Binding properties of liposomes containing the myelin-associated glycoprotein MAG to neural cell cultures

TY - JOUR

T1 - Binding properties of liposomes containing the myelin-associated glycoprotein MAG to neural cell cultures

AU - Sadoul, R

AU - Fahrig, T

AU - Bartsch, U

AU - Schachner, M

PY - 1990/1

Y1 - 1990/1

N2 - The myelin-associated glycoprotein MAG is a neural cell adhesion molecule which belongs to the immunoglobulin superfamily and the carbohydrate based L2/HNK-1 family of adhesion molecules. In this study we further characterize the adhesive properties of MAG. MAG incorporated into liposomes bound to cultured peripheral and central nervous system neurons known to be myelinated in vivo. Expression of the neuronal MAG receptor(s) on spinal cord neurons increased with time in culture and correlated with the time of active myelination of these neurons in vivo. MAG bound only poorly if at all to cerebellar neurons which are not myelinated in vivo and not to cultured oligodendrocytes or Schwann cells. A low level of MAG binding to astrocytes or fibroblast-like cells that was MAG antibody inhibitable could also be observed. The adhesion molecules L1 and N-CAM, two other members of the immunoglobulin superfamily, were not found to be the neuronal receptors for MAG. RGD containing peptides did not inhibit binding of MAG-liposomes to neurons. The soluble form of MAG which contains most, if not all, of the extracellular domain of the molecule and binds to collagen, did not interfere with the binding of MAG-liposomes to neurons. Conversely, MAG-liposomes did not bind to collagen, suggesting that MAG shows different binding properties as an integral membrane protein than as a fragment containing the extracellular domain of the molecule.

AB - The myelin-associated glycoprotein MAG is a neural cell adhesion molecule which belongs to the immunoglobulin superfamily and the carbohydrate based L2/HNK-1 family of adhesion molecules. In this study we further characterize the adhesive properties of MAG. MAG incorporated into liposomes bound to cultured peripheral and central nervous system neurons known to be myelinated in vivo. Expression of the neuronal MAG receptor(s) on spinal cord neurons increased with time in culture and correlated with the time of active myelination of these neurons in vivo. MAG bound only poorly if at all to cerebellar neurons which are not myelinated in vivo and not to cultured oligodendrocytes or Schwann cells. A low level of MAG binding to astrocytes or fibroblast-like cells that was MAG antibody inhibitable could also be observed. The adhesion molecules L1 and N-CAM, two other members of the immunoglobulin superfamily, were not found to be the neuronal receptors for MAG. RGD containing peptides did not inhibit binding of MAG-liposomes to neurons. The soluble form of MAG which contains most, if not all, of the extracellular domain of the molecule and binds to collagen, did not interfere with the binding of MAG-liposomes to neurons. Conversely, MAG-liposomes did not bind to collagen, suggesting that MAG shows different binding properties as an integral membrane protein than as a fragment containing the extracellular domain of the molecule.

KW - Animals

KW - Cells, Cultured

KW - Extracellular Matrix

KW - Liposomes

KW - Mice

KW - Mice, Inbred Strains

KW - Myelin Proteins

KW - Myelin-Associated Glycoprotein

KW - Spinal Cord

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1002/jnr.490250102

DO - 10.1002/jnr.490250102

M3 - SCORING: Journal article

C2 - 1690814

VL - 25

SP - 1

EP - 13

JO - J NEUROSCI RES

JF - J NEUROSCI RES

SN - 0360-4012

IS - 1

ER -