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Volume 271, Number 12, Issue of March 22, 1996 pp. 6694-6701
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
The Occurrence of Novel 9-O-Sulfated N-Glycolylneuraminic Acid-capped 25-O-linked Oligo/PolyNeu5Gc Chains in Sea Urchin Egg Cell Surface Glycoprotein
IDENTIFICATION OF A NEW CHAIN TERMINATION SIGNAL FOR POLYSIALYLTRANSFERASE

(Received for publication, July 20, 1995; and in revised form, November 13, 1995)

Shinobu Kitazume ,  Ken Kitajima ,  Sadako Inoue ,  Stuart M. Haslam ,  Howard R. Morris ,  Anne Dell ,  William J. Lennarz ,  Yasuo Inoue

We report the isolation and structural characterization of an oligo/polysialic acid-containing glycopeptide fraction (designated ESP-Sia) prepared from the egg cell surface complex of the sea urchin, Hemicentrotus pulcherrimus, by exhaustive pronase treatment. The carbohydrate chains isolated from ESP-Sia were shown to consist of O-linked oligo/polysialic acid-containing glycan units and N-linked carbohydrate chains. The present studies have revealed that the O-linked oligo/polysialic acid-containing glycan chains derived from the ESP-Sia were similar to those present in egg jelly coat polysialylated glycoprotein in being composed of tandem repeats of N-glycolylneuraminic acid (Neu5Gc) glycosidically linked in a novel fashion through the glycolyl group, (5-ONeu5Gcalpha2). However, they differ from the egg jelly coat in two key respects. First, the average degree of polymerization of the oligo/polysialic acid chains of ESP-Sia is only 3; a value far lower than that found in the jelly coat glycoprotein (average degree of polymerization was about 20). Second, ESP-Sia is uniquely characterized by the presence of 9-O-sulfated N-glycolylneuraminic acid (Neu5Gc9HSO(3)) residues at the nonreducing termini of the (5-ONeu5Gcalpha 2) chains. The terminal sialyl residues in the Neu5Gc9HSO(3)alpha2(5-ONeu5Gcalpha2)chains were totally resistant to exosialidases. The discovery of Neu5Gc9HSO(3) as the nonreducing terminal residue of oligo/poly(5-ONeu5Gcalpha 2) group is especially noteworthy in that Neu5Gc9HSO(3) appears to be of limited distribution among glycoconjugates. Following the earlier discovery of oligo/polysialic acid chains capped with KDN, i.e. KDNalpha2(8Neu5Gcalpha2), found in rainbow trout egg polysialoglycoproteins, it now appears that the sulfated Neu5Gc can serve a similar capping function.



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