Purification of the Synaptic Membrane Glycoprotein D2 from Rat Brain

Rasmussen, Søren; Ramlau, J.; Axelsen, N. H.; Bock, Elisabeth

doi:10.1111/j.1365-3083.1982.tb00636.x

Cited by 63 publications

(39 citation statements)

References 21 publications

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“…NCAM purified from newborn (P0 NCAM) or adult rats (P40 NCAM) according to published procedures [14] is detritonized using SM2 biobeads [15]. Protein is sonicated for 10 s immediately before use and is then immobilized (2/~g/ml; 1 h at 22°C) on nitrocellulose paper discs (5.5 mm diameter).…”

Section: Determination Of Affinity Constantsmentioning

confidence: 99%

Characterization of the kinetics of neural cell adhesion molecule homophilic binding

Moran

Bock

1988

FEBS Letters

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A solid-phase assay has been developed for the investigation of the kinetics of neural cell adhesion molecule (NCAM) binding. Using this assay we can show that NCAM binds to itself in a time-dependent and saturable manner. Binding constants (KB values) of 6.9 x 10 -s M and 1.23 x 10 -~ M, respectively, were obtained for adult and newborn rat NCAM homophilic binding. Binding is specifically inhibited by Fab' fragments of polyclonal anti-NCAM antibodies but is unaffected by heparin or ehondroitin sulphate. This indicates that the NCAM homophilic binding site is separate from and independent of the heparin-binding site and that a developmental modification, probably polysialation, gives rise to marked differences in the adhesive properties of NCAM.

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Section: Determination Of Affinity Constantsmentioning

confidence: 99%

Characterization of the kinetics of neural cell adhesion molecule homophilic binding

Moran

Bock

1988

FEBS Letters

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“…Rabbit antibodies to rat NCAM were made as described by Rasmussen et al [8]. Horse antiserum against E. coli polysialic acid (PSA) residues was a gift from Drs F.A.…”

Section: Methodsmentioning

confidence: 99%

Characterization of soluble forms of NCAM

et al. 1987

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Neural cell adhesion molecule (NCAM) has been described as a family of membrane glycoproteins. However, soluble NCAM immunoreactivity has long been recognized. We here show that soluble NCAM is composed of two quantitatively major polypeptides of M r 180 000 and 115 000 and two minor components of M r 160 000 and 145 000. Soluble NCAM was immunochemically identical to membrane NCAM, was polysialylated and carried the HNK‐1 epitope. It only constituted 0.8% of total NCAM in newborn rat brain. Soluble NCAM appeared in neuronal cell culture medium 15–30 min after the start of synthesis preceding accumulation of membrane‐associated NCAM on the cell surface. This indicates that soluble NCAM contains a secreted component.

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“…Dulbecco's modified Eagle's medium (DME), methionine -free DME and basal medium (Eagle's) ,'sulfate-free with Earle's salts) were obtained from Gibco Laboratories (Grand Island Rasmussen et al [1982],…”

Section: Methodsmentioning

confidence: 99%

“…During early postnatal development this pattern changes to one with three distinct polypeptides with approximate Mr of ca. (A) 200,000, (B) 135.000 and (C) 115.000 [Rasmussen et al, 1982;Edelman and Chuong, 1982;Him et al, 1983;Ibsen et al, 1983;Lyles et al, 1984a, b].…”

Section: Introductionmentioning

confidence: 99%

A Developmental Study of the Biosynthesis of the Neural Cell Adhesion Molecule

Linnemann¹,

Lyles²,

Bock³

1985

Dev Neurosci

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The neural cell adhesion molecule (N-CAM) is a glycoprotein found in neurons, glial cells and muscle cells. In this report we describe developmental changes in biosynthesis of N-CAM polypeptides in rat forebrain explant cultures. N-CAM was synthesized as the following polypeptides: HM_r (M_r between 250,000 and 350,000), A (200,000 M_r), B (135,000 M_r) and C (115,000 M_r). The biosynthetic pattern of N-CAM polypeptides changed during development: the biosynthesis of HM_r and C increased relative to A and B. N-CAM biosynthesis decreased 100-fold from embryonic day 17 to postnatal day 25; N-CAM turnover decreased 350-fold during the same period. N-CAM polysialylation and sulfatation decreased markedly with age, whereas phosphorylation seemed to be constant during development. Only polypeptides A and B were phosphorylated, whereas A, B and C were sulfated. A was more sulfated and phosphorylated than B. It is concluded that the above described modulations of N-CAM may be of importance in the developmental regulation of cell-cell adhesion.

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Purification of the Synaptic Membrane Glycoprotein D2 from Rat Brain

Cited by 63 publications

References 21 publications

Characterization of the kinetics of neural cell adhesion molecule homophilic binding

Characterization of the kinetics of neural cell adhesion molecule homophilic binding

Characterization of soluble forms of NCAM

A Developmental Study of the Biosynthesis of the Neural Cell Adhesion Molecule

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