PMID- 10504403
OWN - NLM
STAT- MEDLINE
DCOM- 19991122
LR  - 20190620
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 265
IP  - 2
DP  - 1999 Oct
TI  - Structural characterization of the oligosaccharide chains of native and
      crystallized boar seminal plasma spermadhesin PSP-I and PSP-II glycoforms.
PG  - 703-18
AB  - The PSP-I/PSP-II heterodimer is the major protein of boar seminal plasma. Both
      subunits are glycoproteins of the spermadhesin family and each contains a single 
      N-glycosylation site. After enzymatic release of the oligosaccharides from
      isolated PSP-I and PSP-II, mainly neutral and monosialylated oligosaccharides,
      and small amounts of disialylated oligosaccharides, were recovered from both
      proteins. Twenty-two neutral oligosaccharides, 11 monosialylated glycans and
      three disialylated carbohydrate chains were characterized using mass
      spectrometric and NMR techniques. PSP-I and PSP-II share the same glycans but
      differ in their relative molar ratios. Most glycan structures are proximally
      alpha1-6-fucosylated, diantennary complex-type bearing nonsialylated or
      alpha2-6-sialylated N-acetyllactosamine or di-N-acetyllactosamine antennae. The
      majority of nonsialylated N-acetyllactosamine antennae bear terminal
      alpha1-3-linked Gal residues. In addition, the N-acetylglucosamine residue of
      nonsialylated N-acetyl and di-N-acetyllactosamine antennae can be modified by an 
      alpha1-3-linked fucose residue. Structures of higher antennarity, as well as
      structures 3,6-branched at galactose residues, were found in smaller amounts. In 
      one oligosaccharide, N-acetylneuraminic acid is substituted by
      N-glycolylneuraminic acid. Mass spectrometric analysis of PSP-I and PSP-II
      glycoforms isolated from crystallized PSP-I/PSP-II heterodimer showed the
      coexistence of major PSP-I and PSP-II glycoforms in the hexagonal crystals.
      Oligosaccharides with the NeuNAcalpha2-6GalNAcbeta1-4GlcNAc-R motif block
      adhesive and activation-related events mediated by CD22, suggesting a possible
      immunoregulatory activity for PSP-I/PSP-II.
FAU - Nimtz, M
AU  - Nimtz M
AD  - Gesellschaft fur Biotechnologische Forschung (GBF) mbH, Braunschweig, Germany.
FAU - Grabenhorst, E
AU  - Grabenhorst E
FAU - Conradt, H S
AU  - Conradt HS
FAU - Sanz, L
AU  - Sanz L
FAU - Calvete, J J
AU  - Calvete JJ
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 (Glycoproteins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Seminal Vesicle Secretory Proteins)
RN  - 0 (seminal vesicle secretory protein II, porcine)
RN  - 147258-06-8 (seminal vesicle secretory protein 109, porcine)
SB  - IM
MH  - Animals
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Dimerization
MH  - Glycoproteins/*chemistry
MH  - Glycosylation
MH  - Magnetic Resonance Spectroscopy
MH  - Male
MH  - Methylation
MH  - Molecular Sequence Data
MH  - Oligosaccharides/*chemistry
MH  - Semen/chemistry
MH  - *Seminal Vesicle Secretory Proteins
MH  - Sequence Analysis
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Swine
EDAT- 1999/10/03 00:00
MHDA- 1999/10/03 00:01
CRDT- 1999/10/03 00:00
PHST- 1999/10/03 00:00 [pubmed]
PHST- 1999/10/03 00:01 [medline]
PHST- 1999/10/03 00:00 [entrez]
AID - ejb766 [pii]
AID - 10.1046/j.1432-1327.1999.00766.x [doi]
PST - ppublish
SO  - Eur J Biochem. 1999 Oct;265(2):703-18. doi: 10.1046/j.1432-1327.1999.00766.x.