PMID- 10091584
OWN - NLM
STAT- MEDLINE
DCOM- 19990422
LR  - 20190620
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 260
IP  - 1
DP  - 1999 Feb
TI  - Localization of neutral N-linked carbohydrate chains in pig zona pellucida
      glycoprotein ZPC.
PG  - 57-63
AB  - Zona pellucida, a transparent envelope surrounding the mammalian oocyte, plays
      important roles in fertilization and consists of three glycoproteins; ZPA, ZPB
      and ZPC. In pig, neutral complex-type N-linked chains obtained from a ZPB/ZPC
      mixture possess sperm-binding activity. We have recently reported that among
      neutral N-linked chains triantennary and tetraantennary chains have a
      sperm-binding activity stronger than that of diantennary chains. Triantennary and
      tetraantennary chains are localized at the second of the three N-glycosylation
      sites of ZPB. In this study, we focused on the localization of neutral N-linked
      chains in ZPC. ZPB and ZPC can not be separated from each other unless the acidic
      N-acetyllactosamine regions of their carbohydrate chains are removed by
      endo-beta-galactosidase digestion. A large part of the acidic N-linked chains
      becomes neutral by the digestion, but the main neutral N-linked chains are not
      susceptible to the enzyme. N-glycanase digestion indicated that ZPC has three
      N-glycosylation sites. Three glycopeptides each containing one of the
      N-glycosylation sites were obtained by tryptic digestion of ZPC and the
      N-glycosylation sites were revealed as Asn124, Asn146 and Asn271. The
      carbohydrate structures of the neutral N-linked chains from each glycopeptide
      were characterized by two-dimensional sugar mapping analysis taking into
      consideration the structures of the main, intact neutral N-linked chains of
      ZPB/ZPC mixture reported previously. Triantennary and tetraantennary chains were 
      found mainly at Asn271 of ZPC, whereas diantennary chains were present at all
      three N-glycosylation sites. Thus, ZPC has tri-antennary and tetra-antennary
      chains as well as ZPB, but the localization of the chains is different from that 
      in ZPB.
FAU - Yonezawa, N
AU  - Yonezawa N
AD  - Graduate School of Science and Technology, Chiba University, Japan.
FAU - Fukui, N
AU  - Fukui N
FAU - Kudo, K
AU  - Kudo K
FAU - Nakano, M
AU  - Nakano M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 0 (Egg Proteins)
RN  - 0 (Glycopeptides)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Zona Pellucida Glycoproteins)
RN  - EC 3.2.1.- (Glycoside Hydrolases)
RN  - EC 3.2.1.103 (keratan-sulfate endo-1,4-beta-galactosidase)
RN  - EC 3.2.1.23 (beta-Galactosidase)
RN  - EC 3.4.21.4 (Trypsin)
RN  - EC 3.5.- (Amidohydrolases)
RN  - EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase)
SB  - IM
MH  - Amidohydrolases/metabolism
MH  - Animals
MH  - Carbohydrate Sequence
MH  - Egg Proteins/*chemistry
MH  - Female
MH  - Glycopeptides/chemistry
MH  - *Glycoside Hydrolases
MH  - Glycosylation
MH  - Membrane Glycoproteins/*chemistry
MH  - Molecular Sequence Data
MH  - Oligosaccharides/chemistry
MH  - Oocytes/chemistry
MH  - Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
MH  - *Receptors, Cell Surface
MH  - Swine
MH  - Trypsin/metabolism
MH  - Zona Pellucida/*chemistry
MH  - Zona Pellucida Glycoproteins
MH  - beta-Galactosidase/metabolism
EDAT- 1999/03/26 00:00
MHDA- 1999/03/26 00:01
CRDT- 1999/03/26 00:00
PHST- 1999/03/26 00:00 [pubmed]
PHST- 1999/03/26 00:01 [medline]
PHST- 1999/03/26 00:00 [entrez]
AID - 10.1046/j.1432-1327.1999.00095.x [doi]
PST - ppublish
SO  - Eur J Biochem. 1999 Feb;260(1):57-63. doi: 10.1046/j.1432-1327.1999.00095.x.