Identification of polysialic acid-containing glycoprotein in the jelly coat of sea urchin eggs. Occurrence of a novel type of polysialic acid structure

S. Kitazume, K. Kitajima, S. Inoue, F. A. Troy, J. W. Cho, W. J. Lennarz, Y. Inoue

Research output: Contribution to journalArticle

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Abstract

Sea urchin eggs are surrounded by a gelatinous layer (called the jelly coat) that consists of mixture of fucose-rich polysaccharides and sialic acid-rich glycoproteins. Chemical and 500 MHz 1H NMR spectroscopic studies revealed for the first time the presence of a novel polysialic acid (polySia) structure in the jelly coat glycoproteins isolated from Hemicentrotus pulcherrimus (designated polySia-gp(H)). The structure of the polySia chains was thoroughly characterized as (→5-O(glycolyl)-Neu5Gcα2→)(n), where n ranges from 4 to more than 40 Neu5Gc residues. The polyNeu5Gc chains were attached to core oligosaccharides that were O-glycosidically linked to threonine residues on a core polypeptide. Each polypeptide contained about 17 O-linked polysialylglycan chains. The apparent molecular weight of polySia- gp(H) was 180,000. The expression of this new polySia structure in place of α2→8-linked polySia is the main structural feature that distinguishes polySia-gp from other known polysialylated glycoproteins. The (→5- O(glycolyl)-Neu5Gcα2→)(n) chains were resistant to exo- and endosialidases from Arthrobacter ureafaciens and bacteriophage K1F, respectively. Discovery of these (→5-O(glycolyl)-Neu5Gcα2→)(n) chains adds a new class of naturally occurring polySia to the structurally diverse family of polysialylated glycoproteins. The structure of a polySia-gp from a different sea urchin species, Strongylocentrotus purpuratus (designated polySia- gp(S)), was also determined to ascertain if there were any species-specific differences. The 500 MHz 1H NMR spectra of the two polySia-gps were identical, indicating that at this level of molecular detail the structures were the same. The molecular weight of polySia-gp(S) was larger, however (250,000), and it contained about 25 polySia chains O-glycosidically linked to both threonine (two-thirds) and serine (one-third) residues.

Original languageEnglish
Pages (from-to)22712-22718
Number of pages7
JournalJournal of Biological Chemistry
Volume269
Issue number36
Publication statusPublished - 1994 Jan 1

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Sea Urchins
Eggs
Glycoproteins
Threonine
polysialic acid
Hemicentrotus
Molecular Weight
Molecular weight
Strongylocentrotus purpuratus
Nuclear magnetic resonance
Arthrobacter
Peptides
Bacteriophages
Fucose
N-Acetylneuraminic Acid
Molecular Structure
Oligosaccharides
Serine
Polysaccharides

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Kitazume, S. ; Kitajima, K. ; Inoue, S. ; Troy, F. A. ; Cho, J. W. ; Lennarz, W. J. ; Inoue, Y. / Identification of polysialic acid-containing glycoprotein in the jelly coat of sea urchin eggs. Occurrence of a novel type of polysialic acid structure. In: Journal of Biological Chemistry. 1994 ; Vol. 269, No. 36. pp. 22712-22718.
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abstract = "Sea urchin eggs are surrounded by a gelatinous layer (called the jelly coat) that consists of mixture of fucose-rich polysaccharides and sialic acid-rich glycoproteins. Chemical and 500 MHz 1H NMR spectroscopic studies revealed for the first time the presence of a novel polysialic acid (polySia) structure in the jelly coat glycoproteins isolated from Hemicentrotus pulcherrimus (designated polySia-gp(H)). The structure of the polySia chains was thoroughly characterized as (→5-O(glycolyl)-Neu5Gcα2→)(n), where n ranges from 4 to more than 40 Neu5Gc residues. The polyNeu5Gc chains were attached to core oligosaccharides that were O-glycosidically linked to threonine residues on a core polypeptide. Each polypeptide contained about 17 O-linked polysialylglycan chains. The apparent molecular weight of polySia- gp(H) was 180,000. The expression of this new polySia structure in place of α2→8-linked polySia is the main structural feature that distinguishes polySia-gp from other known polysialylated glycoproteins. The (→5- O(glycolyl)-Neu5Gcα2→)(n) chains were resistant to exo- and endosialidases from Arthrobacter ureafaciens and bacteriophage K1F, respectively. Discovery of these (→5-O(glycolyl)-Neu5Gcα2→)(n) chains adds a new class of naturally occurring polySia to the structurally diverse family of polysialylated glycoproteins. The structure of a polySia-gp from a different sea urchin species, Strongylocentrotus purpuratus (designated polySia- gp(S)), was also determined to ascertain if there were any species-specific differences. The 500 MHz 1H NMR spectra of the two polySia-gps were identical, indicating that at this level of molecular detail the structures were the same. The molecular weight of polySia-gp(S) was larger, however (250,000), and it contained about 25 polySia chains O-glycosidically linked to both threonine (two-thirds) and serine (one-third) residues.",
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Identification of polysialic acid-containing glycoprotein in the jelly coat of sea urchin eggs. Occurrence of a novel type of polysialic acid structure. / Kitazume, S.; Kitajima, K.; Inoue, S.; Troy, F. A.; Cho, J. W.; Lennarz, W. J.; Inoue, Y.

In: Journal of Biological Chemistry, Vol. 269, No. 36, 01.01.1994, p. 22712-22718.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Identification of polysialic acid-containing glycoprotein in the jelly coat of sea urchin eggs. Occurrence of a novel type of polysialic acid structure

AU - Kitazume, S.

AU - Kitajima, K.

AU - Inoue, S.

AU - Troy, F. A.

AU - Cho, J. W.

AU - Lennarz, W. J.

AU - Inoue, Y.

PY - 1994/1/1

Y1 - 1994/1/1

N2 - Sea urchin eggs are surrounded by a gelatinous layer (called the jelly coat) that consists of mixture of fucose-rich polysaccharides and sialic acid-rich glycoproteins. Chemical and 500 MHz 1H NMR spectroscopic studies revealed for the first time the presence of a novel polysialic acid (polySia) structure in the jelly coat glycoproteins isolated from Hemicentrotus pulcherrimus (designated polySia-gp(H)). The structure of the polySia chains was thoroughly characterized as (→5-O(glycolyl)-Neu5Gcα2→)(n), where n ranges from 4 to more than 40 Neu5Gc residues. The polyNeu5Gc chains were attached to core oligosaccharides that were O-glycosidically linked to threonine residues on a core polypeptide. Each polypeptide contained about 17 O-linked polysialylglycan chains. The apparent molecular weight of polySia- gp(H) was 180,000. The expression of this new polySia structure in place of α2→8-linked polySia is the main structural feature that distinguishes polySia-gp from other known polysialylated glycoproteins. The (→5- O(glycolyl)-Neu5Gcα2→)(n) chains were resistant to exo- and endosialidases from Arthrobacter ureafaciens and bacteriophage K1F, respectively. Discovery of these (→5-O(glycolyl)-Neu5Gcα2→)(n) chains adds a new class of naturally occurring polySia to the structurally diverse family of polysialylated glycoproteins. The structure of a polySia-gp from a different sea urchin species, Strongylocentrotus purpuratus (designated polySia- gp(S)), was also determined to ascertain if there were any species-specific differences. The 500 MHz 1H NMR spectra of the two polySia-gps were identical, indicating that at this level of molecular detail the structures were the same. The molecular weight of polySia-gp(S) was larger, however (250,000), and it contained about 25 polySia chains O-glycosidically linked to both threonine (two-thirds) and serine (one-third) residues.

AB - Sea urchin eggs are surrounded by a gelatinous layer (called the jelly coat) that consists of mixture of fucose-rich polysaccharides and sialic acid-rich glycoproteins. Chemical and 500 MHz 1H NMR spectroscopic studies revealed for the first time the presence of a novel polysialic acid (polySia) structure in the jelly coat glycoproteins isolated from Hemicentrotus pulcherrimus (designated polySia-gp(H)). The structure of the polySia chains was thoroughly characterized as (→5-O(glycolyl)-Neu5Gcα2→)(n), where n ranges from 4 to more than 40 Neu5Gc residues. The polyNeu5Gc chains were attached to core oligosaccharides that were O-glycosidically linked to threonine residues on a core polypeptide. Each polypeptide contained about 17 O-linked polysialylglycan chains. The apparent molecular weight of polySia- gp(H) was 180,000. The expression of this new polySia structure in place of α2→8-linked polySia is the main structural feature that distinguishes polySia-gp from other known polysialylated glycoproteins. The (→5- O(glycolyl)-Neu5Gcα2→)(n) chains were resistant to exo- and endosialidases from Arthrobacter ureafaciens and bacteriophage K1F, respectively. Discovery of these (→5-O(glycolyl)-Neu5Gcα2→)(n) chains adds a new class of naturally occurring polySia to the structurally diverse family of polysialylated glycoproteins. The structure of a polySia-gp from a different sea urchin species, Strongylocentrotus purpuratus (designated polySia- gp(S)), was also determined to ascertain if there were any species-specific differences. The 500 MHz 1H NMR spectra of the two polySia-gps were identical, indicating that at this level of molecular detail the structures were the same. The molecular weight of polySia-gp(S) was larger, however (250,000), and it contained about 25 polySia chains O-glycosidically linked to both threonine (two-thirds) and serine (one-third) residues.

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