Antibody that reacts with 6-sulfated sialyl Lewis X

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Blood proteins or globulins – e.g. – proteoglycans – platelet...

Reexamination Certificate

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C530S387100, C536S001110

Reexamination Certificate

active

07423126

ABSTRACT:
A polypeptide of N-acetylglucosamine-6-O-sulfotransferase and a DNA encoding the peptide are provided. The polypeptide is (a) or (b) below:(a) a polypeptide consisting of an amino acid sequence represented by SEQ ID NO: 2; or(b) a polypeptide which comprises an amino acid sequence including substitution, deletion, insertion or transposition of one or few amino acids in the amino acid sequence of (a) and which has an enzymatic activity to transfer a sulfate group from a sulfate group donor to a hydroxyl group at 6 position of an N-acetylglucosamine residue located at a non-reducing end of an oligosaccharide represented by the formula I:in-line-formulae description="In-line Formulae" end="lead"?GlcNAcβ1-3Galβ1-4GlcNAc   (I)in-line-formulae description="In-line Formulae" end="tail"?wherein GlcNAc represents an N-acetylglucosamine residue, Gal represents a galactose residue, β1-3 represents a β1-3 glycosidic linkage, and β1-4 represents a β1-4 glycosidic linkage.

REFERENCES:
Yasumoto, et al., “Characterization of a Rat Liver Golgi Sulphotransferase Responsible for the 6-O-Sulphation of N-Acetylglucosamine Residues in β-Linkage to Mannose; Role in Assembly of Sialyl-Galactosyl-N-Acetylglucosamine 6-Sulphate Sequence of N-Linked Oligosaccharides,”Journal of Biochemistry, vol. 319, pp. 209-216, 1996.
Degroote, et al., “Characterization of an N-Acetylglucosamine-6-O-Sulfotransferase from Human Respiratory Mucosa Active on Mucin Carbohydrate Chains,”The Journal of Biological Chemistry, vol. 272, No. 47, pp. 29493-29501, Nov. 21, 1997.
Bowman, et al., “Identification of an N-Acetylglucosamine-6-O-Sulfotransferase Activity Specific to Lymphoid Tissue: An Enzyme with a Possible Role in Lymphocyte Homing,”Chemistry&Biology, vol. 5, pp. 447-460, Aug. 1998.
Uchimura, et al., “Human N-Acetylglucosamine-6-O-Sulfotransferase Involved in the Biosynthesis of 6-Sulfo Sialyl Lewis X: Molecular Cloning, Chromosomal Mapping, and Expression in Various Organs and Tumor Cells,”Journal of Biochemistry, vol. 124, pp. 670-678, 1998.
Uchimura, et al., “Molecular Cloning and Characterization of an N-Acetylglucosamine-6-O-Sulfotransferase,”The Journal of Biological Chemistry, vol. 273, No. 35, pp. 22577-22583, Aug. 28, 1998.
Nakazawa, et al., “Glycosyltransferase and Sulfotransferase Activities in Chick Corneal Stromal Cells Before and After In Vitro Culture,”Archives of Biochemistry and Biophysics, vol. 359, No. 2, pp. 269-282, Nov. 14, 1998.
Tsuboi, et al., “6′-Sulfo Sialyl Lexbut Not 6-Sulfo Sialyl LexExpressed on the Cell Surface Supports L-Selectin-Mediated Adhesion,”The Journal of Biological Chemistry, vol. 271, No. 44, pp. 27213-27216, Nov. 1996.
Chyandresekaran, et al., “Specificity Analysis of Three Clonal and Five Non-Clonal α1,3-L-Fucosyltransferases with Sulfated, Sialylated, or Fucosylated Synthetic Carbohydrates as Acceptors in Relation to the Assembly of 3′-Sialyl-6′-Sulfo Lewis x (the L-Selectin Ligand) and Related Complex Structures,”Biochemistry, vol. 35, pp. 8925-9833, 1996.
Mitsuoka, et al., “Identification of a Major Carbohydrate Capping Group of the L-Selectin Ligand on High Endothelial Venules in Human Lymph Nodes as 6-Sulfo Sialyl Lewis X,”The Journal of Biological Chemistry, vol. 273, No. 18, pp. 11225-11233, May 1, 1998.

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