title: Glycosilated nucleolin as marker for human gliomas.
abstract: Nucleolin is a multifunctional DNA and RNA binding protein involved in regulation of gene transcription, chromatin remodeling, RNA metabolism, and ribosomal RNA synthesis. Nucleolin seems to be over-expressed in highly proliferative cells and is involved in many aspect of gene expression: DNA recombination and replication, RNA transcription by RNA polymerase I and II, rRNA processing, mRNA stabilization, cytokinesis, and apoptosis. Although nucleolin is localized predominantly in the nucleolus, it has also been shown to be localized in a phosphorylated/glycolsilated form on the cell surface of different cells. Numerous articles dealing with surface nucleolin targeting for tumor therapy have been recently published. However, at present, no extensive informations are so far available for the presence of nucleolin in human gliomas. In the present work we investigated on the presence and localization of nucleolin in glioma on glioma specimens at different grade of malignancy and on primary glioma cell cultures derived by surgical resection, trying to correlate the presence of glycosilated membrane nucleolin with the malignancy grade. To this purpose an antibody produced by us against gp273 protein, demonstrated to recognized the glycosilated surface nucleolin, has been used. The results obtained demonstrate that surface nucleolin increase with the malignancy grade thus suggesting that it may constitute a histopathological marker for glioma grading and a possible tool for targeted therapy.
authors.affiliation: Department of Health Sciences, University of L'Aquila, L'Aquila, Italy.
authors.forename: R
authors.initials: R
authors.lastname: Galzio
authors.forename: F
authors.initials: F
authors.lastname: Rosati
authors.forename: E
authors.initials: E
authors.lastname: Benedetti
authors.forename: L
authors.initials: L
authors.lastname: Cristiano
authors.forename: S
authors.initials: S
authors.lastname: Aldi
authors.forename: S
authors.initials: S
authors.lastname: Mei
authors.forename: B
authors.initials: B
authors.lastname: D'Angelo
authors.forename: R
authors.initials: R
authors.lastname: Gentile
authors.forename: G
authors.initials: G
authors.lastname: Laurenti
authors.forename: M G
authors.initials: MG
authors.lastname: Cifone
authors.forename: A
authors.initials: A
authors.lastname: Giordano
authors.forename: A
authors.initials: A
authors.lastname: Cimini
mesh_terms: D000071916:AC133 Antigen; D000368:Aged; D015703:Antigens, CD / Q000378:metabolism; D001254:Astrocytoma / Q000378:metabolism* / Q000473:pathology; D014408:Biomarkers, Tumor / Q000378:metabolism*; D001932:Brain Neoplasms / Q000378:metabolism* / Q000473:pathology; D002478:Cells, Cultured; D005904:Glial Fibrillary Acidic Protein / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D008875:Middle Aged; D060787:Neoplasm Grading; D014411:Neoplastic Stem Cells / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D021381:Protein Transport; D016601:RNA-Binding Proteins / Q000378:metabolism*; D055748:SOXB1 Transcription Factors / Q000378:metabolism; D000097796:Nucleolin
chemical_list: D000071916:AC133 Antigen; D015703:Antigens, CD; D014408:Biomarkers, Tumor; D005904:Glial Fibrillary Acidic Protein; D006023:Glycoproteins; D010455:Peptides; D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D055748:SOXB1 Transcription Factors; D000097796:Nucleolin; C527782:SOX2 protein, human