An Experimental Brackish Aquaponic System Using Juvenile Gilthead Sea Bream (Sparus aurata) and Rock Samphire (Crithmum maritimum)

Brackish aquaponics using Mediterranean fish and plants provides an alternative opportunity for a combined production of high-quality food products with high commercial and nutritional value. This is the first study that investigates the effect of two different salinities (8 and 20 ppt) on growth and survival of Sparus aurata and Crithmum maritimum along with the cellular stress pathways using the activation of heat shock proteins (HSPs) and mitogen-activated protein kinase (MAPK) protein family members and the water bacterial abundance. In total, 156 fish were used (average initial weight of 2.55 g, length of 5.57 cm) and 36 plants (average initial height of 8.23 cm) in floating racks above the 135 L fish tanks. Survival rate for both organisms was 100%. C. crithmum grew better at 8 ppt (t-test, p < 0.05). The growth rate of S. aurata was similar for both treatments (p > 0.05). HSPs and MAPK were differentially expressed, showing tissue-specific responses. The average bacterial abundance at the end of the experiment was higher (p < 0.05) in the 20 ppt (18.6 ± 0.91 cells × 105/mL) compared to the 8 ppt (6.8 ± 1.9 cells × 105/mL). The results suggest that the combined culture of euryhaline fish and halophytes provides good quality products in brackish aquaponics systems.

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The influence of organic versus conventional feeding on the growth and survival of gilthead sea bream Sparus aurata L. juveniles

Veterinarski arhiv ◽

10.24099/vet.arhiv.0319 ◽

2019 ◽

Vol 89 (5) ◽

pp. 683-695

Author(s):

María D. Ayala ◽

◽

Antonio García-Saorín ◽

Helena Martínez-Torres ◽

Alicia García-Alcázar ◽

...

Keyword(s):

Sparus Aurata ◽

Gilthead Sea Bream ◽

Sea Bream ◽

Growth And Survival

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Association and Regulation of Heat Shock Transcription Factor 4b with both Extracellular Signal-Regulated Kinase Mitogen-Activated Protein Kinase and Dual-Specificity Tyrosine Phosphatase DUSP26

Molecular and Cellular Biology ◽

10.1128/mcb.26.8.3282-3294.2006 ◽

2006 ◽

Vol 26 (8) ◽

pp. 3282-3294 ◽

Cited By ~ 44

Author(s):

Yanzhong Hu ◽

Nahid F. Mivechi

Keyword(s):

Transcription Factor ◽

Heat Shock ◽

Map Kinase ◽

Tyrosine Phosphatase ◽

Mitogen Activated Protein Kinase ◽

Lens Fiber Cell ◽

Dual Specificity ◽

Extracellular Signal ◽

Mitogen Activated Protein ◽

Shock Proteins

ABSTRACT The heat shock transcription factors (Hsfs) activate the stress-inducible expression of heat shock proteins (Hsps) and other molecular chaperones in response to stress and, therefore, play an essential role in protein disaggregation and protein folding. In humans, missense mutation in the hsf4 gene causes cataract, and mice bearing a targeted disruption of the hsf4 gene exhibit defects in lens fiber cell differentiation and early cataract formation. Here, we show that Hsf4b is a direct target of the mitogen-activated protein (MAP) kinase extracellular signal-related kinase (ERK) and that phosphorylation of Hsf4b by ERK leads to increased ability of Hsf4b to bind DNA. Surprisingly, Hsf4b also interacts with an ERK-specific dual-specificity tyrosine phosphatase named DUSP26 identified from a yeast two-hybrid screen. While activated ERK phosphorylates Hsf4b, DUSP26 controls the activity of ERK, leading to phosphorylation/dephosphorylation of Hsf4b, altering its ability to bind DNA. Therefore, DUSP26 interaction with Hsf4b places this transcription factor within a regulatory circuit in the MAP kinase signaling pathway.

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Optimization of Artemia Metanauplii on Growth and Survival of Gilthead Sea Bream Larvae Sparus aurata

Journal of the World Aquaculture Society ◽

10.1111/j.1749-7345.2004.tb01063.x ◽

2004 ◽

Vol 35 (1) ◽

pp. 87-93 ◽

Cited By ~ 3

Author(s):

Apostolos Mihelakakis ◽

Christos Tsolkas ◽

Takao Yoshimatsu

Keyword(s):

Sparus Aurata ◽

Gilthead Sea Bream ◽

Sea Bream ◽

Growth And Survival

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Combination of the mTOR inhibitor rapamycin and CC-5013 has synergistic activity in multiple myeloma

Blood ◽

10.1182/blood-2004-06-2281 ◽

2004 ◽

Vol 104 (13) ◽

pp. 4188-4193 ◽

Cited By ~ 137

Author(s):

Noopur Raje ◽

Shaji Kumar ◽

Teru Hideshima ◽

Kenji Ishitsuka ◽

Dharminder Chauhan ◽

...

Keyword(s):

Multiple Myeloma ◽

Mtor Inhibitor ◽

Mtor Inhibitors ◽

Mitogen Activated Protein Kinase ◽

Synergistic Activity ◽

Growth And Survival ◽

Mitogen Activated Protein ◽

Induced Apoptosis

Abstract Previous studies have demonstrated the in vitro and in vivo activity of CC-5013 (Revlimid), an immunomodulatory analog (IMiD) of thalidomide, in multiple myeloma (MM). In the present study, we have examined the anti-MM activity of rapamycin (Rapamune), a specific mTOR inhibitor, combined with CC-5013. Based on the Chou-Talalay method, combination indices of less than 1 were obtained for all dose ranges of CC-5013 when combined with rapamycin, suggesting strong synergism. Importantly, this combination was able to overcome drug resistance when tested against MM cell lines resistant to conventional chemotherapy. Moreover, the combination, but not rapamycin alone, was able to overcome the growth advantage conferred on MM cells by interleukin-6 (IL-6), insulin-like growth factor-1 (IGF-1), or adherence to bone marrow stromal cells (BMSCs). Combining rapamycin and CC-5013 induced apoptosis of MM cells. Differential signaling cascades, including the mitogen-activated protein kinase (MAPK) and the phosphatidylinositol 3′-kinase/Akt kinase (PI3K/Akt) pathways, were targeted by these drugs individually and in combination, suggesting the molecular mechanism by which they interfere with MM growth and survival. These studies, therefore, provide the framework for clinical evaluation of mTOR inhibitors combined with IMiDs to improve patient outcome in MM.

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IGF-1 suppresses Bim expression in multiple myeloma via epigenetic and posttranslational mechanisms

Blood ◽

10.1182/blood-2009-07-232801 ◽

2010 ◽

Vol 115 (12) ◽

pp. 2430-2440 ◽

Cited By ~ 63

Author(s):

Elke De Bruyne ◽

Tomas J. Bos ◽

Frans Schuit ◽

Els Van Valckenborgh ◽

Eline Menu ◽

...

Keyword(s):

Multiple Myeloma ◽

Mitogen Activated Protein Kinase ◽

Down Regulation ◽

Drug Induced ◽

Growth And Survival ◽

Deacetylase Inhibitor ◽

Mitogen Activated Protein ◽

Methylation Inhibitor ◽

H3k9 Dimethylation ◽

Kinase Pathway

Abstract Insulin-like growth factor-1 (IGF-1) is an important growth and survival factor in multiple myeloma (MM). Here, we demonstrate that IGF-1 induces significant down-regulation of the proapoptotic BH3-only protein Bim in MM cells. Reduced Bim levels by RNA interference (RNAi) protected cells from drug-induced cell death. The IGF-1–mediated down-regulation of Bim was the result of (1) reduced transcription by activation of the Akt pathway and inactivation of the transcription factor FoxO3a, (2) increased proteasome-mediated degradation of the Bim extra-long protein by activation of the mitogen-activated protein kinase pathway, and (3) epigenetic regulation of both the Bim and the FoxO3a promoter. Treatment of cells with the histone deacetylase inhibitor LBH589 resulted in a clear up-regulation in the expression of Bim. Furthermore, the methylation inhibitor 5-aza-2′deoxycytidine (decitabine) significantly increased the effects of LBH589. On IGF-1 treatment, the Bim promoter region was found to be unmethylated, whereas chromatin immunoprecipitation analysis of the IGF-1–treated cells showed both a reduced histone H3 tail Lys9 (H3K9) acetylation and an increased H3K9 dimethylation, which contributed actively to its silencing. These data identify a new mechanism in the IGF-1–dependent survival of MM cells and emphasize the need for IGF-1–targeted drug therapy.

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Role of p38 mitogen-activated protein kinase pathway in estrogen-mediated cardioprotection following trauma-hemorrhage

AJP Heart and Circulatory Physiology ◽

10.1152/ajpheart.01303.2006 ◽

2007 ◽

Vol 292 (6) ◽

pp. H2982-H2987 ◽

Cited By ~ 30

Author(s):

Jun-Te Hsu ◽

Ya-Ching Hsieh ◽

Wen Hong Kan ◽

Jian Guo Chen ◽

Mashkoor A. Choudhry ◽

...

Keyword(s):

Protein Kinase ◽

Cardiac Function ◽

P38 Mapk ◽

Mitogen Activated Protein Kinase ◽

Male Rats ◽

Mitogen Activated Protein ◽

Salutary Effect ◽

The Stability ◽

Shock Proteins ◽

Sb 203580

p38 mitogen-activated protein kinase (MAPK) activates a number of heat shock proteins (HSPs), including HSP27 and αB-crystallin, in response to stress. Activation of HSP27 or αB-crystallin is known to protect organs/cells by increasing the stability of actin microfilaments. Although our previous studies showed that 17β-estradiol (E2) improves cardiovascular function after trauma-hemorrhage, whether the salutary effects of E2 under those conditions are mediated via p38 MAPK remains unknown. Male rats (275–325 g body wt) were subjected to soft tissue trauma and hemorrhage (35–40 mmHg mean blood pressure for ∼90 min) followed by fluid resuscitation. At the onset of resuscitation, rats were injected intravenously with vehicle, E2 (1 mg/kg body wt), E2 + the p38 MAPK inhibitor SB-203580 (2 mg/kg body wt), or SB-203580 alone, and various parameters were measured 2 h thereafter. Cardiac functions that were depressed after trauma-hemorrhage were returned to normal levels by E2 administration, and phosphorylation of cardiac p38 MAPK, HSP27, and αB-crystallin was increased. The E2-mediated improvement of cardiac function and increase in p38 MAPK, HSP27, and αB-crystallin phosphorylation were abolished with coadministration of SB-203580. These results suggest that the salutary effect of E2 on cardiac function after trauma-hemorrhage is in part mediated via upregulation of p38 MAPK and subsequent phosphorylation of HSP27 and αB-crystallin.

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Combination of the mTOR Inhibitor Rapamycin and Revlimid™ (CC-5013) Has Synergistic Activity in Multiple Myeloma (MM).

Blood ◽

10.1182/blood.v104.11.1492.1492 ◽

2004 ◽

Vol 104 (11) ◽

pp. 1492-1492 ◽

Cited By ~ 1

Author(s):

Noopur Raje ◽

Shaji Kumar ◽

Teru Hideshima ◽

Kenji Ishitsuka ◽

Dharminder Chauhan ◽

...

Keyword(s):

Mtor Inhibitor ◽

Mtor Inhibitors ◽

Mitogen Activated Protein Kinase ◽

Signaling Cascades ◽

Synergistic Activity ◽

Phosphatidylinositol 3 Kinase ◽

Growth And Survival ◽

Mitogen Activated Protein

Abstract Interleukin-6 (IL-6) and insulin-like growth factor-1 (IGF-1) mediate growth of MM cells via activation of the mitogen-activated protein kinase (MAPK), JAK2/STAT3, and phosphatidylinositol 3′-kinase/Akt kinase (PI3-K/Akt) signaling cascades. We have previously demonstrated the in vitro and in vivo activity of Revlimid™ (CC-5013), an immunomodulatory analog (IMiD) of thalidomide, in MM. In the present study, we have examined the anti-MM activity of rapamycin, a specific mTOR inhibitor, combined with Revlimid™. This combination was highly synergistic at 0.1nmol/L of rapamycin with 0.1mmol/L of Revlimid™, and remained synergistic at higher concentrations. Based on the Chou-Talalay method, combination indices of < 1 were noted for all dose ranges of Revlimid™ and rapamycin, suggesting strong synergism. Importantly, this combination was able to overcome drug resistance when tested against MM cell lines resistant to conventional (doxorubicin, melphalan, dexamethasone) chemotherapy. Moreover, the combination, but not rapamycin alone, was able to overcome the growth advantage conferred on MM cells by IL-6, IGF-1, or adherence to bone marrow stromal cells (BMSCs). Cytotoxicity triggered by a combination of rapamycin with Revlimid™ resulted in apoptosis of MM cells. Furthermore, differential signaling cascades, including the MAPK and PI3-K/Akt pathways, were targeted by these drugs individually and in combination, suggesting the molecular mechanism by which they interfere with MM growth and survival. These studies therefore provide the framework for the clinical evaluation of targeted agents like mTOR inhibitors combined with immunomodulatory agents like Revlimid™ to improve patient outcome in MM.

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