Refrigerated warehouses as intelligent hubs to integrate renewable energy in industrial food refrigeration and to enhance power grid sustainability

Background Independence from fossil fuels, energy diversification, decarbonisation and energy efficiency are key prerequisites to make a national, regional or continental economy competitive in the global marketplace. As Europe is about to generate 20% of its energy demand from Renewable Energy Sources (RES) by 2020, adequate RES integration and renewable energy storage throughout the entire food cold chain must properly be addressed. Scope and approach Refrigerated warehouses for chilled and frozen foods are large energy consumers and account for a significant portion of the global energy demand. Nevertheless, the opportunity for RES integration in the energy supply of large food storage facilities is often neglected. In situ power generation using RES permits capture of a large portion of virtually free energy, thereby reducing dramatically the running costs and carbon footprint, while enhancing the economic competitiveness. In that context, there exist promising engineering solutions to exploit various renewables in the food preservation sector, in combination with the emerging sustainability-enhancing technology of Cryogenic Energy Storage (CES). Key findings and conclusions Substantial research endeavours are driven by the noble objective to turn the Europe's Energy Union into the world's number one in renewable energies. Integrating RES, in synchrony with CES development and proper control, is capable of both strengthening the food refrigeration sector and improving dramatically the power grid balance and energy system sustainability. Hence, this article aims to familiarise stakeholders of the European and global food preservation industry with state-of-the-art knowledge, know-how, opportunities and professional achievements in the concerned field

A Case of Eosinophilic Pneumonia in a Tobacco Harvester

Background: Eosinophilic pneumonia comprises a group of lung diseases in which eosinophils appear in increased numbers in the lungs. The distinct etiology of eosinophilic pneumonia is unknown, although the previous case series have indicated a relationship between acute eosinophilic pneumonia and the exposure to exogenous substances including the constituents of cigarettes. Case Summary: A 60-year-old nonsmoking female, who had started to harvest and sort tobacco leaves two months before presentation, was admitted because of persistent coughing, breathlessness, and general malaise. Her laboratory findings revealed eosinophilia. Chest computed tomography showed nonsegmental airspace consolidations bilaterally. A bronchoalveolar lavage fluid analysis also revealed that the numbers of total cells and eosinophils had increased. Although the urine level of cotinine was within the normal range, positive findings were found in the skin scratch-patch tests using tobacco leaf and its extracts, and a biopsy specimen obtained from the positive site demonstrated infiltration of eosinophils in the dermis. The patient was successfully treated with corticosteroids. Discussion: Green tobacco sickness, a type of nicotine poisoning caused by the dermal absorption of nicotine, is a well known occupational illness of tobacco harvesters. Although it is unclear whether the present case could be identified as a subtype of green tobacco sickness, this is the first report of eosinophilic pneumonia occurred in a tobacco harvester which was possibly induced by tobacco leaf exposure

Protective Effects of Clenbuterol against Dexamethasone-Induced Masseter Muscle Atrophy and Myosin Heavy Chain Transition.

Glucocorticoid has a direct catabolic effect on skeletal muscle, leading to muscle atrophy, but no effective pharmacotherapy is available. We reported that clenbuterol (CB) induced masseter muscle hypertrophy and slow-to-fast myosin heavy chain (MHC) isoform transition through direct muscle β2-adrenergic receptor stimulation. Thus, we hypothesized that CB would antagonize glucocorticoid (dexamethasone; DEX)-induced muscle atrophy and fast-to-slow MHC isoform transition.We examined the effect of CB on DEX-induced masseter muscle atrophy by measuring masseter muscle weight, fiber diameter, cross-sectional area, and myosin heavy chain (MHC) composition. To elucidate the mechanisms involved, we used immunoblotting to study the effects of CB on muscle hypertrophic signaling (insulin growth factor 1 (IGF1) expression, Akt/mammalian target of rapamycin (mTOR) pathway, and calcineurin pathway) and atrophic signaling (Akt/Forkhead box-O (FOXO) pathway and myostatin expression) in masseter muscle of rats treated with DEX and/or CB.Masseter muscle weight in the DEX-treated group was significantly lower than that in the Control group, as expected, but co-treatment with CB suppressed the DEX-induced masseter muscle atrophy, concomitantly with inhibition of fast-to-slow MHC isoforms transition. Activation of the Akt/mTOR pathway in masseter muscle of the DEX-treated group was significantly inhibited compared to that of the Control group, and CB suppressed this inhibition. DEX also suppressed expression of IGF1 (positive regulator of muscle growth), and CB attenuated this inhibition. Myostatin protein expression was unchanged. CB had no effect on activation of the Akt/FOXO pathway. These results indicate that CB antagonizes DEX-induced muscle atrophy and fast-to-slow MHC isoform transition via modulation of Akt/mTOR activity and IGF1 expression. CB might be a useful pharmacological agent for treatment of glucocorticoid-induced muscle atrophy

Changes in expression of β₂-AR and glucocorticoid receptor after treatment with CB and/or DEX for 2 weeks.

<p><b>(A)</b> Expression of β_<b>2</b>-AR protein in masseter muscle of the CB, DEX, and CB+DEX groups was smaller than that in the Control (*<i>P</i> < 0.05, **<i>P</i> < 0.01 vs. Control), but the magnitude of the attenuation was similar among the three groups. <b>(B)</b> There was no change in expression of glucocorticoid receptor protein in the CB, DEX, and CB+DEX groups (<i>P</i> = NS vs. Control in each case). <b>(C)</b> Representative immunoblotting results for β_<b>2</b>-AR and glucocorticoid receptor. The amount of expression in the Control was taken as 100% in each determination. GAPDH; glyceraldehyde 3-phosphate dehydrogenase</p

Changes of body weight, daily consumption of food and water, and daily intake of CB and energy.

<p>(<b>A)</b> Body weight (BW: g) of CB was similar to the Control (<i>P</i> = NS vs. Control). On the other hand, BW of both the DEX and CB+DEX groups was significantly smaller than that in the Control (**<i>P</i> < 0.01 vs. Control in each case). <b>(B-C)</b> No significant difference in daily consumption of food <b>(B)</b> or water <b>(C)</b> was observed among the CB, DEX, CB+DEX, and the Control groups (<i>P</i> = NS vs. Control in each case).<b>(D-E)</b> No significant difference was observed in daily intake of CB per baseline BW between the CB and CB+DEX groups <b>(D)</b> or in energy intake among the CB, DEX, CB+DEX, and the Control groups <b>(E)</b> (<i>P</i> = NS vs. Control in each case). The values of BW, consumption of food, consumption of water, CB intake, and energy intake in the Control group were taken as 100% in each determination.</p

Effects of CB and DEX on phosphorylation of FOXO1, FOXO3a, and S6K1.

<p><b>(A)</b> Phosphorylation of FOXO1 at serine 259 in the CB, DEX, and CB+DEX groups was similarly and significantly greater than that in the Control (**<i>P</i> < 0.01 vs. Control in each case). <b>(B)</b> Phosphorylation of FOXO3a at serine 253 in CB, DEX, and CB+DEX was similarly and significantly greater than that in the Control (**<i>P</i> < 0.01 vs. Control in each case). <b>(C)</b> Phosphorylation of S6K1 on threonine 389 in the CB group was significantly greater than that in the Control (*<i>P</i> < 0.05), while that in the DEX group was significantly lower than that in the Control (*<i>P</i> < 0.05). Importantly, DEX-induced dephosphorylation at this site was significantly suppressed by co-treatment with CB (CB+DEX vs. DEX (^#<i>P</i> < 0.05)). <b>(D)</b> Representative immunoblotting results for phosphorylated and total FOXO1,FOXO3a, and S6K1. The amount of phosphorylation in the Control was taken as 100% in each determination. p-FOXO1, phosphorylated FOXO1 at serine 259; t-FOXO1, total FOXO1; p-FOXO3a, phosphorylated FOXO3a at serine 253; t-FOXO3a, total FOXO3a, p-S6K1, phosphorylated S6K1 at threonine 389; total S6K1, t-S6K1.</p

Effects of CB and DEX on IGF1 expression, myostatin expression, and Akt phosphorylation in masseter muscle after treatment with CB and/or DEX for 2 weeks.

<p><b>(A)</b> IGF1 expression in masseter muscle of the CB group was greater than that of the Control (**<i>P</i> < 0.01). Conversely, IGF1 expression of the DEX group was smaller than that of the Control (*<i>P</i> < 0.05). The DEX-mediated inhibition of IGF1 was suppressed by co-treatment with CB (CB+DEX vs. DEX, ^#<i>P</i> < 0.05) <b>(B)</b> Expression of myostatin protein was similar in all four groups (<i>P</i> = NS vs. Control in each case). <b>(C)</b> Phosphorylation of Akt on serine 473 in the CB, DEX, and CB+DEX groups was significantly greater than that in the Control (*<i>P</i> < 0.05, **<i>P</i> < 0.01 vs. Control). <b>(D)</b> Representative immunoblotting results for IGF1, myostatin, and phosphorylated Akt, and total Akt. The amount of expression or phosphorylation level in the Control was taken as 100% in each determination. p-Akt, phosphorylated Akt at serine 473; t-Akt, total Akt, GAPDH; glyceraldehyde 3- phosphate dehydrogenase</p

Muscle mass (mg) of rats in Control, CB, DEX or CB+DEX group.

<p>* p < 0.05,</p><p>** p < 0.01, vs. Control, n = 3.</p><p>Muscle mass (mg) of rats in Control, CB, DEX or CB+DEX group.</p