Exposure of Sperm Head Equatorin after Acrosome Reaction and Its Fate after Fertilization in Mice
Equatorin is a sperm head equatorial protein, possibly involved in sperm-oocyte fusion (Toshimori et al., Biol Reprod 1998; 59:22â29). In the present work, we have shown that equatorin contained in the posterior acrosome is detectable only after spontaneous or induced acrosome reactions following...
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Published in | Biology of reproduction Vol. 65; no. 5; pp. 1425 - 1436 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Madison, WI
Society for the Study of Reproduction
01.11.2001
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Subjects | |
Online Access | Get full text |
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Summary: | Equatorin is a sperm head equatorial protein, possibly involved in sperm-oocyte fusion (Toshimori et al., Biol Reprod 1998;
59:22â29). In the present work, we have shown that equatorin contained in the posterior acrosome is detectable only after
spontaneous or induced acrosome reactions following fixation and permeabilization, but not in intact spermatozoa. The presence
of protease inhibitors during sonication or ionophore treatments does not inhibit the exposure of the antigenic epitope. The
zona-penetrated spermatozoa lying in the perivitelline space display equatorin, similar to those of the acrosome-reacted ones.
After sperm-egg fusion during in vitro fertilization (IVF), the equatorin dissociates from the sperm head equatorial region
and remains at the vicinity of the decondensing male pronuclei. During pronuclear apposition stage, it is pushed away from
the pronuclei, possibly by the perinuclear microtubules. After first cleavage, equatorin is inherited by one of the proembryonic
cells. The residual equatorin disappears after the second cleavage. Microinjected whole spermatozoa or sperm heads into the
MII stage oocytes display equatorin similar to those of the perivitelline sperm. After activation, it dissociates from the
sperm nuclei in a similar manner as during IVF. The mode of equatorin degeneration during fertilization is similar to those
of the sperm tail components or mitochondria, but different from those of the membrane associated proteins. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0006-3363 1529-7268 |
DOI: | 10.1095/biolreprod65.5.1425 |