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Oral Presentations OP02: Myelin and Diseases of Myelin. NPP2, A matricellular protein expressed during myelination, actively modulates oligodendrocyte adhesion
Author(s) -
Fox M. A.,
Bowlin G.,
Fuss B.
Publication year - 2002
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.81.s1.45_1.x
Subject(s) - oligodendrocyte , microbiology and biotechnology , myelin , biology , matricellular protein , cell adhesion molecule , neuroscience , central nervous system , extracellular matrix
NPP2, also known as phosphodiesterase‐I alpha/autotaxin, is a type‐II membrane protein that belongs to the nucleotide pyrophosphatase/phosphodiesterase family (NPP). We have recently demonstrated that NPP2 is expressed and released by differentiating oligodendrocytes during the critical stages of CNS myelination. The structural domains of this secreted macromolecule suggest a functional role in the regulation of oligodendrocyte adhesion. Here, we present data that demonstrates that NPP2 interferes with the ability of oligodendroglial cells to adhere to known CNS adhesion molecules present during the onset of myelination, such as fibronection, vitronectin, and merosin (laminin2). Responses to NPP2 appear to be regulated by a different mechanism depending on the developmental stage of the oligodendrocyte. Although the exact mechanisms for NPP2 mediated counter‐adhesion are unknown, our studies have implicated that an active signalling mechanism involving heterotrimeric G proteins is responsible for adhesion modulation. These studies clearly define a role of NPP2 as a matricellular protein modulating oligodendrocyte adhesion and suggest that NPP2 function may represent the first step of oligodendrocyte remodelling when differentiating oligodendrocytes are actively involved in the formation of the myelin sheath.