Studies on the transmembrane disposition of the neural cell adhesion molecule N-CAM. A monoclonal antibody recognizing a cytoplasmic domain and evidence for the presence of phosphoserine residues.

Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model: Print Cited Medium: Print ISSN: 0014-2956 (Print) Linking ISSN: 00142956 NLM ISO Abbreviation: Eur J Biochem Subsets: MEDLINE

Publication: -2004: Oxford, UK : Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Original Publication: Berlin, New York, Springer.

Antigens, Surface/*analysis ; Membrane Proteins/*analysis ; Neuroblastoma/*analysis ; Neurons/*analysis; Animals ; Antibodies, Monoclonal ; Antigens, Neoplasm/analysis ; Brain/cytology ; Brain Chemistry ; Cell Adhesion ; Cell Adhesion Molecules ; Cell Line ; Cell Membrane/analysis ; Cell Membrane/immunology ; Cytoplasm/analysis ; Electrophoresis, Polyacrylamide Gel ; Mice ; Molecular Weight ; Neuroblastoma/immunology ; Neuroblastoma/pathology ; Neurons/cytology ; Neurons/immunology ; Phosphoserine/analysis ; Precipitin Tests ; Rats

The N-CAMs are a group of surface glycoproteins involved in adhesive interactions of neurones. Related molecules of the mouse nervous system, identified in our laboratory, have been called BSP-2 and shown to act as ligands in adhesion of neuroblastoma cells. Results presented in this report show that they are immunochemically identical with N-CAM. A monoclonal anti-(N-CAM) antibody, that recognized a determinant accessible only after permeabilization of intact cells, was used to define the mode of association of the N-CAMs with the plasma membrane. This antibody bound a 35 000-Mr fragment in lysates of trypsin-treated neuroblastoma cells. It is concluded that the antibody reacts with a transmembrane or cytoplasmic domain of the molecules. The same antibody recognized the Mr-180 000 and Mr-140 000 proteins but not the Mr-120 000 chain, which co-purify from adult mouse brain. The latter polypeptide was detected in the cytosol and could be partially released from brain membranes by osmotic shock. Part or all of the Mr-120 000 protein may thus lack a transmembrane segment. Our conclusion that the N-CAM forms of higher Mr are transmembrane proteins was further corroborated by our finding that they contain phosphoserine residues, which can be labeled with (32P)phosphate in intact neuroblastoma cells.

0 (Antibodies, Monoclonal)
0 (Antigens, Neoplasm)
0 (Antigens, Surface)
0 (Cell Adhesion Molecules)
0 (Membrane Proteins)
17885-08-4 (Phosphoserine)

Date Created: 19840702 Date Completed: 19840904 Latest Revision: 20190620

20240829

10.1111/j.1432-1033.1984.tb08250.x

6745267