Med-index: a food product labeling system to promote adherence to the mediterranean diet encouraging producers to make healthier and more sustainable food products

Consumers are increasingly demanding transparency in food labeling as they want more and better information about what they are eating and where their food comes from. Several food indexes have been developed in the last decades to promote healthy eating with the aim of reducing certain diseases such as obesity, cancer, and diabetes. The Mediterranean diet is known to be one of the healthiest dietary patterns, and it is associated with a lower incidence of mortality from all-causes, and it is also related to a lower incidence of cardiovascular diseases, type 2 diabetes, certain types of cancer, and neurodegenerative diseases; however, a comprehensive index that quantifies the Mediteraneaness of foods is still missing. The real European challenge is to identify a uniform labeling system for the whole of Europe which promotes a healthy lifestyle. This article describes the development of the Mediterranean Index (MI), which aims to accurately measure the degree of food Mediterraneaness. The MI simultaneously integrates nutritional and sustainability characteristics of foods. The MI may provide an objective basis for the use of the “Mediterraneaness” label on food products, which can ultimately promote adherence to the Mediterranean diet encouraging producers to make healthier and more sustainable food products. Growing consumer concern toward health foods for better health can be a factor useful to promote the applicability of the precision nutrition principles by means of conscious choice.

Feature-rich covalent stains for super-resolution and cleared tissue fluorescence microscopy

Fluorescence microscopy is a workhorse tool in biomedical imaging but often poses substantial challenges to practitioners in achieving bright or uniform labeling. In addition, while antibodies are effective specific labels, their reproducibility is often inconsistent, and they are difficult to use when staining thick specimens. We report the use of conventional, commercially available fluorescent dyes for rapid and intense covalent labeling of proteins and carbohydrates in super-resolution (expansion) microscopy and cleared tissue microscopy. This approach, which we refer to as Fluorescent Labeling of Abundant Reactive Entities (FLARE), produces simple and robust stains that are modern equivalents of classic small-molecule histology stains. It efficiently reveals a wealth of key landmarks in cells and tissues under different fixation or sample processing conditions and is compatible with immunolabeling of proteins and in situ hybridization labeling of nucleic acids.

A protocol to automatically calculate homo-oligomeric protein structures through the integration of evolutionary constraints and ambiguous contacts derived from solid- or solution-state NMR

ABSTRACTProtein assemblies are involved in many important biological processes. Solid-state NMR (SSNMR) spectroscopy is a technique suitable for the structural characterization of samples with high molecular weight and thus can be applied to such assemblies. A significant bottleneck in terms of both effort and time required is the manual identification of unambiguous intermolecular contacts. This is particularly challenging for homo-oligomeric complexes, where simple uniform labeling may not be effective. We tackled this challenge by exploiting coevolution analysis to extract information on homo-oligomeric interfaces from NMR-derived ambiguous contacts. After removing the evolutionary couplings (ECs) that are already satisfied by the 3D structure of the monomer, the predicted ECs are matched with the automatically generated list of experimental contacts. This approach provides a selection of potential interface residues that is used directly in monomer-monomer docking calculations. We validated the protocol on tetrameric L-asparaginase II and dimeric Sod1.

Ultrafast immunostaining of organ-scale tissues for scalable proteomic phenotyping

ABSTRACTStudying the function and dysfunction of complex biological systems necessitates comprehensive understanding of individual cells. Advancements in three-dimensional (3D) tissue processing and imaging modalities have enabled rapid visualization and phenotyping of cells in their spatial context. However, system-wide interrogation of individual cells within large intact tissue remains challenging, low throughput, and error-prone owing to the lack of robust labeling technologies. Here we introduce a rapid, versatile, and scalable method, eFLASH, that enables complete and uniform labeling of organ-scale tissue within one day. eFLASH dynamically modulates chemical transport and reaction kinetics to establish system-wide uniform labeling conditions throughout the day-long labeling period. This unique approach enables the same protocol to be compatible with a wide range of tissue types and probes, enabling combinatorial molecular phenotyping across different organs and species. We applied eFLASH to generate quantitative maps of various cell types in mouse brains. We also demonstrated multidimensional cell profiling in a marmoset brain block. We envision that eFLASH will spur holistic phenotyping of emerging animal models and disease models to help assess their functions and dysfunctions.

Uniform Labeling of Blocks and Slides in Surgical Pathology: Guideline From the College of American Pathologists Pathology and Laboratory Quality Center and the National Society for Histotechnology

Context The labeling of paraffin blocks and microscopic glass slides in the practice of surgical pathology varies from institution to institution and introduces potential risk of preanalytic error. Currently there are no evidence-based guidelines regarding the uniform labeling of these materials. Objective To develop recommendations that will address the need for adequate patient identification and provide a consistent method of identifying slides originating from a particular block. Design The College of American Pathologists Pathology and Laboratory Quality Center and the National Society for Histotechnology convened a panel of pathologists and histotechnologists with expertise in histology laboratory quality practices to develop labeling recommendations. A systematic evidence review was conducted to address 6 main key questions. Recommendations were derived from strength of evidence, open comment feedback, and expert panel consensus. Results Twelve guideline statements were established to assist pathology laboratories in developing standardized block and slide labeling practices. These guidelines call for the use of 2 patient identifiers, 1 of which includes the accession number and case type, on all paraffin blocks and slides. Recommendations were also developed to address the order and format in which identifying elements should appear. Conclusions Uniform labeling of paraffin blocks and slides derived from patient specimens will provide an important enhancement to patient safety by assuring that all preparations derived from a patient's tissue can be uniquely and unambiguously linked to that patient. Adoption of standardized practices additionally will improve patient care by facilitating interpretation of histologic sections when they are referred in consultation to a second institution.

Determination of the Localization of Gangliosides Using Anti-ganglioside Antibodies: Comparison of Fixation Methods

Many studies have examined the localization of gangliosides using anti-ganglioside antibodies, although widely differing conclusions have been reached. We now demonstrate that the apparent localization of gangliosides can be greatly influenced by the fixation method. Using monoclonal antibody (MAb) A2B5 (which reacts with a variety of gangliosides), hippocampal neurons were labeled at the cell surface when incubated with the antibody before fixation, but when incubated after fixation the cells displayed a variety of labeling patterns, depending on the fixation method. Biochemical analysis demonstrated that some of the fixatives (particularly acetone and methanol) significantly reduced or completely depleted cellular gangliosides, implying that the immunoreactivity observed with A2B5, and with other antibodies, was not due to gangliosides. When neurons were incubated with an anti-GD1b antibody prefixation, uniform labeling of the plasma membrane was observed, but after ganglioside depletion using biochemical inhibitors of ganglioside synthesis no cell surface labeling was detected. However, even in cells depleted of gangliosides, labeling of both the cell surface and intracellular compartments was observed when the anti-GD1b antibody was applied after fixation. Moreover, after fixation, antibodies to GM4 and GD2 reacted with hippocampal neurons, although these ganglio-sides are absent from these neurons. In contrast, the JONES antibody (which reacts with 9- O-acetylated GD3) labeled neurons with a similar pattern, essentially irrespective of the fixation method. These observations demonstrate that great care must be taken in assigning gangliosides to specific cell populations or to intracellular locations solely on the basis of use of anti-ganglioside antibodies, and suggest that optimal fixation conditions must be established for each anti-ganglioside antibody.