Biosynthesis of the neural cell adhesion molecule: characterization of polypeptide C
Research output: Contribution to journal › Journal article › Research › peer-review
The biosynthesis of the neural cell adhesion molecule (N-CAM) was studied in primary cultures of rat cerebral glial cells, cerebellar granule neurons, and skeletal muscle cells. The three cell types produced different N-CAM polypeptide patterns. Glial cells synthesized a 135,000 Mr polypeptide B and a 115,000 Mr polypeptide C, whereas neurons expressed a 200,000 Mr polypeptide A as well as polypeptide B. Skeletal muscle cells produced polypeptide B. The polypeptides synthesized by the three cell types were immunochemically identical. The membrane association of polypeptide C was investigated with methods that distinguish peripheral and integral membrane proteins. Polypeptide C was found to be a peripheral membrane protein, whereas polypeptides A and B were integral membrane proteins with cytoplasmic domains of approximately 50,000 and approximately 25,000 Mr, respectively. The affinity of the membrane binding of polypeptide C increased during postnatal development. The posttranslational modifications of polypeptide C were investigated in glial cell cultures, and it was found to be N-linked glycosylated and sulfated.
Original language | English |
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Journal | Journal of Cell Biology |
Volume | 101 |
Issue number | 6 |
Pages (from-to) | 2310-5 |
Number of pages | 5 |
ISSN | 0021-9525 |
Publication status | Published - 1985 |
Bibliographical note
Keywords: Age Factors; Animals; Antigens, Surface; Astrocytes; Cell Adhesion; Cell Adhesion Molecules; Cells, Cultured; Cerebellum; Cytoplasm; Glycoproteins; Macromolecular Substances; Membrane Proteins; Molecular Weight; Muscles; Protein Processing, Post-Translational; Rats; Sulfates; Tunicamycin
ID: 21607038