Protein-Carbohydrate Interaction between Sperm and the Egg-Coating Envelope and Its Regulation by Dicalcin, a Xenopus laevis Zona Pellucida Protein-Associated Protein

Abstract

Protein-carbohydrate interaction regulates multiple important processes during fertilization, an essential biological event where individual gametes undergo intercellular recognition to fuse and generate a zygote. In the mammalian female reproductive tract, sperm temporarily adhere to the oviductal epithelium via the complementary interaction between carbohydrate-binding proteins on the sperm membrane and carbohydrates on the oviductal cells. After detachment from the oviductal epithelium at the appropriate time point following ovulation, sperm migrate and occasionally bind to the extracellular matrix, called the zona pellucida (ZP), which surrounds the egg, thereafter undergoing the exocytotic acrosomal reaction to penetrate the envelope and to reach the egg plasma membrane. This sperm-ZP interaction also involves the direct interaction between sperm carbohydrate-binding proteins and carbohydrates within the ZP, most of which have been conserved across divergent species from mammals to amphibians and echinoderms. This review focuses on the carbohydrate-mediated interaction of sperm with the female reproductive tract, mainly the interaction between sperm and the ZP, and introduces the fertilization-suppressive action of dicalcin, a Xenopus laevis ZP protein-associated protein.The action of dicalcin correlates significantly with a dicalcin-dependent change in the lectin-staining pattern within the ZP, suggesting a unique role of dicalcin as an inherent protein that is capable of regulating the affinity between the lectin and oligosaccharides attached on its target glycoprotein.

The Catsper channel and its roles in male fertility: a systematic review

“…The ZP protein surrounding the oocyte is important in the fertilization process, because only when sperm pass through the ZP protein to complete the acrosome reaction can participate in fertilization. In fact, ZP glycoproteins consist of three subunits in mice: ZP1, ZP2 and ZP3 [ 63 , 64 ]. Whereas four subunits-ZP1, ZP2, ZP3 and ZP4 exist in human sperm [ 65 ].…”

“…In recent years, studies have found that the Catsper channel plays a critical role in ZP-induced Ca 2+ entry into mouse sperm. Using patch-clamp techniques, Ca 2+ currents after 2 min of ZP stimulation were undetectable in Catsper1-null mouse sperm, showing that the Catsper channel is necessary for ZP to induce [Ca 2+ ]i increases and suggesting that the ZP-induced [Ca 2+ ]i increases start from sperm tails and propagate toward the sperm heads [ 64 ].…”

Criopreservación espermática de Ambystoma mexicanum (Shaw & Nodder, 1798)

“…Cada preparación se observó directamente en un microscopio de fluorescencia a 260 nm de excitación y >560 nm emisión, contabilizando 100 espermatozoides. Se determinó la presencia de los carbohidratos membranales, mediante patrones de fluorescencia y la proporción de espermatozoides con cada patrón determinado (Naofumi, 2015).…”

Profiling N-glycans of the egg jelly coat of the sea urchinParacentrotus lividusby MALDI-TOF mass spectrometry and capillary liquid chromatography electrospray ionization-ion trap tandem mass spectrometry systems

“…Animal eggs are surrounded by an extracellular material called zona pellucida in mammals, vitelline envelope, or jelly coat in non‐mammals, and chorion in fish (Miwa, ; Shu, Suter, & Rasanen, ). Each of these egg coats is enriched with glycoproteins.…”