Lectin binding sites on the luminal surface of ependymal cells of the rat spinal cord: implications for neuropathological investigation.
Twenty fluorescein isothiocyanate-labeled lectins were applied to formalin-fixed, paraffin-embedded sections of rat spinal cord to delineate the specific lectin binding sites on the ependymal cells. Only two lectins, Solanum tuberosum agglutinin (STA) and wheat germ agglutinin (WGA), were found to bind intensely to the ciliated surface of rat ependymal cells. Inhibition studies indicated that terminal N-acetylglucosamine and sialic acid were abundantly present on the ciliated surface of ependymal cells and accounted for the binding of these two lectins. Experimentally induced hydromyelia was accompanied by a loss of lectin binding sites on the ependymal cells. These data show that STA and WGA represent potentially valuable new histochemical markers for ciliated ependymal cells.
D000818:Animals; D050260:Carbohydrate Metabolism; D004805:Ependyma / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism; D008856:Microscopy, Fluorescence; D051381:Rats; D011919:Rats, Inbred Strains; D011975:Receptors, Mitogen / Q000378:metabolism*; D013116:Spinal Cord / Q000378:metabolism*; D013119:Spinal Cord Injuries / Q000378:metabolism*
D037102:Lectins; D011975:Receptors, Mitogen