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Evidence from many recent studies has linked uncontrolled inflammatory processes to aging and aging-related diseases. Decreased a nuclear receptor subfamily of transcription factors, peroxisome proliferator-activated receptors (PPARs) activity is closely associated with increased levels of inflammatory mediators during the aging process. The anti-inflammatory action of PPARs is substantiated by both in vitro and in vivo studies that signify the importance of PPARs as major players in the pathogenesis of many inflammatory diseases. In this review, we highlight the molecular mechanisms and roles of PPARα, γ in regulation of age-related inflammation. By understanding these current findings of PPARs, we open up the possibility of developing new therapeutic agents that modulate these nuclear receptors to control various inflammatory diseases such as atherosclerosis, vascular diseases, Alzheimer's disease, and cancer.

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Determination of the concentration of α1 - antitrypsin in the stool is a diagnostic indicator of inflammatory diseases of the small and the large intestine, especially malabsorption syndrome. α1 - antitrypsin belongs to the family of plasma proteins with antiproteinase effect. α1 - antitrypsin is synthesized in liver, in small amount in macrophage and is a protease inhibitor of serine proteases sercected from neutrophils. α1 - antitrypsin is acute phase protein. Higher α1 - antitrypsin values are in early phase of inflammation associated with raised CRP and other pozitive acute phase proteins. Fecal α1 - antitrypsin clearance is a sensitive and specific marker of protein loss. For α1 - antitrypsin determination in stool samples ELISA method can be used. ELISA is noncompetetive immunoassay used to detect presence of antibody or an antigen in a sample. The aim of this work was to compare two ELISA sets (Immundiagnostik and Ridascreen) used for determination α1 - antitrypsin in the stool. Then examine stability of α1 - antitrypsin in the stool and in extract prepared from stool in various storing conditions temperature and time. After this establish this method as routine in laboratory. 20 patient stool samples were examined to compare ELISA sets. Samples were suggested to be α1 - antitrypsin...

Majorer la tolérance de l’hôte à l’inflammation est un facteur qui pourrait diminuer l’ampleur des lésions tissulaires au cours des pathologies inflammatoires. Dans ce travail, nous rapportons que la molécule clusterine, une protéine chaperonne extracellulaire très conservée et présente dans la plupart des tissus et fluides biologiques, neutralise les effets cytotoxiques de molécules associées à l’inflammation. Le taux sérique de clusterine est diminué chez les patients atteints de certaines maladies inflammatoires, et les souris déficientes en clusterine ont une sensibilité plus importante à l’inflammation. Clusterine interagit avec certaines molécules associées à l’inflammation et forme des complexes qui sont détectés dans le sérum des patients. In vitro, clusterine inhibe la mort cellulaire induite par les molécules associées à l’inflammation. Bien que l’inflammation induise la libération rapide d’un stock préformé contenu dans les polynucléaires neutrophiles et les plaquettes, les taux de clusterine sérique sont abaissés chez l’homme et la souris en contexte inflammatoire. Démontrant la non redondance et le rôle protecteur de clusterine, l’inflammation est majorée chez la souris déficiente en clusterine.Nous concluons que clusterine augmente la tolérance de l’hôte à l’inflammation. / Increasing host tolerance to inflammation may lower the intensity of tissular injury in inflammatory diseases. We report here that clusterin, a conserved extracellular chaperone, present in most tissues and fluids, neutralizes the in vitro and in vivo cytotoxic properties of inflammation-induced molecules. Serum clusterin levels are decreased in patients with some inflammatory diseases and clusterin deficient mice have higher sensibility to inflammation.Clusterin interacts with some inflammation-associated molecules and form complexes that are detected in human serum and, consequently, prevents in vitro cell death induced by these molecules. Although inflammation triggers the rapid release of preformed clusterin stock by neutrophils and platelets, serum clusterin concentrations get down in inflammatory conditions in human and mice. Inflammation is boosted, in vivo and in vitro, using clusterin-deficient mice, showing the non-redundant and major protective roles of clusterin. We conclude that clusterin enhances host tolerance to inflammation.