Food Nanotechnologies: Purchasing a Double Edge Sword

Rapid development of nanotechnology has revolutionsed various areas of conventional food science and food industry. The novel properties of nanoparticles (NPs) have led to increasing application of nanotechnology in food industry. Nanofood market have a variety of products like the creamy ice-cream, drinks with no fat, enhanced flavour with nutrients and better textured, coloured and fresh looking food. Continuous monitoring for food spoilage or contamination is possible too. Nanotechnology has transformed the food industries which claim health benefits along with better taste. With the increasing use of NPs especially in food products, where humans are in close contact of the engineered nanomaterials (NMs), it is important to ensure safety before use. Bio-nano interactions often result in novel reaction and formation of products leading to toxicity. NPs mediated toxicity mainly includes inflammation, oxidative damage and genotoxicity. Prolong use of these particles can cause detrimental effects on health. Presently, due to lack of appropriate guidelines and regulations for food nanotechnology there are uncertainties regarding risk identification. Hence, it is essential to evaluate the consequences of this technology in terms of general public and occupational health risks associated with the manufacture, use and disposal of NMs, before instigating the same in day to day use

Protein Profile of Human Lung Epithelial Cells (A549) Revealing Deviation in Cytoskeleton Proteins in Response to Zinc Oxide Nanoparticles Exposure

Zinc oxide nanoparticles (ZnO NPs) are widely used in biomedicine and scientific research because of their high dissolution property and bioavailability. On the contrary, this property also increases the intracellular reactivity, accessibility and cytotoxicity. These nano-bio interactions could induce undesirable changes in the proteome of the interacting cells, especially in the lung cells as these are the primary contact site. However, the potential effects of ZnO NPs exposure on proteome remain unclear. Proteomics data will substantiate the detailed mechanism of cellular interactions and modulatory effects of ZnO NPs on cells. Quantitative proteomic profiling was done using MALDI-TOF/TOF and MS/MS to identify differential protein expression on exposure to NPs among non exposed and exposed cells. Twenty-two proteins, with approximately 1.5 fold differential expression in cells exposed to ZnO NPs as compared to control cells were identified. Differentially expressed proteins were further classified using PANTHER software on the basis of functional gene ontology term: molecular function, biological process and cellular component. ToppGene suite was used to study protein-protein interaction and network was enriched with STRING. This study is a systematic analysis of protein modulation of the A549 cells exposed to ZnO NPs indicating alterations in the cytoskeleton

Advances in Electromagnetic Therapy for Wound Healing

Understanding the molecular basis of wound healing and tissue regeneration continues to remain as one of the major challenges in modern medicine. There is absolute necessity to unveil the rather elusive mechanism with a special emphasis on the approaches to accelerate wound healing. Low frequency low intensity Pulsed electromagnetic therapy is evidenced to have a significant impact on wound repair and regeneration. It provides a non-invasive reparative technique to treat an injury. In vitro studies reported a significant effect of electromagnetic field on neovascularisation and angiogenesis. There are also many pieces of evidence which support its efficiency in reducing the duration of wound healing and improving the tensile strength of scars. Here, we compared the traditional stigma associated with pulsed electromagnetic fields and weighed them with its potential therapeutic effect on wound healing. Furthermore, we emphasized the need for more focused research to determine the therapeutic strategies and optimised parameters of pulsed electromagnetic field that can assure efficient wound healing and regeneration.

Hypobaric hypoxia induced renal damage is mediated by altering redox pathway

<div><p>Systemic hypobaric hypoxia is reported to cause renal damage; nevertheless the exact pathophysiological mechanisms are not completely understood. Therefore, the present study aims to explore renal pathophysiology by using proteomics approach under hypobaric hypoxia. Six to eight week old male Sprague Dawley rats were exposed to hypobaric hypoxia equivalent to altitude of 7628 metres (pO₂-282mmhg) at 28°C and 55% humidity in decompression chamber for different time intervals; 1, 3, and7 days. Various physiological, proteomic and bioinformatic studies were carried out to examine the effect of chronic hypobaric hypoxia on kidney. Our data demonstrated mild to moderate degenerative tubular changes, altered renal function, injury biomarkers and systolic blood pressure with increase in duration of hypobaric hypoxia exposure. Renal proteomic analysis showed 38 differential expressed spots, out of which 25 spots were down regulated and 13 were up regulated in 7 dayhypobarichypoxic exposure group of rats as compared to normoxia control. Identified proteins were involved in specific molecular changes pertinent to endogenous redox pathways, cellular integrity and energy metabolism. The study provides an empirical evidence of renal homeostasis under hypobaric hypoxia by investigating both physiological and proteomics changes. The identification of explicit key proteins provides a valuable clue about redox signalling mediated renal damage under hypobaric hypoxia.</p></div

Hypobaric hypoxia induced renal damage is mediated by altering redox pathway - Fig 7

<p><b>A. Heat map showing differently expressed spots obtained after 2DE</b>. Spots that showed up regulation in hypobaric hypoxia condition shown in orange. While spots that showed down regulation shown in blue. Fig 7 (B-F). Magnified comparison maps of spot 31316, 30660 31162, 30340 and 30428 in the 2DE patterns of control and 7 day hypoxia. Spot 31316, 30660 and 30428 had decreased expression in the 7 day hypobaric hypoxia exposure group while 31162 and 30340 had increased expression in 7 day hypoxia group.</p

Immunohistochemical analysis of tubulointerstitial injury and other cellular changes under hypobaric hypoxia.

<p>(A) Tubular apoptosis by tunnel method. (B) Renal injury by Kim-1. (C) Hypoxia response by HIF-1alpha. (D-E) Fibrosis: Collagen-1 and Fibronectin. (F) Macrophage infiltration CD14. Data represented here is Mean ± S. E. M. Values are significant if <i>P</i><. 05. * stands for level of significance when <i>P</i><0.05, **when <i>P</i><0.05, *** when <i>P</i><0.05 vs. control. Scale bar refers to 100μm at 400x and 200μm at 200x.</p

Effect of hypobaric hypoxia on inflammatory cell adhesion molecules.

<p>(A)ICAM -1 (in kidney). (B) VCAM-1 (in kidney). Data represented here is Mean ± S. E. M. Values are significant if <i>P</i><. 05. * stands for level of significance when <i>P</i><0.05, **when <i>P</i><0.05, *** when <i>P</i><0.05 vs. Control.</p

List of differently expressed spots during hypobaric hypoxia exposure, identified by MALDI-TOF/TOF.

<p>List of differently expressed spots during hypobaric hypoxia exposure, identified by MALDI-TOF/TOF.</p

List of differently expressed spots with proteomics spot ID and their respective fold changes.

<p>List of differently expressed spots with proteomics spot ID and their respective fold changes.</p

List of pathways obtained by KEGG pathway enrichment analysis of some of these identified proteins.

<p>List of pathways obtained by KEGG pathway enrichment analysis of some of these identified proteins.</p