Localization of prostaglandin on the plasmalemma of rabbit sperm

Bartoszewicz, W; Dandekar, Pramila V.; Glass, Robert H.; Gordon, Mildred

doi:10.1002/jez.1401910202

Cited by 12 publications

(1 citation statement)

References 22 publications

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“…The autacoids have also been implicated in the events leading to sperm acrosome reaction and fertilization (Lau et al, 1973;Lau and Saksena, 1979;Turner, 1983, 1984;Aitken and Kelly, 1985;Aitken et al, 1986;Joyce et al, 1987;Yanagimachi, 1988). They and/or their receptors have also been located in the plasmalemma of rabbit (Bartoszewicz et al, 1975) and human (Mercado et al, 1978) spermatozoa, respectively. Therefore, it is possible that generation of the arachidonate cyclooxygenase products by spermatozoa is important in the induction of the acrosome reaction and fertilization.…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis of prostaglandins by human spermatozoa in vitro and their role in acrosome reaction and fertilization

Roy

Ratnam

1992

Molecular Reproduction Devel

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Five homogenates of human sperm cells were separately incubated with [14C]arachidonic acid in the presence of reduced glutathione, L-tryptophan, and haematin as cofactors. The cyclooxygenase products of arachidonic acid metabolism were extracted, separated, and measured for their radioactivity. The rate of formation of prostaglandin (PG)D2, PGE2, PGF2 alpha, 6-keto PGF1 alpha, and thromboxane (TX)B2 were 18.0 +/- 1.11, 10.9 +/- 0.68, 5.8 +/- 0.21, 3.9 +/- 0.13 and 6.6 +/- 0.52 pmol/10(6) cells/min, respectively. These results are discussed in relation to the hypothesis that cyclooxygenase metabolites of certain polyunsaturated fatty acids play an important part in the sperm acrosome reaction and fertilization.

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Section: Introductionmentioning

confidence: 99%

Biosynthesis of prostaglandins by human spermatozoa in vitro and their role in acrosome reaction and fertilization

Roy

Ratnam

1992

Molecular Reproduction Devel

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Molecules that initiate or help stimulate the acrosome reaction by their interaction with the mammalian sperm surface

Meizel¹

1985

Am. J. Anat.

204

113

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This review deals with exogenous molecules that stimulate the acrosome reaction (AR) of mammalian sperm in vitro, presumably by acting at the sperm surface. Such molecules may exert their effect(s) by stimulating capacitation and/or by stimulation or initiation of the AR, and they are probably present at one of three putative in vivo sites (also discussed here) for the AR of a fertilizing sperm: the oviductal fluid, the cumulus oophorus matrix, and the zona pellucida. The molecules discussed include serum albumin, hydrolytic enzymes (particularly proteases); hormones including biogenic amines, estradiol, and arachidonic acid metabolites; sulfur-containing beta-amino acids; glycosaminoglycans such as hyaluronic acid; and a zona pellucida glycoprotein. Possible mechanisms to explain the effects of these molecules are also discussed. Several conclusions and suggestions are offered in this review: There is more than one site for the AR of a fertilizing sperm in vitro, depending on experimental conditions and species, but the site(s) at which the AR of a fertilizing sperm occur(s) in vivo is/are still a matter of disagreement; there are a number of molecules that can stimulate or initiate the AR in vitro, and such molecular duplication may also exist in vivo to ensure fertility; and synergistic interaction between some of those exogenous molecules may occur in the stimulation of capacitation and the stimulation or initiation of the AR.

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Identification of phosphatases on the membranes of guinea pig sperm

1978

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Guinea pig epididymal sperm, incubated for ATPases at pH 7.0 or pH 9.0, localize reaction product on both the periacrosomal segment of the plasmalemma and the outer acrosome membrane. In other species, e.g., rabbit, Ca++-ATPase is identified with the outer acrosome membrane. It may transport Ca++ into the acrosome for activation of enzymes released during the acrosome reaction. The neutral ATPase is demonstrable on the periacrosomal plasmalemma and possibly modifies Ca++ concentration in the fluid around the acrosome. In guinea pig sperm, Ca++-ATPase is sensitive to centrifugation or washing of sperm which indicates that the ductal fluid has unusual properties for preservation of the acrosome. Inhibition of the enzyme by these treatments suggests that conditions on the plasmalemmal surface affect the acrosome membrane. Inability to separate reaction product on the plasmalemma from that on the acrosome membrane may be due to migration of reaction product across the periacrosomal space. However, the ATPases are elicited in the guinea pig under the same conditions as in other species. The pH 9.0 enzyme requires Ca++ while the enzyme at pH 7.0 has no ion specificities. Demonstration of these enzymes indicates that mechanisms of acrosome activation, similar to those in other sperm, are relevant to the guinea pig.

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Localization of prostaglandin on the plasmalemma of rabbit sperm

Cited by 12 publications

References 22 publications

Biosynthesis of prostaglandins by human spermatozoa in vitro and their role in acrosome reaction and fertilization

Biosynthesis of prostaglandins by human spermatozoa in vitro and their role in acrosome reaction and fertilization

Molecules that initiate or help stimulate the acrosome reaction by their interaction with the mammalian sperm surface

Identification of phosphatases on the membranes of guinea pig sperm

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