Lectin histochemical detection of sulfoglycans in the zona pellucida of mammalian antral oocytes

Citation
F. Parillo et al., Lectin histochemical detection of sulfoglycans in the zona pellucida of mammalian antral oocytes, ACT HISTOCH, 102(2), 2000, pp. 193-202
Citations number
18
Categorie Soggetti
Medical Research Diagnosis & Treatment
Journal title
ACTA HISTOCHEMICA
ISSN journal
00651281 → ACNP
Volume
102
Issue
2
Year of publication
2000
Pages
193 - 202
Database
ISI
SICI code
0065-1281(200005)102:2<193:LHDOSI>2.0.ZU;2-#
Abstract
Sulphated esters are important to increase effectiveness of specific biolog ical activities of carbohydrates. Biochemical studies revealed the presence of distinct sulphated glycoproteins in mammal zona pellucida (ZP) that bin d proacrosin and thus participate in the sperm-egg fusion processes. In the present study, 6 lectin-horseradish peroxidase conjugates (SBA, PNA, RCA-I , GSA-IB4, GSA-II and DBA) were used in combination with desulphation and s ialidase digestion to identify sulphocarbohydrates in the terminal and/or s ubterminal position of oligosaccharide side chains of glycoproteins in the ZP of bovine, ovine, caprine and porcine antral oocytes. In particular, we identified the following terminal sulphoglycans located in the outer layer of the ZP only: SO4-GalNAc in bovine ZP; SO4-Gal beta 1,3GalNAc in bovine a nd ovine ZP; SO4-Gal beta 1,4GlcNAc in bovine, ovine and caprine ZP; SO4-al pha-Gal in bovine, caprine and porcine ZP. Subterminal sulphoglycans linked to sialic acid residues were evenly distributed throughout the entire thic kness of the ZP: Neu5Ac-SO4-Gal beta 1,3GalNAc in bovine and porcine ZP; Ne u5Ac-SO4-Gal beta 1,4GlcNAc in caprine ZP; Neu5Ac-SO4-alpha-Gal in porcine ZP; Neu5Ac-SO4-GlcNAc in bovine ZP. The results demonstrate that the chemic al composition of the ZP differs among species determining the species-spec ificity of gamete interactions.