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A spermatozoon is a motile sperm cell, or moving form of the haploid cell that is the male gamete. A spermatozoon joins an ovum to form a zygote.
Fertilisation or fertilization, also known as generative fertilisation, insemination, pollination, fecundation, syngamy and impregnation, is the fusion of gametes to give rise to a new individual organism or offspring and initiate its development. This cycle of fertilisation and development of new individuals is called sexual reproduction. During double fertilisation in angiosperms the haploid male gamete combines with two haploid polar nuclei to form a triploid primary endosperm nucleus by the process of vegetative fertilisation.
During fertilization, a sperm must first fuse with the plasma membrane and then penetrate the female egg cell in order to fertilize it. Fusing to the egg cell usually causes little problem, whereas penetrating through the egg's hard shell or extracellular matrix can present more of a problem to the sperm. Therefore, sperm cells go through a process known as the acrosome reaction which is the reaction that occurs in the acrosome of the sperm as it approaches the egg. The acrosome is a cap-like structure over the anterior half of the sperm's head.
Transferrins are glycoproteins found in vertebrates which bind to and consequently mediate the transport of Iron (Fe) through blood plasma. It is produced in the liver and contains binding sites for two Fe3+ atoms. Human transferrin is encoded by the TF gene and produced as a 76 kDa glycoprotein.
The zona pellucida is a glycoprotein layer surrounding the plasma membrane of mammalian oocytes. It is a vital constitutive part of the oocyte. The zona pellucida first appears in unilaminar primary oocytes. It is secreted by both the oocyte and the ovarian follicles. The zona pellucida is surrounded by the corona radiata. The corona is composed of cells that care for the egg when it is emitted from the ovary.
Calcium signaling is the use of calcium ions (Ca2+) to communicate and drive intracellular processes often as a step in signal transduction. Ca2+ is important for cellular signalling, for once it enters the cytosol of the cytoplasm it exerts allosteric regulatory effects on many enzymes and proteins. Ca2+ can act in signal transduction resulting from activation of ion channels or as a second messenger caused by indirect signal transduction pathways such as G protein-coupled receptors.
Human fertilization is the union of a human egg and sperm, usually occurring in the ampulla of the fallopian tube. The result of this union is the production of a zygote cell, or fertilized egg, initiating prenatal development. Scientists discovered the dynamics of human fertilization in the nineteenth century.
The cortical reaction is a process initiated during fertilization by the release of cortical granules from the egg, which prevents polyspermy, the fusion of multiple sperm with one egg. In contrast to the fast block of polyspermy which immediately but temporarily blocks additional sperm from fertilizing the egg, the cortical reaction gradually establishes a permanent barrier to sperm entry and functions as the main part of the slow block of polyspermy in many animals.
Major sperm protein (MSP) is a nematode specific small protein of 126 amino acids with a molecular weight of 14 kDa. It is the key player in the motility machinery of nematodes that propels the crawling movement/motility of nematode sperm. It is the most abundant protein present in nematode sperm, comprising 15% of the total protein and more than 40% of the soluble protein. MSP is exclusively synthesized in spermatocytes of the nematodes. The MSP has two main functions in the reproduction of the helminthes: i) as cytosolic component it is responsible for the crawling movement of the mature sperm, and ii) once released, it acts as hormone on the female germ cells, where it triggers oocyte maturation and stimulates the oviduct wall to contract to bring the oocytes into position for fertilization. MSP has first been identified in Caenorhabditis elegans.
The vitelline membrane or vitelline envelope is a structure surrounding the outer surface of the plasma membrane of an ovum or, in some animals, the extracellular yolk and the oolemma. It is composed mostly of protein fibers, with protein receptors needed for sperm binding which, in turn, are bound to sperm plasma membrane receptors. The species-specificity between these receptors contributes to prevention of breeding between different species. It is called zona pellucida in mammals.
Activin receptor type-2B is a protein that in humans is encoded by the ACVR2B gene. ACVR2B is an activin type 2 receptor.
Type II topoisomerases cut both strands of the DNA helix simultaneously in order to manage DNA tangles and supercoils. They use the hydrolysis of ATP, unlike Type I topoisomerase. In this process, these enzymes change the linking number of circular DNA by ±2.
Zona pellucida sperm-binding protein 3, also known as zona pellucida glycoprotein 3 (Zp-3) or the sperm receptor, is a ZP module-containing protein that in humans is encoded by the ZP3 gene. ZP3 is the receptor in the zona pellucida which binds sperm at the beginning of fertilization.
Sperm surface protein Sp17 is a protein that in humans is encoded by the SPA17 gene.
Zona pellucida sperm-binding protein 2 is a protein that in humans is encoded by the ZP2 gene.
Sperm chemotaxis is a form of sperm guidance, in which sperm cells (spermatozoa) follow a concentration gradient of a chemoattractant secreted from the oocyte and thereby reach the oocyte.
The Zona pellucida-like domain is a large protein region of about 260 amino acids. It has been recognised in a variety of receptor-like eukaryotic glycoproteins. All of these molecules are mosaic proteins with a large extracellular region composed of various domains, often followed by either a transmembrane region and a very short cytoplasmic region or by a GPI-anchor.
Oocyteactivation is a series of processes that occur in the oocyte during fertilization.
Juno also known as folate receptor 4, folate receptor delta or IZUMO1R is a protein that in humans is encoded by the FOLR4 gene. Juno is a member of the folate receptor family and is GPI-anchored to the plasmalemma of the mammalian egg cell that recognizes its sperm-riding counterpart, IZUMO1, and facilitates fertilization. The protein was named after Juno, the Roman goddess of fertility and marriage.
Egg jelly(extracellular layer, jelly coat) is a gelatinous layer that surrounds the oocytes of many organisms and releases species-specific chemoattractants that activate and guide sperm to the oocyte. The egg jelly is located immediately surrounding the vitelline envelope and consists primarily of a network of short peptides and sulfated fucan glycoproteins. These short peptides diffuse into the surrounding area and stimulate respiration and movement of the sperm to the egg. An example of such a peptide is resact which has been studied as the primary means of attracting and orientating sperm to the eggs in sea urchins. The sulfated fucan glycoproteins play an important role in binding to sperm receptors and triggering the acrosomal reaction.
References
- ↑ Stout CD, Vacquier VD, Kresge N (2000). "1.35 and 2.07 A resolution structures of the red abalone sperm lysin monomer and dimer reveal features involved in receptor binding". Acta Crystallogr. D. 56 (Pt 1): 34–41. doi:10.1107/s0907444999014626. PMID 10666624.
- ↑ Stout CD, Vacquier VD, Kresge N (2000). "The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of the egg receptor". J. Mol. Biol. 296 (5): 1225–1234. doi:10.1006/jmbi.2000.3533. PMID 10698629.
- ↑ Stout CD, Vacquier VD, Kresge N (2001). "The crystal structure of a fusagenic sperm protein reveals extreme surface properties". Biochemistry. 40 (18): 5407–5413. doi:10.1021/bi002779v. PMID 11331004.
- ↑ Raj I, Sadat Al Hosseini H, Dioguardi E, Nishimura K, Han L, Villa A, de Sanctis D, Jovine L (2017). "Structural Basis of Egg Coat-Sperm Recognition at Fertilization". Cell. 169 (7): 1315–1326. doi:10.1016/j.cell.2017.05.033. PMC 5480393 . PMID 28622512. PDB: 5MR3, 5IIA, 5IIB