Osteopontin (OPN) was initially identified as glycosylated phosphoprotein in bones of vertebrates. Recently, OPN is reported to express in the primitive neuroepithelia of early chick embryonic hindbrain. We have demonstrated that rat OPN is immunohistochemically localized in the white matter of chick CNS. We have further confirmed the specificity of OPN cross-immunoreaction in myelin using demyelinated optic nerve induced by lysophosphatidylcholine (LPC), where the intensity of immunoreaction was closely related to the degree of demyelination. Immunoblot analyses showed that rat OPN antibody recognized a protein with molecular weights of approximately 47 kDa from chick CNS. Our data suggest that the antigen recognized by rat OPN is a previously undescribed myelin-associated protein in the chick CNS.
Copyright 1999 Elsevier Science B.V.