Gruppo di Studio per la Proteomica e la Struttura delle Proteine

Gressoney-La-Trinité, Italy

Gruppo di Studio per la Proteomica e la Struttura delle Proteine

Gressoney-La-Trinité, Italy

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Gianazza E.,Gruppo di Studio per la Proteomica e la Struttura delle Proteine | Gianazza E.,University of Milan | Vegeto E.,University of Milan | Vegeto E.,Centro Of Eccellenza Per Le Malattie Neurodegenerative | And 5 more authors.
Proteomics | Year: 2012

More than a decade ago our groups pioneered the analysis of serum proteins of laboratory animals with up-to-date proteomic techniques. We were, and still are, convinced that conforming animal procedures to the minimally invasive approaches typical of clinical biochemistry focuses attention on the actual conditions under which any finding arrived at on animal models of disease may eventually be applied to human patients for screening/diagnosis. We are also convinced that, besides the proteins present in trace level as a result of tissue leakage during disorders affecting specific peripheral organs, changes in the concentration of some of the major serum proteins as part of an acute-phase response may be taken as biological end-points during a number of experimental procedures. When reviewing literature data about proteomic investigations on plasma or serum of mice, we realized that not much work has been done in the direction we favor. In addition, we noticed that sometimes information about serum proteome has been coarsely treated and in a few cases even misunderstood/misused. In the following, we present current findings on serum/plasma proteome of the laboratory mouse not only under control conditions and during an experimentally induced acute-phase reaction, but also in a number of models of disease, mainly related to cancer and to metabolic disorders. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.


Eberini I.,Gruppo di Studio per la Proteomica e la Struttura delle Proteine | Eberini I.,University of Milan | Wait R.,Imperial College London | Calabresi L.,Centro Universitario Per Le Dislipidemie Presso Lospedale Of Niguarda | And 6 more authors.
Journal of Proteomics | Year: 2013

We have arranged in this review the main evidence about proteome alterations in different cell and body fluid compartments along the progression of atherosclerosis. With time the description of the molecular phenomena is becoming more and more detailed yet the complex interrelationships among different factors are still elusive and previously neglected aspects (such as size for lipoprotein particles) emerge as not less relevant than the absolute abundance of individual proteins. Physiological limits to the kinetics of protein distribution through the biological fluids seem to hinder the early diagnosis of acute conditions through plasma analysis but suggest urine analysis as a workable alternative for the assessment of chronic conditions.The survey of literature data is complemented with a few unpublished results from our laboratories, featuring 2DE maps of the proteins extracted from human thrombi. © 2013 Published by Elsevier B.V.


PubMed | Gruppo di Studio per la Proteomica e la Struttura delle Proteine
Type: | Journal: Journal of proteomics | Year: 2013

We have arranged in this review the main evidence about proteome alterations in different cell and body fluid compartments along the progression of atherosclerosis. With time the description of the molecular phenomena is becoming more and more detailed yet the complex interrelationships among different factors are still elusive and previously neglected aspects (such as size for lipoprotein particles) emerge as not less relevant than the absolute abundance of individual proteins. Physiological limits to the kinetics of protein distribution through the biological fluids seem to hinder the early diagnosis of acute conditions through plasma analysis but suggest urine analysis as a workable alternative for the assessment of chronic conditions. The survey of literature data is complemented with a few unpublished results from our laboratories, featuring 2DE maps of the proteins extracted from human thrombi.

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