Immunocytochemical detection of actin and 53 kDa polypeptide in the epididymal spermatozoa of rat and mouse

Paranko, Jorma; Yagi, Ahmed; Kuusisto, Mari

doi:10.1002/ar.1092400409

Cited by 18 publications

(9 citation statements)

References 51 publications

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“…This clear redistribution of F-actin in the post-acrosomal region was not seen in rodent sperm, and may be due to the fact that samples of rodent sperm were obtained from the epididymis. Nevertheless, in agreement with the studies of Brener et al (2003) and Paranko et al (1994), the post-acrosomal region in control sperm showed the presence of F-actin, and this was in contrast to Howes et al (2001). The polymeric form of actin (F-actin) is thought to be particularly important as its depolymerization between the outer acrosomal and plasma membrane is correlated with initiation of the AR in studies on guinea pig (Breitbart & Spungin 1997) and on bull, ram, mouse and human sperm (Brener et al 2003).…”

Section: Discussionsupporting

confidence: 90%

Cytoskeleton localization in the sperm head prior to fertilization

Dvořáková¹,

Moore²,

Šebková³

et al. 2005

Reproduction

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Three major cytoskeletal proteins, actin, tubulin and spectrin, are present in the head of mammalian spermatozoa. Although cytoskeletal proteins are implicated in the regulation of capacitation and the acrosome reaction (AR), their exact role remains poorly understood. The aim of this study was to compare the distribution of the sperm head cytoskeleton before and after the AR in spermatozoa representing a range of acrosome size and shape. Spermatozoa from the human and three rodents (rat, hamster and grey squirrel) were fixed before and after the AR in appropriate medium in vitro. Indirect immunofluorescent localization of cytoskeletal proteins was undertaken with antibodies recognizing actin, spectrin and a-tubulin. Preparations were counterstained with propidium iodide and examined by epifluorescent and confocal microscopy. Our results clearly demonstrated changes in localization of cytoskeleton during the AR, mainly in the apical acrosome with further changes to the equatorial segment and post-acrosomal regions. The pattern of cytoskeletal proteins in the sperm head of all the species was similar in respect to various sub-compartments. These observations indicated that the sperm head cortical cytoskeleton exhibits significant changes during the AR and, therefore, support the image of cytoskeletal proteins as highly dynamic structures participating actively in processes prior to fertilization.

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Section: Discussionsupporting

confidence: 90%

Cytoskeleton localization in the sperm head prior to fertilization

Dvořáková¹,

Moore²,

Šebková³

et al. 2005

Reproduction

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“…Prior to the acrosome reaction, F actin undergoes depolymerization. Actin is also detected in the outer dense fibers of the sperm tail, suggesting that actin may regulate sperm motility (3,13,29). We postulate that altered expression of Fscn1 contributes to reduced sperm motility and folding of sperm tails in Taf7l Ϫ/Y testes.…”

Section: Discussionmentioning

confidence: 77%

“…To avoid saturation of PCR, products were taken after various cycles (20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30) and analyzed by gel electrophoresis. One microgram of total RNA from adult wildtype and XX Y‫ء‬ testes was used for reverse transcription.…”

Section: Quantitative and Semiquantitative Reverse Transcription (Rt)mentioning

confidence: 99%

Abnormal Sperm in Mice Lacking the Taf7l Gene

Cheng

Buffone

Kouadio

et al. 2007

Molecular and Cellular Biology

109

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TFIID is a general transcription factor required for transcription of most protein-coding genes by RNA polymerase II. TAF7L is an X-linked germ cell-specific paralogue of TAF7, which is a generally expressed component of TFIID. Here, we report the generation of Taf7l mutant mice by homologous recombination in embryonic stem cells by using the Cre-loxP strategy. While spermatogenesis was completed in Taf7l ؊/Y mice, the weight of Taf7l ؊/Y testis decreased and the amount of sperm in the epididymides was sharply reduced. Mutant epididymal sperm exhibited abnormal morphology, including folded tails. Sperm motility was significantly reduced, and Taf7l ؊/Y males were fertile with reduced litter size. Microarray profiling revealed that the abundance of six gene transcripts (including Fscn1) in Taf7l ؊/Y testes decreased more than twofold. In particular, FSCN1 is an F-action-bundling protein and thus may be critical for normal sperm morphology and sperm motility. Although deficiency of Taf7l may be compensated in part by Taf7, Taf7l has apparently evolved new specialized functions in the gene-selective transcription in male germ cell differentiation. Our mouse studies suggest that mutations in the human TAF7L gene might be implicated in X-linked oligozoospermia in men.TFIID, a general transcription factor, plays a central role in transcription initiation of most protein-coding genes by RNA polymerase II. TFIID is a multiprotein complex consisting of TATA-binding protein (TBP) and 12 to 15 TBPassociated factors (TAFs) (20,35). The assembly of TFIID at the promoter region recruits other basal transcription factors and RNA polymerase II (2, 31). TAFs play important roles in transcriptional regulation. Some TAFs directly interact with transcriptional activators and thus serve as coactivators. In addition, interactions between TAFs are critical for promoter recognition and selectivity by RNA polymerase II (17,36).Strikingly, studies of a number of tissue-specific TAFs in Drosophila melanogaster and mouse have identified cell-typespecific transcription programs. In Drosophila melanogaster, five testis-specific homologues of widely expressed TAFs have been reported: Can (homologue of dTAF5), Nht (homologue of dTAF4), Mia (homologue of dTAF6), Sa (homologue of dTAF8), and Rye (homologue of dTAF12) (18,19). Null mutations in can, nht, mia, and sa result in the same male sterile phenotype, and all four genes are required for meiotic cell cycle progression and onset of spermatid differentiation (27). In addition, Rye interacts with Nht, suggesting that these five testis-specific TAFs in Drosophila function in the same transcription regulatory pathway (18). Mechanistically, these TAFs may counteract transcriptional repression by Polycomb group (PcG) proteins in spermatocytes (8). In mice, TAF4B (homologue of TAF4) is highly expressed in the testis and the granulosa cells of the ovary, where it is required for follicular development (14). Testes of TAF4B-deficient males are initially normal but undergo progressive germ cell loss, r...

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“…The presence of actin in mammalian spermatozoa has been demonstrated in several species including cattle, boar, rat, mouse, guinea pig, hamster, mole, human, rabbit, fat tailed dunnart and opossum (Flaherty et al 1986 ;Halenda et al 1987 ;Olson & Winfrey, 1991 ;Castellani-Ceresa et al 1992 ;MorenoFierros et al 1992 ;Breed et al 1993 ;Paranko et al 1994). However, the precise localisation of this protein has not been conclusively demonstrated (Lora-Lamia et al 1986 ;Paranko et al 1994 ;Yagi & Paranko, 1995).…”

mentioning

confidence: 99%

“…However, the precise localisation of this protein has not been conclusively demonstrated (Lora-Lamia et al 1986 ;Paranko et al 1994 ;Yagi & Paranko, 1995). In the prepubertal testis, F-actin is uniformly distributed throughout the cytoplasm of the undifferentiated spermatid.…”

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confidence: 99%

Actin polymerisation during morphogenesis of the acrosome as spermatozoa undergo epididymal maturation in the tammar wallaby (Macropus eugenii)

2001

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In the tammar wallaby (Macropus eugenii), post-testicular acrosomal shaping involves a complex infolding and fusion of the anterior and lateral projections of the scoop-shaped acrosome into a compact button-like structure occupying the depression on the anterior end of the sperm nucleus. The present study has generated cytochemical and histological evidence to demonstrate that the occurrence of actin filaments (F-actin, labelled by Phalloidin-FITC) in the acrosome of tammar wallaby spermatozoa is temporally and spatially associated with the process of acrosomal shaping in the epididymis, through a pool of monomeric actin (G-actin, labelled by Rh-DNase I) present in the acrosome throughout all stages of epididymal maturation. F-actin was not detected in the acrosome of testicular spermatozoa, but was found in the infolding and condensing acrosome of caput and corpus epididymal spermatozoa. When the spermatozoa completed acrosome shaping in the cauda epididymidis, F-actin disappeared from the acrosomal area. The strong correlation between the occurrence of F-actin and the events of acrosomal shaping suggested that the post-testicular shaping of the acrosome might depend on a precise succession of assembly and disassembly of F-actin within the acrosome as the spermatozoa transit the epididymis. Thus, actin filaments might play a significant role in the acrosomal transformation, as they are commonly involved in morphological changes in somatic cells.

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Immunocytochemical detection of actin and 53 kDa polypeptide in the epididymal spermatozoa of rat and mouse

Cited by 18 publications

References 51 publications

Cytoskeleton localization in the sperm head prior to fertilization

Cytoskeleton localization in the sperm head prior to fertilization

Abnormal Sperm in Mice Lacking the Taf7l Gene

Actin polymerisation during morphogenesis of the acrosome as spermatozoa undergo epididymal maturation in the tammar wallaby (Macropus eugenii)

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