scholarly journals Enzyme-dependent Variations in the Polysialylation of the Neural Cell Adhesion Molecule (NCAM)in Vivo

2007 ◽  
Vol 283 (1) ◽  
pp. 17-28 ◽  
Author(s):  
Sebastian P. Galuska ◽  
Rudolf Geyer ◽  
Rita Gerardy-Schahn ◽  
Martina Mühlenhoff ◽  
Hildegard Geyer
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Neural Cell Adhesion

scholarly journals Intact transmembrane isoforms of the neural cell adhesion molecule are released from the plasma membrane

1993 ◽  
Vol 295 (3) ◽  
pp. 833-840 ◽  
Author(s):  
M Olsen ◽  
L Krog ◽  
K Edvardsen ◽  
L T Skovgaard ◽  
E Bock
Keyword(s):  
Cerebrospinal Fluid ◽  
Plasma Membrane ◽  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Soluble Form ◽  
Neural Cell Adhesion

Three soluble neural cell adhesion molecule (NCAM) polypeptide classes of M(r) values 190,000 (NCAM-s1), 135,000 (NCAM-s2) and 115,000-110,000 (NCAM-s3) have been demonstrated in rat brain and cerebrospinal fluid [Krog, Olsen, Dalseg, Roth and Bock (1992) J. Neurochem. 59, 838-847]. NCAM-s3 is known to arise from released glycosylphosphatidylinositol (GPI)-linked NCAM [He, Finne and Goridis (1987) J. Cell. Biol. 105, 2489-2500] as well as from extracellularly cleaved transmembrane NCAM isoforms [Nybroe, Linnemann and Bock (1989) J. Neurochem. 53, 1372-1378]. In this study the origin of NCAM-s1 and NCAM-s2 and the function of soluble NCAM forms were investigated. It was shown that all three soluble forms could be released from brain membranes with M(r) values identical to the three major membrane-associated forms: the large transmembrane 190,000-M(r) form (NCAM-A), the smaller transmembrane 135,000-M(r) form (NCAM-B) and the GPI-anchored 115,000-110,000-M(r) form (NCAM-C). A polyclonal antibody, directed against transmembrane and cytoplasmic epitopes common to NCAM-A and NCAM-B, was shown to react with NCAM-s1 and NCAM-s2. Furthermore, NCAM-B was shown to be shed in a presumably intact soluble form from membranes of cells transfected with this isoform. Thus, NCAM-s1 and NCAM-s2 probably represent intact released transmembrane NCAM-A and NCAM-B. The soluble transmembrane forms are likely to exist in vivo, as NCAM-s1 and NCAM-s2 were readily demonstrated in cerebrospinal fluid. By density-gradient centrifugation it was shown that shed transmembrane NCAM-B was present in fractions of high, as well as low, density, indicating that a fraction of the shed NCAM is associated with minor plasma membrane fragments. Finally, it was shown that isolated soluble NCAM inhibited cell binding to an immobilized NCAM substratum, attributing a pivotal role to soluble NCAM in vivo as a modulator of NCAM-mediated cell behaviour.

scholarly journals The neural cell adhesion molecule-derived peptide FGL facilitates long-term plasticity in the dentate gyrus in vivo

2011 ◽  
Vol 18 (5) ◽  
pp. 306-313 ◽  
Author(s):  
G. Dallerac ◽  
M. Zerwas ◽  
T. Novikova ◽  
D. Callu ◽  
P. Leblanc-Veyrac ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Dentate Gyrus ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Neural Cell Adhesion
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