung inflammation was also demonstrated in vivo by mucin 5AC-enhanced production and airway hyperreactivity induction. This response was mostly mediated by the nuclear translocation of p65 NF-κB, itself a consequence of protein phosphatase 2A (PP2A) activation. Short inhibiting RNAs (siRNAs) targeted toward PP2Ac reversed the effect of carbon dioxide, i.e., disrupted the NF-κB activation and the proinflammatory cytokine secretion. In conclusion, this study strongly suggests that exposure to carbon dioxide may be more toxic than previously thought. This may be relevant for carcinogenic effects of combustion products.

scholarly journals Effect of dimethyl sulfoxide on human carcinoma cells, inhibition of plasminogen activator synthesis, change in cell morphology, and alteration of response to cholera toxin.

1985 ◽  
Vol 5 (12) ◽  
pp. 3552-3559 ◽  
Author(s):  
L Ossowski ◽  
D Belin
Keyword(s):  
Dimethyl Sulfoxide ◽  
Cholera Toxin ◽  
Plasminogen Activator ◽  
Cell Morphology ◽  
Control Level ◽  
Metastatic Potential ◽  
Inhibitory Effect ◽  
Human Carcinoma ◽  
Enhanced Production

Human carcinoma HEp-3 lost its tumorigenic and metastatic potential upon prolonged culture in vitro. This change was accompanied by a reduced production of plasminogen activator (PA) of the urokinase type (uPA), which is secreted by HEp-3 cells, a change in response to effectors that modulate uPA production, and an alteration of cell morphology. Similar but more rapid changes occurred when malignant HEp-3 cells were exposed to dimethyl sulfoxide (DMSO). uPA activity in the culture medium dropped below 50% of the control level within 6 h after the addition of DMSO and became undetectable after 24 h of treatment. This drop in uPA activity was not caused by an increased production of PA inhibitors. The cell-associated uPA decreased to 25 to 30% of the control level within 6 h of DMSO treatment and remained at this level for at least 96 h; the reduced uPA production was partially accounted for by a rapid decrease in the functional and chemical concentration of uPA mRNA. In contrast, the concentrations of most of the abundant mRNA species did not appear to be significantly affected, and cell growth was only slightly inhibited in the presence of DMSO. Malignant HEp-3 cells treated with DMSO responded to cholera toxin with an enhanced production of uPA, and their morphology became indistinguishable from that of nonmalignant HEp-3 cells grown in vitro for prolonged periods of time. All of the above changes were fully and rapidly reversible. The inhibitory effect of DMSO on PA production appears to be specific for uPA of human cell lines.

scholarly journals Phagocytosis by Human Monocytes

Blood ◽  
1968 ◽  
Vol 32 (3) ◽  
pp. 423-435 ◽  
Author(s):  
MARTIN J. CLINE ◽  
ROBERT I. LEHRER
Keyword(s):  
Rna Synthesis ◽  
Glucose Utilization ◽  
Human Monocytes ◽  
Igg Antibody ◽  
Enhanced Production ◽  
Serum Fractions ◽  
Particle Ingestion ◽  
Ph Range ◽  
Total Glucose

Abstract Human monocytes isolated from peripheral blood phagocytized polystyrene particles, Escherichia coli, Staphylococcus aureus, Candida albicans, Cryptococcus neoformans, and red cells coated with IgG antibody in vitro. The ingestion of fungi and bacteria required serum or serum fractions. Ingestion of antibody-coated erythrocytes was inhibited by whole serum or IgG, but not by IgM or albumin. Adherence to a surface appeared to be critical for erythrophagocytosis but not for ingestion of bacteria. Phagocytosis occurred over a broad pH range and in the presence of inhibitors of oxidative metabolism and of RNA synthesis. Phagocytosis was significantly depressed by inhibitors of glycolysis (iodoacetate and fluoride) and by chloroquine at 1 x 10-5M. Particle ingestion by monocytes was accompanied by enhanced production of C14O2 from glucose-1-C14, but was not associated with a detectable increase in total glucose utilization, incorporation of radioactive uridine into RNA, or incorporation of amino acids into protein.

scholarly journals Resistance of cytolytic lymphocytes to perforin-mediated killing. Induction of resistance correlates with increase in cytotoxicity.

1989 ◽  
Vol 169 (6) ◽  
pp. 2211-2225 ◽  
Author(s):  
C C Liu ◽  
S Jiang ◽  
P M Persechini ◽  
A Zychlinsky ◽  
Y Kaufmann ◽  
...  
Keyword(s):  
Killer Cell ◽  
Cell Types ◽  
Serine Esterase ◽  
Short Term ◽  
Lymphokine Activated Killer Cells ◽  
Killer Cells ◽  
Enhanced Production ◽  
Induction Of Resistance ◽  
Lymphocyte Populations

CTL and NK cells cultured in vitro are known to produce a cytolytic pore-forming protein (PFP, perforin) localized in their cytoplasmic granules. Using purified perforin, we showed here that both cloned CTL and primary killer cell populations, including allospecific CTL, NK/lymphokine-activated killer cells, and MHC-non-restricted CTL, were more resistant to perforin-mediated killing than other lymphocyte populations and cell types. Similar results were obtained with both murine and human cytolytic lymphocyte populations. Resistance of killer cells to perforin correlated in general with their cytolytic capability. Thus, cells that have acquired competence to kill after stimulation with Con A, IL-2, or leukocyte-conditioned medium, were also the more resistant cells. IL-2-independent CTL lines and hybridomas derived in our laboratories could be triggered to become cytotoxic and perforin resistant by short-term stimulation with various cytokines, indicating that the acquisition of resistance to perforin-mediated lysis was independent of cell proliferation. Activation of one IL-2-independent CTL line with IL-2 also resulted in enhanced production of perforin and in enhanced serine esterase activity. The acquisition of cell resistance to perforin by these IL-2-independent cell lines after activation with stimulatory reagents was independent of protein and RNA neosynthesis: emetine, cycloheximide, and actinomycin D, while effectively blocking the incorporation of [35S]methionine into cell proteins, did not affect the induced increase in perforin resistance.

scholarly journals Impairment of amyloid precursor protein alpha-processing in cerebral microvessels of type 1 diabetic mice

2017 ◽  
Vol 39 (6) ◽  
pp. 1085-1098
Author(s):  
Tongrong He ◽  
Ruohan Sun ◽  
Anantha VR Santhanam ◽  
Livius V d'Uscio ◽  
Tong Lu ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Local Concentration ◽  
Microvascular Endothelium ◽  
Cerebral Microvessels ◽  
Protein Levels ◽  
Enhanced Production ◽  
Amyloidogenic Processing

The mechanisms underlying dysfunction of cerebral microvasculature induced by type 1 diabetes (T1D) are not fully understood. We hypothesized that in cerebral microvascular endothelium, α-processing of amyloid precursor protein (APP) is impaired by T1D. In cerebral microvessels derived from streptozotocin (STZ)-induced T1D mice protein levels of APP and its α-processing enzyme, a disintegrin and metalloprotease 10 (ADAM10) were significantly decreased, along with down-regulation of adenylate cyclase 3 (AC3) and enhanced production of thromboxane A2 (TXA2). In vitro studies in human brain microvascular endothelial cells (BMECs) revealed that knockdown of AC3 significantly suppressed ADAM10 protein levels, and that activation of TXA2 receptor decreased APP expression. Furthermore, levels of soluble APPα (sAPPα, a product of α-processing of APP) were significantly reduced in hippocampus of T1D mice. In contrast, amyloidogenic processing of APP was not affected by T1D in both cerebral microvessels and hippocampus. Most notably, studies in endothelial specific APP knockout mice established that genetic inactivation of APP in endothelium was sufficient to significantly reduce sAPPα levels in the hippocampus. In aggregate, our findings suggest that T1D impairs non-amyloidogenic processing of APP in cerebral microvessels. This may exert detrimental effect on local concentration of neuroprotective molecule, sAPPα, in the hippocampus.

Epigenetic Modulation of STAT3 by Histone Deacetylase 6 (HDAC6) Regulates IL-10 Gene Expression and Immune Tolerance Mediated by Antigen-Presenting Cells (APCs)

Blood ◽  
2011 ◽  
Vol 118 (21) ◽  
pp. 519-519 ◽  
Author(s):  
Fengdong Cheng ◽  
Zi Wang ◽  
Hongwei Wang ◽  
Karrune V. Woan ◽  
Eva Sahakian ◽  
...  
Keyword(s):  
Gene Expression ◽  
T Cells ◽  
Cd4 T Cells ◽  
Transcriptional Activity ◽  
Gene Promoter ◽  
B Cell Lymphoma ◽  
Gene Promoters ◽  
Enhanced Production ◽  
Stat3 Phosphorylation

Abstract Abstract 519 We have previously shown that the pan-HDAC inhibitors LAQ824 and LBH589 inhibit IL-10 production in APCs, rendering these cells more inflammatory and capable of effectively priming naïve antigen-specific CD4+ T-cells and restoring the responsiveness of tolerant T-cells1. These findings led us to explore which HDAC(s) might be involved in the regulation of IL-10 gene transcription and be the putative target(s) of HDI-mediated IL-10 inhibition. To answer these questions we subjected the macrophage cell line RAW264.7 to shRNA screening using specific shRNAs to knockdown each known HDAC. We found that among all the HDACs, knocking down HDAC6 (HDAC6KD) was associated with a significant decrease in IL-10 mRNA and protein in response to LPS stimulation. Furthermore, HDAC6KD clones display an enhanced expression of the co-stimulatory molecule B7.2. Functionally, HDAC6KD cells were better activators of anti-HA (hemagglutinin-influenza) transgenic CD4+ T cells, leading to significantly enhanced production of IL-2 and IFN-g in response to cognate antigen. More importantly, anti-HA CD4+ anergic T cells isolated from animals bearing HA-expressing A20 B-cell lymphoma regained their ability to produce IL-2 and IFN-g when cultured in vitro with HDAC6KD cells. These results have been confirmed in APCs isolated from HDAC6 knock-out mice and in wild type APCs treated in vitro with isotype-selective HDAC6 inhibitors. Given that HDACs do not bind to DNA and they need to interact with transcription factors to regulate gene expression, we investigate next which transcription factor(s) HDAC6 might be associated with, to regulate IL-10 transcriptional activity. One likely candidate was Stat3, a well-known transcriptional activator of IL-10 gene expression that we have previously shown to play a central role in tolerance induction by APCs2. By co-immunoprecipitation studies we found that HDAC6 indeed interacts physically with Stat3. Of note, knocking down HDAC6 in APCs resulted in absence of Stat3 phosphorylation and decreased recruitment of Stat3 to the IL-10 gene promoter which might explain the inability of HDAC6KD cells to produce IL-10. The additional findings that IL-10 production by HDAC6KD cells was restored when these cells were transfected with a constitutively active mutant version of Stat3 (Stat3c) provides additional support for the important role of HDAC6 upon Stat3 activation. Further confirmation for a concerted regulatory mechanism involving HDAC6 and Stat3 in IL-10 gene regulation was provided by studies using CPA-7, a specific Stat3 inhibitor that disrupts Stat3 recruitment and binding to gene promoters. As expected, a complete abrogation of Stat3 recruitment to the IL-10 gene promoter was observed in CPA-7 treated APCs. Interestingly, such an effect was accompanied by a parallel decrease in HDAC6 recruitment to the IL-10 promoter and inhibition of IL-10 gene transcriptional activity. Taken together, we have shown for the first time that HDAC6 interacts physically with Stat3 and is required for its phosphorylation. Since Stat3 phosphorylation is absolutely necessary for activation of Stat3 target genes, HDAC6 inhibition is an enticing molecular approach to disrupt the Stat3/IL-10 axis and overcome tolerogenic mechanisms in APCs. Disclosures: No relevant conflicts of interest to declare.

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