Characterization of glycoside residues of porcine zona pellucida and ooplasm during follicular development and atresia

Abstract

The glycoside residues (glycoconjugates, GC) of the zona pellucida (ZP) glycoproteins are important during the first phases of fecundation. Our aim in this work was to determine the lectin affinity pattern of porcine ZP in order to analyze the changes that take place during: (a) preantral folliculogenesis, (b) the follicular atresia process, and (c) antral growth. Several prepubertal and adult pig ovaries and different sized antral follicles were used. Conventional carbohydrate histochemical techniques and peroxidase and digoxigenin (DIG) lectins were used to reveal the acid groups and the glycosidic residues of the ZP. It was seen that the ZP forms in the preantral follicles throughout their growth period. In primordial and primary follicles, ZP in the process of formation showed neutral GC. SBA, RCA-I, MAA, WGA lectins, and AAA after methylation-saponification (MS) were positive in the ZP of primordial and primary follicles. The affinity for SBA, RCA-I, MAA, and WGA increased in the multilaminar-primary follicles and new affinities for UEA-I and LFA were observed. After MS, AAA, SNA, PNA, and SBA reactivity was observed. The ZP of antral follicle oocytes of different sizes showed the same lectin pattern as multilaminar-primary follicles. The oocyte ooplasm and the follicular fluid of large antral follicles showed less affinity for WGA and LFA lectins and less intensive staining with AB (pH 2.5). Atresia did not change the antral or preantral follicle oocyte ZP lectin pattern. In conclusion, the follicles showed substantial changes in their ZP glycosidic composition as they developed, especially, during the change from primary to multilaminar-primary follicles. The ZP glycosidic composition showed no significant change during the growth of antral follicles and follicular atresia in our study.

Relationship between motile sperm subpopulations identified in frozen‐thawed dog semen samples and their ability to bind to the zona pellucida of canine oocytes

“…Oocytes released from the canine ovarian cortex constitute a heterogeneous population that includes oocytes proceeding from viable follicles (mainly preantral) at different developmental stages and from atretic follicles. In other species, the three‐dimensional structure of the zona pellucida and its carbohydrate composition has been observed to change during follicular growth and atresia (Calafell, Nogués, Ponsá, Santaló, & Egozcue, ; Familiari, Nottola, Familiari, & Motta, ; Pastor et al., ). In this study, oocyte heterogeneity was expected to cause a high variability in sperm binding capacity.…”

α-L-fucosidase enhances capacitation-associated events in porcine spermatozoa

“…Fucose has been detected in the porcine ZP using Ulex europaeus agglutinin 1 (UEA-I) lectin histochemistry (Song et al, 1999;Pastor et al, Pattern A showed significant differences, with higher values observed in the control group (54.7 ± 1.6%) than in the TALP (15.1 ± 1.2%) and TALP + E (12.2 ± 1.1%) groups (P < 0.001); pattern B showed higher values in the TALP group (61.8 ± 1.6%) than in the TALP + E (35.2 ± 1.6%) and control (43.2 ± 1.6%) groups (P < 0.01); pattern C showed significant differences (P < 0.001), with maximum values observed in the TALP + E group (52.5 ± 1.7%) compared with the TALP (23.1 ± 1.4%) and control (2.1 ± 0.5%) groups. Different letters indicate significant differences.…”

Identification of Apoptotic Cells by Means of Lectin Histochemistry: State of the Art Review

“…Their molecular structure, carbohydrate-binding properties and biological activities have been covered in detail in several reviews [18][19][20][21][22][23][24][25]. These proteins have been widely used for the detection of carbohydrate in various tissues and organs, e.g., the respiratory system [26][27][28][29], digestive system [30][31][32], and male [33][34][35][36][37] and female [38][39][40] reproductive systems, and in diverse pathological situations [41]. The use of lectins for the histochemical detection of glycans in tissue sections (lectin histochemistry) is an area of important applications for these molecules.…”