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 language | English |
|---|---|
| Pages (from-to) | 22712-22718 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 269 |
| Issue number | 36 |
| Publication status | Published - 1994 Jan 1 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
}
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 journal › Article
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.
UR - http://www.scopus.com/inward/record.url?scp=0027989902&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027989902&partnerID=8YFLogxK
M3 - Article
C2 - 8077223
AN - SCOPUS:0027989902
VL - 269
SP - 22712
EP - 22718
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 36
ER -