Publications by authors named "Eivind Larssen"

Objectives: Fatigue is a frequent and often disabling phenomenon that occurs in patients with chronic inflammatory and immunological diseases, and the underlying biological mechanisms are largely unknown. Because fatigue is generated in the brain, we aimed to investigate cerebrospinal fluid and search for molecules that participate in the pathophysiology of fatigue processes.

Methods: A label-free shotgun proteomics approach was applied to analyze the cerebrospinal fluid proteome of 20 patients with primary Sjögren's syndrome.

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Polycyclic aromatic hydrocarbons (PAHs) are well known contaminants, ubiquitously present in the habitat and spawning areas for Atlantic cod (Gadus morhua). The Atlantic cod is a key species and a globally important food source, thus continuous monitoring of PAHs is considered highly valuable to ensure ecosystem sustainability and human food safety. PAH adducts to plasma proteins are applied as sensitive biomarkers of PAH exposure in humans and other species, thus the presence of PAH protein adducts in Atlantic cod plasma was investigated to identify PAH protein adduct biomarker candidates of exposure to PAHs.

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For the environmental monitoring of coral, mucus appears to be an appropriate biological matrix due to its array of functions in coral biology and the non-intrusive manner in which it can be collected. The aim of the present study was to evaluate the feasibility of using mucus of the stony coral Lophelia pertusa (L. pertusa) as an analytical matrix for discovery of biomarkers used for environmental monitoring.

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PAH metabolites present in bile are well-known biological markers of exposure in fish, and their investigation is recommended by the ICES (International Council for the Exploration of the Sea) and the OSPAR convention (Convention for the Protection of the Marine Environment of the North-East Atlantic) for monitoring purposes. Development of analytical strategies for fish bile is encouraged by the need for more sensitive and informative markers (e.g.

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The cerebrospinal fluid (CSF) proteome is of great interest for investigation of diseases and conditions involving the CNS. However, the presence of high-abundance proteins (HAPs) can interfere with the detection of low-abundance proteins, potentially hindering the discovery of new biomarkers. Therefore, an assessment of the CSF subproteome composition requires depletion strategies.

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Understanding the complex biology of the brain requires analyzing its structural and functional complexity at the protein level. The large-scale analysis of the brain proteome, coupled with characterization of central brain proteins, provides insight into fundamental brain processes and processes linked to neurodegenerative diseases. Here we provide a map of the zebrafish brain proteome by using two-dimensional gel electrophoresis (2DE), followed by the identification of 95 brain proteins using mass spectrometry (LC-ESI MS/MS).

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Recent research has shown that fish residual materials contain a range of components with interesting biological activity. Therefore, there is a great potential in the marine bioprocess industry to utilize these by-products as starting material for generating more valuable products. The aim of the present study was to search for bioactive peptides (in particular small natural bioactive peptides with molecular weight lower than 10 kDa) in Atlantic herring (Clupea harengus L.

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Because Atlantic cod (Gadus morhua) has high economic value and its protein-rich muscle tissue is a food source, an increased understanding of the effects and consequences of environmental, nutritional, biological, and industrial factors on meat quality is necessary. To gain insight into cod muscle tissue protein composition, a large-scale proteomics approach has been used. One-dimensional polyacrylamide gel electrophoresis, nanoflow liquid chromatography peptide separation, and linear trap quadrupole mass spectrometry were used to identify 4804 peptides, which retrieved 9113 cod expressed sequence tags (ESTs), which in turn were mapped to 446 unique proteins.

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Exposure to natural and anthropogenic compounds can potentially alter the proteome in body fluids and tissues of living organisms, and by applying proteomics it is possible to discover, identify and understand such alterations. This study show results from a proteomic approach where one- or multidimensional separation (MudPIT) combined with high-accuracy tandem mass spectrometry (i.e.

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