Biosynthesis of the neural cell adhesion molecule: characterization of polypeptide C.
J Cell Biol
; 101(6): 2310-5, 1985 Dec.
Article
em En
| MEDLINE
| ID: mdl-4066759
ABSTRACT
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Glicoproteínas
/
Adesão Celular
/
Proteínas de Membrana
/
Antígenos de Superfície
Idioma:
En
Ano de publicação:
1985
Tipo de documento:
Article