scholarly journals Clinical Mutations in the L1 Neural Cell Adhesion Molecule Affect Cell-Surface Expression

2000 ◽  
Vol 20 (15) ◽  
pp. 5696-5702 ◽  
Author(s):  
Hugh D. Moulding ◽  
Robert L. Martuza ◽  
Samuel D. Rabkin
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Surface Expression ◽  
Neural Cell ◽  
Cell Surface Expression ◽  
Neural Cell Adhesion

scholarly journals Olfactory neurons express a unique glycosylated form of the neural cell adhesion molecule (N-CAM).

1990 ◽  
Vol 110 (5) ◽  
pp. 1729-1743 ◽  
Author(s):  
B Key ◽  
R A Akeson
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Adhesion Molecule ◽  
Olfactory System ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Olfactory Neurons ◽  
Cell Surface Glycoprotein ◽  
Neural Cell Adhesion

mAb-based approaches were used to identify cell surface components involved in the development and function of the frog olfactory system. We describe here a 205-kD cell surface glycoprotein on olfactory receptor neurons that was detected with three mAbs: 9-OE, 5-OE, and 13-OE. mAb 9-OE immunoreactivity, unlike mAbs 5-OE and 13-OE, was restricted to only the axons and terminations of the primary sensory olfactory neurons in the frog nervous system. The 9-OE polypeptide(s) were immunoprecipitated and tested for cross-reactivity with known neural cell surface components including HNK-1, the cell adhesion molecule L1, and the neural cell adhesion molecule (N-CAM). These experiments revealed that 9-OE-reactive molecules were not L1 related but were a subset of the 200-kD isoforms of N-CAM. mAb 9-OE recognized epitopes associated with N-linked carbohydrate residues that were distinct from the polysialic acid chains present on the embryonic form of N-CAM. Moreover, 9-OE N-CAM was a heterogeneous population consisting of subsets both with and without the HNK-1 epitope. Thus, combined immunohistochemical and immunoprecipitation experiments have revealed a new glycosylated form of N-CAM unique to the olfactory system. The restricted spatial expression pattern of this N-CAM glycoform suggests a possible role in the unusual regenerative properties of this sensory system.

Neural cell adhesion molecule: structure, immunoglobulin-like domains, cell surface modulation, and alternative RNA splicing

Science ◽  
1987 ◽  
Vol 236 (4803) ◽  
pp. 799-806 ◽  
Author(s):  
B. Cunningham ◽  
J. Hemperly ◽  
B. Murray ◽  
E. Prediger ◽  
R Brackenbury ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Adhesion Molecule ◽  
Rna Splicing ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Molecule Structure ◽  
Neural Cell Adhesion ◽  
Surface Modulation

scholarly journals Biosynthesis, membrane association, and release of N-CAM-120, a phosphatidylinositol-linked form of the neural cell adhesion molecule.

1987 ◽  
Vol 105 (6) ◽  
pp. 2489-2500 ◽  
Author(s):  
H T He ◽  
J Finne ◽  
C Goridis
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Transmembrane Domain ◽  
Extracellular Fluid ◽  
Neural Cell ◽  
Ionic Detergent ◽  
Neural Cell Adhesion

The neural cell adhesion molecule (N-CAM) of rodents comprises three distinct proteins of Mr 180,000, 140,000, and 120,000 (designated N-CAM-180, -140, and -120). They are expressed in different proportions by different tissues and cell types. but the individual contribution of each form to cell adhesion is presently unknown. Previous studies have shown that the two N-CAM species of higher relative molecular mass span the membrane whereas N-CAM-120 lacks a transmembrane domain and can be released from the cell surface by phosphatidylinositol-specific phospholipase C. In this report, we provided evidence that N-CAM-120 contained covalently bound phosphatidylinositol and studied N-CAM-120 from its biosynthesis to its membrane insertion and finally to its release from the cell surface. Evidence was presented showing that the lipid tail of N-CAM-120 contained ethanolamine as is the case for other lipid-linked molecules. The phospholipid anchor was attached to the protein during the first minutes after completion of the polypeptide chain. This process took place in the endoplasmic reticulum as judged from endoglycosidase H digestion experiments. Immediately after a 2-min pulse with [35S]methionine, we detected also a short-lived precursor that had not yet acquired the lipid tail. Pulse-chase studies established that N-CAM-120 was transported to the cell surface from which it was slowly released into the extracellular milieu. The molecules recovered in the incubation medium appeared to have lost all of their bound fatty acid but only around half of the ethanolamine. Upon fractionation of brain tissue, approximately 75% of N-CAM-120 was recovered with a membrane fraction and approximately 25% in a membrane-free supernatant. A small proportion (approximately 6%) was found to be resistant to extraction by non-ionic detergent. A major posttranslational modification of N-CAM is polysialylation. Our results showed that also N-CAM-120 was polysialylated in the young postnatal brain and released in this form from cultured cerebellar cells. The presence of N-CAM in a form that can be released from the cell surface and accumulates in the extracellular fluid suggests a novel mechanism by which N-CAM-mediated adhesion may be modulated.

Expression of Neural Cell Adhesion Molecule and Polysialic Acid in Cultured Spiral Ganglion Neurons

Skull Base ◽  
2007 ◽  
Vol 17 (S 1) ◽  
Author(s):  
Kyoung Ho Park ◽  
Ki Hong Jang ◽  
Sang Yeo ◽  
Helge Rask-Andersen ◽  
Frederic Troy, II
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Polysialic Acid ◽  
Spiral Ganglion ◽  
Neural Cell ◽  
Spiral Ganglion Neurons ◽  
Neural Cell Adhesion ◽  
Ganglion Neurons
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