A novel soluble brain-specific protein (Sy-1)☆Identification and partial characterization

Gennarini, Gianfranco; Corsi, Patrizia; Pavia, R.; Vitiello, Francesco; Benedetta, C. Di

doi:10.1016/0165-5728(83)90012-7

Cited by 2 publications

(1 citation statement)

References 21 publications

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“…More recently, soluble D2 was found in young and adult rat brain [35]. However, the relationship between the soluble and membrane-bound molecules on the one hand and the three bands revealed in SDS/polyacrylamide gels on the other hand has never been studied.…”

Section: Monoclonal Antibodiesmentioning

confidence: 99%

Studies on the transmembrane disposition of the neural cell adhesion molecule N‐CAM

Gennarini

Rougon

Deagostini‐Bazin

et al. 1984

European Journal of Biochemistry

126

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The N‐CAMs are a group of surface glycoproteins involved in adhesive interactions of neurones. Related molecules of the mouse nervous system, identified in our laboratory, have been called BSP‐2 and shown to act as ligands in adhesion of neuroblastoma cells. Results presented in this report show that they are immunochemically identical with N‐CAM. A monoclonal anti‐(N‐CAM) antibody, that recognized a determinant accessible only after permeabilization of intact cells, was used to define the mode of association of the N‐CAMs with the plasma membrane. This antibody bound a 35000‐Mr fragment in lysates of trypsin‐treated neuroblastoma cells. It is concluded that the antibody reacts with a transmembrane or cytoplasmic domain of the molecules. The same antibody recognized the Mr‐180000 and Mr‐140000 proteins but not the Mr‐120000 chain, which copurify from adult mouse brain. The latter polypeptide was detected in the cytosol and could be partially released from brain membranes by osmotic shock. Part or all of the Mr‐120000 protein may thus lack a transmembrane segment. Our conclusion that the N‐CAM forms of higher Mr are transmembrane proteins was further corroborated by our finding that they contain phosphoserine residues, which can be labeled with (32P)phosphate in intact neuroblastoma cells.

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Section: Monoclonal Antibodiesmentioning

confidence: 99%

Studies on the transmembrane disposition of the neural cell adhesion molecule N‐CAM

Gennarini

Rougon

Deagostini‐Bazin

et al. 1984

European Journal of Biochemistry

126

View full text Add to dashboard Cite

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Ontogenetic changes of the soluble and membrane‐bound D2 glycoprotein in rat forebrain

Gennarini¹,

Corsi²,

Pavia³

et al. 1984

Intl J of Devlp Neuroscience

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A soluble form of the D2 glycoprotein, detected in the rat brain hypotonic extract, is described. Its specific relative concentration did not differ significantly in the three examined cerebral regions (forebrain, brainstem and cerebellum), while in the cerebellum the membrane-bound form was about three and four times more concentrated than in the forebrain and brainstem, respectively. No sizeable developmental variations of the soluble D2 concentration could be detected in forebrain, whereas the amount of the membrane-bound protein rose from birth to postnatal day 6 and then decreased to the adult value (about 40% of the newborn concentration). Ontogenetic modifications of the membranous D2 glycans (studied through the binding of the molecule to several lectins) occur around postnatal day 18 when the binding to Ricinus communis lectin, specific for galactose, becomes evident. At all ages both soluble and membrane-bound forms bind to Concanavalin A, specific for mannose and glucose, and to wheat germ agglutinin, specific for N-acetylglucosamine, while the lack of binding to Ulex europeus lectin suggests the absence of discrete amount of fucose. The results are discussed in relation to the possible involvement of D2 glycoprotein in cell-to-cell adhesion.

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A novel soluble brain-specific protein (Sy-1)☆Identification and partial characterization

Cited by 2 publications

References 21 publications

Studies on the transmembrane disposition of the neural cell adhesion molecule N‐CAM

Studies on the transmembrane disposition of the neural cell adhesion molecule N‐CAM

Ontogenetic changes of the soluble and membrane‐bound D2 glycoprotein in rat forebrain

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