Immunohistochemical localization of laminin, neural cell adhesion molecule, collagen type IV and T-61 antigen in the embryonic retina of the Japanese quail by in vivo injection of antibodies

1987 ◽  
Vol 249 (3) ◽  
Author(s):  
Willi Halfter ◽  
ChenSong Fua
2007 ◽  
Vol 283 (1) ◽  
pp. 17-28 ◽  
Author(s):  
Sebastian P. Galuska ◽  
Rudolf Geyer ◽  
Rita Gerardy-Schahn ◽  
Martina Mühlenhoff ◽  
Hildegard Geyer

2007 ◽  
Vol 103 (s1) ◽  
pp. 65-71 ◽  
Author(s):  
Kaya Bork ◽  
Daniel Gagiannis ◽  
André Orthmann ◽  
Wenke Weidemann ◽  
Maria Kontou ◽  
...  

1992 ◽  
Vol 116 (4) ◽  
pp. 1063-1070 ◽  
Author(s):  
R Probstmeier ◽  
T Fahrig ◽  
E Spiess ◽  
M Schachner

To gain insights into the functional role of the molecular association between neural adhesion molecules and extracellular matrix constituents, soluble forms of the myelin-associated glycoprotein (MAG) and the neural cell adhesion molecule (N-CAM), representing most of the extracellular domains of the molecules, were investigated in their ability to modify fibrillogenesis of collagen type I. MAG and N-CAM retarded the rate of fibril formation, as measured by changes in turbidity, and increased the diameter of the fibrils formed, but did not change the banding pattern when compared to collagen type I in the absence of adhesion molecules. Scatchard plot analysis of the binding of MAG and N-CAM to the fibril-forming collagen types I, II, III, and V suggest one binding site for N-CAM and two binding sites for MAG. Binding of MAG, but not of N-CAM, to collagen type I was decreased during fibril formation, probably due to a reduced accessibility of one binding site for MAG during fibrillogenesis. These results indicate that the neural adhesion molecules can influence the configuration of extracellular matrix constituents, thus, implicating them in the modulation of cell-substrate interactions.


1993 ◽  
Vol 295 (3) ◽  
pp. 833-840 ◽  
Author(s):  
M Olsen ◽  
L Krog ◽  
K Edvardsen ◽  
L T Skovgaard ◽  
E Bock

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.


2011 ◽  
Vol 18 (5) ◽  
pp. 306-313 ◽  
Author(s):  
G. Dallerac ◽  
M. Zerwas ◽  
T. Novikova ◽  
D. Callu ◽  
P. Leblanc-Veyrac ◽  
...  

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