Changes of glycosylation of cerebrospinal fluid proteins such as alpha2-macroglobulin, and prostaglandin D synthase were studied by lectin blotting, using concanavalinA, in multiple sclerosis (n = 42) and neuropathies (n = 20) in comparison to neurological controls (n = 22). The concanavalinA-reactivity of alpha2-macroglobulin, which was increased in the neuropathies but not in multiple sclerosis compared to controls, correlated with the total concanavalinA-reactivity in controls and neuropathies but not in multiple sclerosis, indicating that the protein could be abnormally glycosylated in the latter disease. Although the concentration and the concanavalinA-reactivity of prostaglandin D synthase were not significantly different in the three groups, the two parameters correlated only in neuropathies but not in controls or multiple sclerosis, probably due to the high heterogeneity of the protein. These changes deserve to be studied in further detail in view of their potential clinical applications.

Changes in Concanavalin A-Reactive Proteins in Neurological Disorders / Saso, Luciano; Valentini, G; Leone, Mg; Grippa, E; Guglielmi, Renzo; Paris, Luciana; Cantore, Giampaolo; Silvestrini, Bruno. - In: JOURNAL OF CLINICAL LABORATORY ANALYSIS. - ISSN 0887-8013. - 13(1999), pp. 158-165. [10.1002/(SICI)1098-2825(1999)13:4<158::AID-JCLA4>3.0.CO;2-0]

Changes in Concanavalin A-Reactive Proteins in Neurological Disorders

SASO, Luciano;GUGLIELMI, Renzo;PARIS, Luciana;CANTORE, Giampaolo;SILVESTRINI, Bruno
1999

Abstract

Changes of glycosylation of cerebrospinal fluid proteins such as alpha2-macroglobulin, and prostaglandin D synthase were studied by lectin blotting, using concanavalinA, in multiple sclerosis (n = 42) and neuropathies (n = 20) in comparison to neurological controls (n = 22). The concanavalinA-reactivity of alpha2-macroglobulin, which was increased in the neuropathies but not in multiple sclerosis compared to controls, correlated with the total concanavalinA-reactivity in controls and neuropathies but not in multiple sclerosis, indicating that the protein could be abnormally glycosylated in the latter disease. Although the concentration and the concanavalinA-reactivity of prostaglandin D synthase were not significantly different in the three groups, the two parameters correlated only in neuropathies but not in controls or multiple sclerosis, probably due to the high heterogeneity of the protein. These changes deserve to be studied in further detail in view of their potential clinical applications.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11573/245468
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