Structural modification of the hamster sperm acrosome during posttesticular development in the epididymis

Olson, Gary E.; Winfrey, Virginia P.; NagDas, Subir K.

doi:10.1002/jemt.10316

Cited by 29 publications

(29 citation statements)

References 54 publications

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“…18 Spermatozoa were isolated from different regions of mouse epididymis according to Olson et al 11 They were fixed with 2% paraformaldehyde in phosphate-buffered saline and spun onto glass slides using the Shandon Cytospin 4 Cytocentrifuge (Thermo Scientific, Pittsburgh, PA, USA). The cells were stained with the anti-USP26-M antibody 17 and an Alexa Fluor 488 conjugated goat anti-rabbit IgG secondary antibody (Invitrogen, Carlsbad, CA, USA) according to Lin and Yen.…”

Section: Immunostaining Of Tissue Sections and Dispersed Germ Cellsmentioning

confidence: 99%

“…Thin sections prepared were stained with uranyl acetated and examined under a Hitachi H7000 transmission EM (Hitachi High-Technologies Co., Tokyo, Japan) operating at 75 kV under standard operating conditions. Wholemount sperm specimens were prepared according to a published protocol, 11 and immuno-gold staining was performed as previously described. 17 Perforatorial triangular cross-sections were photographed regardless whether they contained gold-labels or not, and the distribution of the gold-labels on the images was then analyzed.…”

Section: Immunostaining Of Tissue Sections and Dispersed Germ Cellsmentioning

confidence: 99%

“…The acrosome changes its shape, which is substantial in some species and subtle in others, as well as its content. 10,11 The structures of several sperm organelles are modified, primarily due to disulfide crosslinking of their protein components. The sperm plasma membrane also undergoes changes in surface charge as well as lipid content and distribution.…”

Section: Introductionmentioning

confidence: 99%

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Mouse sperm acquire a new structure on the apical hook during epididymal maturation

Lin¹,

Hsu²,

Yen³

2013

Asian J Androl

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Spermatozoa emerging from the testis undergo a maturation process in the epididymis during which they change morphologically, biochemically and physiologically to gain motility and the ability to fertilize ova. We examined mouse epididymal sperm with immunostaining and transmission electron microscopy (EM) and identified a previously unknown structure on the apical hook. The structure has a coiled configuration around 11 nm in thickness and is present at the tip of each corner of the triangular-rod shaped perforatorium. Surveying sperm isolated from various regions of the epididymis indicated that mouse sperm acquire the hook rim (HR) structure during its passage through the proximal two-thirds of the caput epididymidis. The structure withstands vigorous sonication and harsh chemical treatments and remains intact after the acrosome reaction. Its location and sturdiness suggest a function in protecting the apical hook from mechanical wear during fertilization. Our EM images of epididymal sperm also revealed additional novel structures as well as lateral asymmetry of the sperm head, indicating that mouse sperm head has a structure more complex than previously recognized.

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Section: Immunostaining Of Tissue Sections and Dispersed Germ Cellsmentioning

confidence: 99%

Section: Immunostaining Of Tissue Sections and Dispersed Germ Cellsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Mouse sperm acquire a new structure on the apical hook during epididymal maturation

Lin¹,

Hsu²,

Yen³

2013

Asian J Androl

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“…nucleus, acrosome, perinuclear theca, fibrous sheath, cytoplasmic droplet, and, especially, plasma membrane (Westhoff & Kamp 1997, Cooper & Yeung 2003, Mujica et al 2003, Olson et al 2003). However, results from different laboratories, using a variety of methods, are quite diverse in their findings on protein variations in the spermatozoa during epididymal transit (Dacheux et al 2003, 2005, Saez et al 2003, Toshimori 2003, Gatti et al 2004.…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of ERp29 in rat spermatozoa during epididymal transit

Guo¹,

Qü²,

Li³

et al. 2007

Reproduction

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The mammalian epididymis is able to create sequential changes in the composition of luminal fluid throughout its length, wherein spermatozoa undergo morphological, biochemical, and physiological modifications. Subsequently, spermatozoa acquire the ability for fertilization upon reaching the epididymal cauda. In this study, protein variations in Sprague-Dawley rat spermatozoa along the caput and caudal regions of epididymis were investigated by high-resolution two-dimensional gel electrophoresis (2DE) in combination with mass spectrometry. From total protein spots on the 2DE maps, 43 spots were shown to be significantly modified as sperm traverse the epididymis, and seven unambiguous proteins were identified from them. Finally, using indirect immunofluorescence, we demonstrated that localization of one of these seven proteins, the endoplasmic reticulum protein (ERp29) precursor, which was first reported in mammalian spermatozoa, was apparently up-regulated as the sperm underwent epididymal maturation and expressed mainly on caudal sperm. Western blot analysis also revealed that ERp29 precursor, from both whole spermatozoa and membrane proteins, increased significantly as the sperm underwent epididymal maturation. Furthermore, the results from immunofluorescence-stained epididymal frozen sections demonstrated that ERp29 was localized in cytoplasm of epididymal epithelia, and the fluorescence intensity was significantly higher in the caudal epididymis than in the caput. These clues indicated that the ERp29 precursor, perhaps related to secretory protein synthesis and absorbed by spermatozoa, may play a vital role in sperm maturation during the epididymal transit, particularly, in the sperm/organelle membrane. Reproduction (2007) 133 575-584

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“…This possibility is indeed consistent with our observation of the appearance of immunogold particles being associated with the inner acrosomal membrane and the matrix components. Loss of the immunoreactive RCP following acrosome reaction, coupled with its presence in the acrosomal matrix, may indicate a possible role for this antigen in regulating acrosomal function involving release of various hydrolytic enzymes required for sperm penetration into the oocyte (Dicarlantonio & Talbot 1988, Olson et al 2003. Such a role has been assigned to the 22 kDa glycoprotein in the hamster (Longo et al 1990).…”

Section: Discussionmentioning

confidence: 99%

Germ cell-specific localization of immunoreactive riboflavin carrier protein in the male golden hamster: appearance during spermatogenesis and role in sperm function

Sreekumar¹,

Acharya²,

Lalitha³

et al. 2005

Reproduction

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Riboflavin carrier protein (RCP) is a phosphoglycoprotein (37 kDa) that is well studied in chicken. An immunologically crossreacting protein was identified in mammals and active immunization of male rats and bonnet monkeys with chicken RCP lead to an ,80% reduction in fertility. However, the physiological mechanism responsible for inhibition of male fertility has not been investigated. Moreover, information on the cell type-specific localization and the origin of immunoreactive RCP during spermatogenesis is extremely limited. Hence, studies were carried out to determine the pattern of expression of immunoreactive RCP during spermatogenesis and its role in sperm function in the golden hamster. Immunoreactive RCP was germ cell-specific, found to be associated with the acrosome-organizing region of early spermatids and showed interesting patterns of immunolocalization during late stages of spermiogenesis. Mature spermatozoa exhibited acrosome-specific localization, mainly in the peri-acrosomal membrane. The immunoreactive protein was undetectable in (non)gonadal somatic cells tested. The protein had a molecular mass of 45 -55 kDa and was biosynthesized by round spermatids. The acrosome-specific localization of immunoreactive RCP was unchanged during capacitation, but it was substantially lost during acrosome reaction. Functional studies indicated that treatment of spermatozoa with anti-RCP antibodies did not have any effect on either capacitation or acrosome reaction, but markedly reduced the rate of sperm penetration into zona-free hamster oocytes. These results show the existence of male germ cell-specific immunoreactive RCP, having a potential role in sperm -egg interaction in hamsters. Also the pattern of immunoreactive-RCP localization makes it an ideal marker to monitor development of acrosome in mammalian spermatozoa.

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Structural modification of the hamster sperm acrosome during posttesticular development in the epididymis

Cited by 29 publications

References 54 publications

Mouse sperm acquire a new structure on the apical hook during epididymal maturation

Mouse sperm acquire a new structure on the apical hook during epididymal maturation

Identification and characterization of ERp29 in rat spermatozoa during epididymal transit

Germ cell-specific localization of immunoreactive riboflavin carrier protein in the male golden hamster: appearance during spermatogenesis and role in sperm function

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