Calcium dependence of the acrosome reaction and activation of guinea pig spermatozoa

Yanagimachi, Ryuzo; Usui, Noriko

doi:10.1016/0014-4827(74)90199-2

Cited by 555 publications

(257 citation statements)

References 37 publications

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“…The propagation of a Ca 2+ -induced wave produced from the opening of Ca 2+ channels along the flagella is a necessary milestone in sperm maturation and makes hyperactivated motility possible [4,54,55]. Additionally, [Ca 2+ ] i plays a pivotal role in acrosome exocytosis [56][57][58][59][60]. Specific ion channels mediate the rise in [Ca 2+ ] i within sperm, and many candidates for the principle Ca 2+ channel in sperm, including various voltagegated Ca 2+ channels, were proposed based primarily on studies using Ca 2+ imaging, immunolabeling, and patch-clamp experiments from sperm precursors [61][62][63].…”

Section: Calcium Channels and Hyperactivationmentioning

confidence: 99%

Flagellar ion channels of sperm: similarities and differences between species

et al. 2015

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a b s t r a c tMotility and fertilization potential of mammalian sperm are regulated by ion homeostasis which in turn is under tight control of ion channels and transporters. Sperm intracellular pH, membrane voltage and calcium concentration ([Ca 2+ ] i ) are all important for sperm activity within the female reproductive tract. While all mammalian sperm are united in their goal to find and fertilize an egg, the molecular mechanisms they utilize for this purpose are diverse and differ between species especially on the level of ion channels. Recent direct recording from sperm cells of different species indicate the differences between rodent, non-human primate, ruminant, and human sperm on the basic levels of their ion channel regulation. In this review we summarize the current knowledge about ion channel diversity of the animal kingdom and concentrate our attention on flagellar ion channels of mammalian sperm.

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Section: Calcium Channels and Hyperactivationmentioning

confidence: 99%

Flagellar ion channels of sperm: similarities and differences between species

et al. 2015

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“…In sea urchins, an egg jelly fucose sulfate glycoconjugate induces acrosome reactions in sperm (SeGall and Lennarz, 1979). The acrosome is a membrane-bound caplike structure, analogous to a lysosome or a zymogen granule, which overlies the anterior portion of the sperm nucleus and whose contents are released in a calcium-dependent, exocytotic event (Dan, 1954;Yanagimachi and Usui, 1974). Following the acrosome reaction, an acrosomal filament is exposed which is coated with the adhesive protein bindin (Vacquier and Moy, 1977).…”

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confidence: 99%

Carbohydrates and fertilization in animals

Miller

1990

Molecular Reproduction Devel

119

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A frequently used mechanism for sperrn-egg recognition in many species involves complementary protein-carbohydrate interaction. The usual paradigm includes complex glycoconjugates in reproductive tract fluids or on the eggs which are recognized by carbohydratebinding proteins on the sperm surface. Various glycoconjugates are utilized in the steps of sperm capacitation, sperm binding to the egg extracellular matrix and vitelline membrane and induction of the acrosome reaction. Several types of complex glycoconjugates are involved in these processes, including proteoglycans, lactosaminoglycans, sulfated fucose-containing glycoconiugates, and glycoproteins. There appear to be some structural similarities between active glycoconjugates; they are large in molecular weight and complex, and they are often sulfated, fucosylated, and attached to a protein through serine or threonine residues. In some species, the protein core of the glycoconjugates also participates in the interaction by limiting the binding of carbohydrates to sperm only of the relevant species, likely by providing the proper steric arrangement for the interaction. In other cases the protein core seems to serve more as a crosslinker of the carbohydrate moieties. This review discusses the types of glycoconjugates implicated in fertilization and the complementary lectinlike proteins found on sperm.Key Words: Sperm, Eggs, Glycosaminoglycans, Glycoconjugates, Glycoproteins, Zona pellucida, Capacitation, Acrosorne reaction, Fertilization cess differ between species, there is remarkable conservation in the ability of sperm to use glycoconjugates in reproductive tract secretions or in the egg extracellular matrix and vitelline membrane for fertilization-related events. This review summarizes research from various animals in which glycoconjugates are important in sperm-egg interaction. It contrasts differences between species at the point of the fertilization process where carbohydrates interact with sperm. Furthermore, a structural comparison between each of the carbohydrates is presented.An understanding of fertilization-related events is necessary prior to a discussion of the potential molecules involved in sperm-egg interaction. There are differences between species in the events occurring both before and during sperm-egg interaction. These events are best understood in sea urchins and mice, although there is recent information from other species. A diagram of sperm-egg interaction in sea urchins is shown in Figure

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“…The mechanism of Ca 2÷ uptake in spermatozoa is not yet clearly understood. Ca 2÷ is, however, known to influence functions associated with ejaculated spermatozoa such as motility, acrosome reaction and fertilizing ability [12,13]. Further studies on the effect of SPLN on the binding of Ca 2+ to the surface of intact spermatozoa and on the translocation of Ca 2+ into the sperm cell may reveal the mechanism by which SPLN inhibits the uptake of Ca 2+ in bovine spermatozoa [11].…”

Section: Resultsmentioning

confidence: 99%

“…SPLN also inhibits the uptake of Ca 2÷ in bovine spermatozoa [11]. Ca 2÷ is known to influence the motility, acrosome reaction and fertilising ability of spermatozoa [12,13]. Hence, studies directed towards understanding the mechanism by which SPLN inhibits Ca 2÷ uptake would be important.…”

Section: Introductionmentioning

confidence: 99%

Interaction of seminalplasmin with chlortetracycline, a fluorescent chelate probe of Ca²⁺

Shivaji

1987

FEBS Letters

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The interaction of seminalplasmin with chlortetracycline, a fluorescent chelate probe of Ca 2+, was studied. The results indicate that seminalplasmin binds to chlortetracycline. The binding is not influenced by salt. Both Ca 2+ and seminalplasmin probably bind to the same site on chlortetracycline. Seminalplasmin also reduced the Tb3+-associated fluorescence of bovine spermatozoal plasma membrane. These results are discussed in relation to the inhibitory effect of seminalplasmin on the uptake of Ca 2+ in bovine spermatozoa.

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Calcium dependence of the acrosome reaction and activation of guinea pig spermatozoa

Cited by 555 publications

References 37 publications

Flagellar ion channels of sperm: similarities and differences between species

Flagellar ion channels of sperm: similarities and differences between species

Carbohydrates and fertilization in animals

Interaction of seminalplasmin with chlortetracycline, a fluorescent chelate probe of Ca²⁺

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Calcium dependence of the acrosome reaction and activation of guinea pig spermatozoa

Cited by 555 publications

References 37 publications

Flagellar ion channels of sperm: similarities and differences between species

Flagellar ion channels of sperm: similarities and differences between species

Carbohydrates and fertilization in animals

Interaction of seminalplasmin with chlortetracycline, a fluorescent chelate probe of Ca2+

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Interaction of seminalplasmin with chlortetracycline, a fluorescent chelate probe of Ca²⁺