Structure of the O‐linked carbohydrate chains of porcine zona pellucida glycoproteins

Hokke, Cornelis H.; Damm, Jan B. L.; Penninkhof, Bea; Aitken, R. John; Kamerling, Johannis P.; Vliegenthart, Johannes F.G.

doi:10.1111/j.1432-1033.1994.tb18762.x

Cited by 91 publications

(48 citation statements)

References 37 publications

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“…Thus, it seems likely that the structural features of carbohydrate chains recognized by sperm proteins differ at least between mouse and pig. Since pig zona pellucida can be obtained relatively easy in sufficient quantities, structural analyses of pig zona pellucida carbohydrate chains have been largely completed [16,[22][23][24][25][26]. Therefore, in pig, studies on the sperm receptor site of zona pellucida can be interpreted on the basis of the structures of carbohydrate chains to characterize further the mechanism of gamete recognition.…”

Section: Discussionmentioning

confidence: 99%

Involvement of N‐Linked Carbohydrate Chains of Pig Zona Pellucida in Sperm‐Egg Binding

Yonezawa

Aoki

Hatanaka

et al. 1995

European Journal of Biochemistry

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The sperm receptor activity of pig zona pellucida has been previously shown to exist in one of the components, pig zona protein 3n (PZP3n), that can be purified after the removal of sialylated and/or sulfated N-acetylpoly(1actosamine) by digestion with endo-P-galactosidase. In this study, we examined whether N-linked or 0-linked carbohydrate chains are involved in the sperm receptor activity of pig zona pellucida. The elimination of N-linked carbohydrate chains from endo-a-galactosidase-digested PZP3a by digestion with N-glycanase markedly reduced its inhibitory effect on sperm-egg binding in an in vitro competition assay, whereas the elimination of 0-linked carbohydrate chains by alkali treatment hardly reduced the inhibitory effect. These results indicate that N-linked carbohydrate chains of PZP3a play a major role in mediating the sperm binding of zona pellucida in pig.Keywords: zona pellucida; N-linked carbohydrate chains; N-glycanase; sperm-egg binding.The zona pellucida, which surrounds mammalian oocytes, consists of 3-4 glycoproteins and plays an important role in species-specific gamete recognition and the blocking of polyspermy after fertilization [I, 21. Pig zona pellucida consists of three glycoproteins: pig zona protein 1 (PZPI ; 90-kDa glycoprotein composed of disulfide-bonded 65-kDa and 25-kDa polypeptides 13, 41); pig zona protein 3n (PZP3a; 55 kDa); pig zona protein 3P (PZP3p; 55 kDa). PZP3a and PZP3p copurify in the pig zona protein 3 (PZP3) fraction during gel-filtration HPLC [5, 61. The separation of PZP3a and PZP3p is only successful after the removal of sialylated and/or sulfated N-acetylpoly(1ac-tosamine) by digestion with endo-j-galactosidase 16, 71. We refer to the purified PZP3a and PZP3p as endo-p-galactosidasedigested PZP3a (EPG-PZP3a; 46 kDa) and endo-p-galactosidase-digested PZP3P (EpG-PZP3B; 42 kDa), respectively. The major component, PZP3, inhibited sperm-egg binding in an in vitro competition assay and E,b'G-PZP3a retained the inhibitory activity [8]. EpG-PZP3P showed no inhibition in this assay [ S ] . It has been reported that the minor component PZPl has also a small but significant inhibitory effect on sperm-egg binding in an in vitro competition assay 191. Using the fluorescein-labelled components of pig zona pellucida, the binding of PZP3 and EPG-PZP3a to boar sperm has been observed, but the binding of PZPl to boar sperm has not been detected [lo]. PZPl did not effectively inhibit the binding of biotinylated PZP3 to sperm membrane [ l 11. Thus, PZP3a may play a major role in sperm- egg binding and we have focused on the involvement of EPGPZP3a in sperm-egg binding in this study.Since the chemical deglycosylation of PZP3 with trifluoromethane sulfonate abolished its sperm receptor activity 18, 91, it is suggested that the sperm receptor activity depends upon the carbohydrate component of PZP3. The involvement of carbohydrates of zona pellucida in sperm-egg recognition has been well examined in mouse. It has been reported that the sperm receptor activity of mouse ZP3 (83 kDa...

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Section: Discussionmentioning

confidence: 99%

Involvement of N‐Linked Carbohydrate Chains of Pig Zona Pellucida in Sperm‐Egg Binding

Yonezawa

Aoki

Hatanaka

et al. 1995

European Journal of Biochemistry

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“…The spectrum showed two ,!-anomeric proton resonances at 4.59 ppm and 4.51 ppm. The resonance at 4.51 ppm was assignable to HI of the penultimate ,!-Gal residue if we considered that (a) the resonance of H1 (4.52 ppm) of the P-Gal residue in the GalPl-4(HSO,-6)GlcNAc,!l-+ structure was downfield shifted by 0.04 ppm compared to that (4.48 ppm) of Gal~l-4GlcNAc~l-sequence [42] and (b) the resonance of H1 of the penultimate P-Gal residue in the Gal~l-4Gal~l-4(2,5)-anhMan-o1 structure was known to appear at 4.47 ppm [43]. Moreover, it is noteworthy that the GalPl-4(HS03-6)(2,5)-anhMan-ol sequence [44].…”

Section: Fab-ms Analysis Of the Intact Glycan Units Derived From Hyosmentioning

confidence: 99%

Occurrence and Structural Analysis of Highly Sulfated Multiantennary N‐linked Glycan Chains Derived from a Fertilization‐Associated Carbohydrate‐Rich Glycoprotein in Unfertilized Eggs of Tribolodon hakonensis

Taguchi

Iwasaki

Muto

et al. 1996

European Journal of Biochemistry

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This study represents the first detailed investigation of the nature of highly sulfated (keratan-sulfatelike) complex-type asparagine-linked glycans having a tetraantennary core structure and shows the effectiveness of fast-atom-bombardment mass spectrometric (FAB-MS) methods incorporating derivatization and mild methanolysis for analyzing such complex types of sulfated glycans.The structure of the N-glycan chains was unambiguously established by a combination of compositional analysis, methylation analysis, mild methanolysis for desulfation, hydrazinolysis/nitrous acid deamination, enzymatic (endo-P-galactosidase and peptide : N-gl ycosidase F) digestions, and instrumental analyses ('H-NMR spectroscopy and FAB-MS) which revealed the novel repeating sulfated carbohydrate sequences, 2 GalPl +4Gal,81[+4(HS03~6)GlcNAc~1-+3( -C GalPl--+4)Gal~l],-+ (see Structure I; p+q+r+s-14). This sequence is unique in: (a) the skeletal structure is similar to that of keratan sulfate but is completely devoid of 6-0-sulfated Gal residues and (b) the presence of branched Gal residues in the sequence -+4GlcNAc~1+3(Gal,81-4)GulPl+. +SO;b6+.Gav-l14 +SO,-b6 Abbreviations. FAB, fast atom bombardment; NeuSAc, N-acetylneuraminic acid; (2,5)-anhMan-ol, 2,5-anhydro-o-mannitol; Gal-ol, D-galactitol ; anhHex-ol, anhydro hexitol ; lD, one-dimensional ; 2D, two-dimensional.Enzymes. Endo-,8-galactosidase (EC 3.2.1.103); peptide:N-glycosidase F (EC 3.5.1.52). The oligosaccharide chains of keratan sulfate are bound to protein either by an N-glycosidic linkage (type I, as found in cornea) [21-241 or an 0-glycosidic linkage (type 11, associated with skin, cartilage, and bone) [25]. In the type I keratan sulfate derived from cornea, the core structures are restricted to diantennary [22-241. The existence of tri-or tetra-antennary complextype core structures carrying glycosaminoglycan chains has been reported in some mammalian cells [ I41 and virus-transformed baby hamster kidney cells [26], but these reports were mostly based on the results of Iectin-affinity chromatography using radioisotopes and the complete structures of these N-linked glycans have not yet been precisely determined.

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“…Porcine ZP3 comprises both O-and N-linked glycans, of which only O-glycans are important in sperm egg interactions including AR (26). These glycans are highly sulfated and also sialylated.…”

Section: Egg Coat Glycans In Vertebratesmentioning

confidence: 99%

Modifications of Acrosome Reaction-Inducing Egg Coat Glycans

Gunaratne¹

2007

TIGG

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The exocytotic acrosome reaction (AR) is a mandatory step in sperm-egg interactions in most metazoans. The molecules present in egg coats play crucial roles in AR induction. These signaling molecules are mainly complex carbohydrates, which are either protein-bound or -free. The structural elucidation of these glycans is in progress. The new knowledge gained should lead to new insights into the molecular mechanisms of AR induction. The modifications of the AR-inducing glycans involve O-glycosylation, fucosylation, sulfation and sialylation. These modifications are conserved from the lowest deuterostomes to the highest vertebrates. The evidence suggests that the AR is mediated by a carbohydrate-protein interaction. Here the primary structures and important features of these AR inducing carbohydrates present in both invertebrate and vertebrate egg coats are reviewed.

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Structure of the O‐linked carbohydrate chains of porcine zona pellucida glycoproteins

Cited by 91 publications

References 37 publications

Involvement of N‐Linked Carbohydrate Chains of Pig Zona Pellucida in Sperm‐Egg Binding

Involvement of N‐Linked Carbohydrate Chains of Pig Zona Pellucida in Sperm‐Egg Binding

Occurrence and Structural Analysis of Highly Sulfated Multiantennary N‐linked Glycan Chains Derived from a Fertilization‐Associated Carbohydrate‐Rich Glycoprotein in Unfertilized Eggs of Tribolodon hakonensis

Modifications of Acrosome Reaction-Inducing Egg Coat Glycans

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