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  • 1
    ISSN: 0148-7280
    Keywords: human ; sperm ; zona pellucida ; zona-free hamster oocyte ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In these experiments the mean number of sperm bound to the zonae pellucidae of immature human oocytes and to the vitelli of zona-free hamster oocytes were counted after centrifuging the oocytes through a discontinuous dextran gradient into a fixative. Sperm suspensions (107 sperm/ml) were preincubated in BWW medium containing 35 mg/ml of human serum albumin for 0 to 20 hr and coincubated with oocytes for 4 hr.The kinetics of sperm binding and sperm penetration were clearly different for the two types of oocytes in this system. Sperm binding to the zona pellucida appeared to be associated with zona penetration; when the zona was penetrated, many sperm were tightly bound and vice versa. A similar association between human sperm binding to the zonafree hamster oocyte and hamster oocyte penetration was not so apparent. Transmission electron microscopy revealed that all sperm which were “bound” to the hamster vitellus were acrosome reacted. On the surface of the human zona pellucida acrosome intact and acrosome reacted sperm were observed.These results suggest that tight binding of spermatozoa to the zona pellucida may be an important preliminary step in human fertilization. If this is true the activity of the sperm's “receptor for zona” may not be detected by the assay with zona-free hamster oocytes.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 10 (1984), S. 153-163 
    ISSN: 0148-7280
    Keywords: mouse ; sperm ; egg ; sperm plasma membrane ; in vitro ; binding ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have studied the molecular mechanisms of gamete interaction in vitro in the laboratory mouse, Mus musculus. In particular, we were interested in whether this interaction is similar to a lectin-hapten-mediated process. Inhibition of sperm-zona binding was examined using various concentrations (.25 mM to 50 mM) of different sugars (sialic acid α-methylmannose, glucose, fucose, galactose, and N-acetyl-glucosamine). Sperm-zona binding was significantly decreased when eggs were pretreated with 10 mM of sialic acid or α-methylmannose but not by other sugars tested. Furthermore, treatment of capacitated sperm with neuraminidase destroyed their ability to bind and fertilize eggs. We have also used a specific lectin for sialic acid from the horseshoe crab (Limulus polyphemus) to agglutinate mouse sperm. The lectin (.120 ng/ml) mediated agglutination of mouse sperm (105 sperm/ml) was routinely observed to increase from a 10% agglutination immediately following their isolation from the epididymis to 100% agglutination 90 minutes later. Collectively, these results suggest the appearance of specific sugar moieties on the surface of the sperm plasma membrane which, in this particular species of mouse, are sialylated glycoproteins acting as ligands for specific receptors on the surface of the egg. These are the first data to indicate that sperm-egg recognition and attachment is a lectin-hapten-mediated process in the mouse.
    Additional Material: 6 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 14 (1986), S. 333-346 
    ISSN: 0148-7280
    Keywords: spermatozoon ; motility ; capacitation ; hamster ; fertilization ; acrosome reaction ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Movement characteristics of golden hamster spermatozoa were studied upon collection from the cauda epididymis, during an incubation which capacitates the spermatozoa in vitro, during penetration of the cumulus, and during attachment to and penetration of the zona pellucida. High-speed videomicrography was employed to quantitate flagellar beat frequency and shape. The status of the acrosome was also assessed. During capacitation, hamster spermatozoa become increasingly invigorated before the onset of hyperactivated motility. Within the cumulus, beat frequency and curvature are reduced, apparently in response to the physical resistive properties of the matrix material. These properties appear to vary within the cumulus. Initial attachment to the zona precedes completion of the acrosome reaction, is non-rigid, and is accompanied by increased beat frequency and curvature. Subsequently, the onset of rigid binding to the zona, completion of the acrosome reaction, and increased flagellar beat frequency are very closely associated in time. The latter produces an increase in thrust against the zona. Preliminary results indicate that ensuing zona penetration requires not more than five minutes, is at oblique angles, and is associated with a continuation of vigorous flagellar beating.
    Additional Material: 7 Ill.
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  • 4
    ISSN: 0148-7280
    Keywords: lectins ; sperm ; capacitation ; plasma membrane ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Human sperm incubated in vitro in BWW medium containing 35 mg/ml human serum albumin acquire the capacity to penetrate the human zona pellucida and to fuse with the zona-free hamster oocyte. We have studied changes in lectin-induced agglutination of human sperm during incubation in this medium to detect alterations in the sperm surface which may be correlated with the acquisition of these functions. Sperm incubated for 1, 6, or 24 hr were combined with two-fold dilutions of lectins for 30 min at 37°C, in 5% CO2, balance air. When pooled data from five donors were analyzed, the average sperm agglutination titer of wheat germ agglutinin (WGA), phytohemagglutinin-E (PHA), Lens culinaris agglutinin (LCA), peanut agglutinin (PNA), and Pisum sativum agglutinin (PSA) was found to increase significantly (P ≤ 0.06) with incubation in vitro, although there was considerable variation between ejaculates. Ulex europaeus and Dolichos biflorus agglutinins did not agglutinate human sperm (≤250 μg/ml). Results of this screening demonstrate the alteration of sperm surface components during in vitro incubation and suggest that WGA, PHA, LCA, and PSA may prove useful in efforts to correlate changes in the sperm surface with the ability of the sperm to fertilize the egg.
    Additional Material: 4 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 4 (1981), S. 525-533 
    ISSN: 0148-7280
    Keywords: capacitation ; fertilization ; spermatozoa ; in vitro ; Little Brown Bat ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The temperature dependence of capacitation in bat sperm (Myotis lucifugus lucifugus) was studied by monitoring fertilizations rates of zona-free hamster ova at different temperatures. Spermatozoa were cultured in BWW medium at temperatures 4°C, 24°C, 32°C, 42°C, and 55°C from 0-24 hr. Activation of sperm could be determined visually due to the change in movement seen through light microscopy. Activation was later confirmed by higher rates of fertilization. Preincubation of the bat sperm was found to have a direct effect on the success of penetration of the zona-free hamster ova. Holding bat spermatozoa at low temperature for long intervals allowed them to remain motile but unable to fertilize. Sperm are not irreversibly damaged, however, and activation, when the temperature is increased to 32°C, is faster than when sperm are intitially put at 32°C, resulting in good fertilization rates.
    Additional Material: 5 Ill.
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  • 6
    Publication Date: 1983-05-01
    Print ISSN: 0092-8674
    Electronic ISSN: 1097-4172
    Topics: Biology , Medicine
    Published by Cell Press
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  • 7
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