JBC Ideal method for primary cell transfection

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J Biol Chem, Vol. 274, Issue 53, 37637-37643, December 31, 1999

Enhanced Binding of the Neural Siglecs, Myelin-associated Glycoprotein and Schwann Cell Myelin Protein, to Chol-1 (alpha -Series) Gangliosides and Novel Sulfated Chol-1 Analogs*

Brian E. CollinsDagger §, Hiromi Ito, Naoki Sawada, Hideharu Ishida, Makoto Kiso, and Ronald L. SchnaarDagger ∥

From the Dagger  Departments of Pharmacology and Neuroscience, The Johns Hopkins School of Medicine, Baltimore, Maryland 21205 and the  Department of Applied Bioorganic Chemistry, Gifu University, Gifu 501-1193, Japan

Extended glycoconjugate binding specificities of three sialic acid-dependent immunoglobulin-like family member lectins (siglecs), myelin-associated glycoprotein (MAG), Schwann cell myelin protein (SMP), and sialoadhesin, were compared by measuring siglec-mediated cell adhesion to immobilized gangliosides. Synthetic gangliosides bearing the alpha -series determinant (NeuAc alpha 2,6-linked to GalNAc on a gangliotetraose core) were tested, including GD1alpha (IV3NeuAc, III6NeuAc-Gg4OseCer), GD1alpha with modified sialic acid residues at the III6-position, and the "Chol-1" gangliosides GT1aalpha (IV3NeuAc, III6NeuAc, II3NeuAc-Gg4OseCer) and GQ1balpha (IV3NeuAc, III6NeuAc, II3(NeuAc)2-Gg4OseCer). The alpha -series gangliosides displayed enhanced potency for MAG- and SMP-mediated cell adhesion (GQ1balpha  > GT1aalpha , GD1alpha  > GT1b, GD1a >> GM1 (nonbinding)), whereas sialoadhesin-mediated adhesion was comparable with alpha -series and non-alpha -series gangliosides. GD1alpha derivatives with modified sialic acids (7-, 8-, or 9-deoxy) or sulfate (instead of sialic acid) at the III6-position supported adhesion comparable with that of GD1alpha . Notably, a novel GT1aalpha analog with sulfates at two internal sites of sialylation (NeuAcalpha 2,3Galbeta 1,4GalNAc-6-sulfatebeta 1, 4Gal3-sulfatebeta 1,4Glcbeta 1,1'ceramide) was the most potent siglec-binding structure tested to date (10-fold more potent than GT1aalpha in supporting MAG and SMP binding). Together with prior studies, these data indicate that MAG and SMP display an extended structural specificity with a requirement for a terminal alpha 2,3-linked NeuAc and great enhancement by nearby precisely spaced anionic charges.

* This work was supported in part by National Institutes of Health Grant NS37096, a grant from the National Multiple Sclerosis Society, National Science Foundation Grant IBN-9631745, and a grant from the Paralyzed Veterans of America Spinal Cord Research Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported in part by National Institutes of Health Grant GM07626. Present address: Dept. of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037.

∥ To whom correspondence should be addressed: Dept. of Pharmacology and Molecular Sciences, The Johns Hopkins School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205-2185. Tel.: 410-955-8392; Fax: 410-955-3023; E-mail: schnaar@jhu.edu.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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