Neural Surface Antigens during Nervous System Development

Goridis, Christo; Deagostini‐Bazin, Hermine; Hirn, M.; Hirsch, Marie-Rose; Rougon, Geneviève; Sadoul, Rémy; Langley, O.K.; Gombos, G.; Finne, Jukka

doi:10.1101/sqb.1983.048.01.057

Cited by 88 publications

(53 citation statements)

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“…They are expressed in a restricted region of the vesicle and later in the primitive tubule adjacent to the former terminal ampulla, and not in the portion that differentiates into parietal and visceral glomerular epithelium. In nervous tissue, the role of polysialic acid units is thought to involve the control of cellular contacts by modulation of the adhesivity of N-CAM (39,40). Although at present the function of the kidney polysialic acid units remains to be clarified, it is tempting to speculate that they could be involved in the regulation of cell-to-cell contacts during differentiation processes of kidney development.…”

Section: Discussionmentioning

confidence: 99%

Polysialic acid units are spatially and temporally expressed in developing postnatal rat kidney.

Roth¹,

Taatjes²,

Bitter‐Suermann³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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We report the presence of a(2--8)-linked polysialic acid as detected with a monoclonal antibody outside the nervous tissue in the postnatal developing rat kidney. By immunoblot analysis, the reactivity was confined to a broad band of apparent molecular mass 200-250 kDa. By immunohistochemistry, the polysialic acid units were found throughout the ureteric bud-derived collecting duct system. In developing nephrons derived from the metanephrogenic mesenchyme, polysialic acid units were only regionally and transiently expressed. Furthermore, the expression of polysialic acid units was developmentally regulated, as evidenced by their gradual disappearance concomitant with postnatal kidney maturation. These findings suggest a possible role for polysialic acid units in cell-cell contact-mediated renal differentiation processes.

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Section: Discussionmentioning

confidence: 99%

Polysialic acid units are spatially and temporally expressed in developing postnatal rat kidney.

Roth¹,

Taatjes²,

Bitter‐Suermann³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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“…Untreated N-CAM vesicles showed the characteristic triplet of bands at around 180000, 140000 and 120000 M,. Two faint bands of higher MI and a weakly laheled band at 48000 M, were probably contaminants of the N-CAM preparation since they were not stained by Western blotting with polyclonal or monoclonal anti-(N-CAM) antibodias (unpublished results, see also [19]). …”

Section: Proteolytic Digestion O J Adult N-cam In Liposomesmentioning

confidence: 96%

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

Gennarini

Hirn

Deagostini‐Bazin

et al. 1984

European Journal of Biochemistry

105

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The transmembrane orientation of the polypeptide chains present in preparations of adult and neonatal mouse N-CAM was studied using, as a model system, liposome-inserted purified N-CAM preparations. N-CAM purified from adult or neonatal mouse brain was 1251-labeled and reconstituted into artificial lipid vesicles. After trypsin digestion, the peptides thar remained associated with the liposomes were isolated by floatation of the vesicles on sucrose gradients. In control experiments the liposomes were lysed before trypsin treatment. Large, overlapping peptides were obtained after this treatment, several of which were protected by the liposome membrane. Sialic-acidbearing peptides were revealed by their sensitivity to neuraminidase. To distinguish between peptides corresponding to intracellular or extracellular domains use was made of the P61 and H28.123 monoclonal antibodies, which recognize determinants located on the cytoplasmic and the extracellular part of the molecules respectively.There was no indication that the N-CAM chains were inserted in an inside-out configuration. Peptides protected from trypsin attack by the liposomes and recognized only by P61 had M , values of 92000,42000 and 35000. The H28.123 determinant could be mapped to a 32000-M, peptide located close to the membrane at the vesicle's exterior. The bulk of the sialic acid seemed to be carried by a rather short sequence distal to the H28.123-reactive peptide but at some distance from the N terminus. Fragments of very similar M , were generated from young and adult material.However, a 45000-M, peptide from neonatal N-CAM appeared to migrate in the high-Mr region of sodium dodecyl sulfatejpolyacrylamide &ells in its fully sialylated form.It is concluded that (a) identical polypeptide chains are present in young and adult preparation, (b) the 180000-Mr, 140000-Mr and 120000-Mr chains differ by the length of their cytoplasmic extensions and (c) the largest cytoplasmic sequences have a Mr close to 90000. A tentative linear model of the transmembrane topography of the N-CAM polypeptides is presented.The neural cell adhesion molecules, called N-CAMS, are among the best-characterized cell adhesion proteins [I, 21. Unsolved questions concerning their structure are their mode of interaction with the cell membrane and the exact relationship between the two or three structurally similar polypeptides isolated from chick [3] or rodent [4 -61 brain. Our approach to these problems has been to reconstitute purified mouse N-CAM into artificial lipid vesicles and to analyze the peptides generated by trypsin digestion of these vesicles. A number of previous studies have addressed the question of how intrinsic membrane proteins insert in liposomes (see for instance [7 -9]), and it is generally agreed that the proteins interact with the vesicle bilayer in a way closely resembling their arrangement in the native membrane. However, few studies on the transmembrane topography of proteins have Abbreviations. SDS, sodium dodecyl sulfate; Tris/saline, 50 mM Tris pH 7.4,...

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“…The recent explosive interest in cell adhesion molecules (CAMS) is a direct consequence of the fundamental roles they are thought to play during early embryogenesis and tissue formation , has been shown to consist in brain of a family of three glycoproteins of M, 180 000, 140 000 and 120 000 [6,7] which are implicated in neurone-neurone adhesion by a homophilic binding mechanism [8,9]. While N-CAM was originally considered to be limited to neurones in adult tissues, ultrastructural immunocytochemical studies have since provided unequivocal evidence that glial cells, both astrocytes [6,10] and Schwann cells [ 111, also express N-CAM (see also [ 12,131).…”

Section: Introductionmentioning

confidence: 99%

Endocrine cells share expression of N‐CAM with neurones

1987

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The expression of the neural cell adhesion molecule, N-CAM, was examined in the anterior lobe of rat hypophysis by immunocytochemistry at light and electron microscope levels. In addition, N-CAM antigenic determinants present in adrenal medulla, anterior hypophysis and PC12 cells were compared by immunoblotting with those found in cerebellum. All secretory cells in the anterior hypophysis were found to be N-CAM positive on their surfaces, but not all of the three polypeptide determinants typical of cerebellum were present in the endocrine tissues or cell line tested. In addition, a new N-CAM determinant of 49 kDa not present in cerebellum was found in adrenal medulla and hypophysis, although it was absent from PC12 cells. The possible implications of these data are discussed.

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Neural Surface Antigens during Nervous System Development

Cited by 88 publications

References 0 publications

Polysialic acid units are spatially and temporally expressed in developing postnatal rat kidney.

Polysialic acid units are spatially and temporally expressed in developing postnatal rat kidney.

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

Endocrine cells share expression of N‐CAM with neurones

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