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Titolo:
Structural characterization of the oligosaccharide chains of native and crystallized boar seminal plasma spermadhesin PSP-I and PSP-II glycoforms
Autore:
Nimtz, M; Grabenhorst, E; Conradt, H; Sanz, L; Calvete, JJ;
Indirizzi:
CSIC, Inst Biomed Valencia, E-46010 Valencia, Spain CSIC Valencia Spain E-46010 nst Biomed Valencia, E-46010 Valencia, Spain Gesell Biotechnol Forsch GmbH, D-3300 Braunschweig, Germany Gesell Biotechnol Forsch GmbH Braunschweig Germany D-3300 hweig, Germany
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 2, volume: 265, anno: 1999,
pagine: 703 - 718
SICI:
0014-2956(199910)265:2<703:SCOTOC>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
PELLUCIDA BINDING CHARACTERISTICS; N-LINKED OLIGOSACCHARIDES; ZONA-PELLUCIDA; CUB DOMAIN; MAJOR PROTEINS; I/PSP-II; GLYCOPROTEIN; HETERODIMER; FAMILY; AWN-1;
Keywords:
mass spectrometry; N-glycosylation; oligosaccharide structure; seminal plasma proteins; spermadhesin PSP-I/ PSP-II;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Calvete, JJ CSIC, Inst Biomed Valencia, C Jaime Roig 11, E-46010 Valencia,Spain CSIC C Jaime Roig 11 Valencia Spain E-46010 0 Valencia, Spain
Citazione:
M. Nimtz et al., "Structural characterization of the oligosaccharide chains of native and crystallized boar seminal plasma spermadhesin PSP-I and PSP-II glycoforms", EUR J BIOCH, 265(2), 1999, pp. 703-718

Abstract

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-TI, 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 alpha 1-6-fucosylated, diantennary complex-type bearing nonsialylated or alpha 2-6-sialylated N-acetyllactosamine or di-N-acetyllactosamine antennae. The majority of nonsialylated N-acetyllactosamine antennae bear terminal alpha 1-3-linked Gal residues. In addition, the N-acetylglucosamine residue of nonsialylated N-acetyl and di-N-acetyllactosamine antennae can be modified by an alpha 1-3-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 NeuNAc alpha 2-6GalNAc beta 1-4GlcNAc-R motif block adhesive and activation-related events mediated by CD22, suggesting a possible immunoregulatory activity for PSP-I/PSP-II.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 15:16:53