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At least 19 recordsLinked to original sources
PubMed1985

Effects of in vivo and in vitro fertilization environments on the expression of a surface antigen of the mouse sperm tail.

Sperm maturation antigen 4 (SMA 4) is a glycoprotein secreted by the mouse epididymis that binds specifically to the sperm tail. Its fate has been examined on cauda epididymidal sperm in vivo and in vitro. SMA 4 was detected by indirect immunofluorescence (IIF) on sperm flushed from uteri of mice 5.5 h after natural or artificial insemination, but not on sperm attached to cumulus cells or zonae pellucidae of eggs recovered at that time. Detectable SMA 4 declines with time in vitro, as assayed by IIF on intact sperm or by enzyme immunoassay (EIA) of detergent extracts. After 3 h in vitro, 90% or more of sperm are not positive for SMA 4 by IIF. EIA of medium in which sperm have been incubated suggests that SMA 4 is being released from the cell surface. This time-dependent loss of SMA 4 is inhibited by mouse or rat cauda epididymidal fluid, low incubation temperature, or lack of protein in the incubation medium. However, the loss does not seem to be affected by the presence of eggs, cumulus cells, or oviduct fluids. SMA 4 is not removed from the sperm by selected treatments, suggesting that it is bound to the plasma membrane by strong, noncovalent interactions.

Animals↗
PubMedDate not supplied

Further characterization of a secreted epididymal glycoprotein in mice that binds to sperm tails.

Sperm maturation antigen 4 (SMA-4) is a surface component of the mouse sperm tail. Previously, immunofluorescence studies indicated that SMA-4 may be secreted by principal cells of the distal caput epididymidis and bound to spermatozoa as they pass through that region of the duct. In the present study, detergent extracts of spermatozoa from the cauda epididymidis were subjected to polyacrylamide gel electrophoresis under reducing and denaturing conditions, transferred to nitrocellulose, and immunostained with a monoclonal antibody against SMA-4. A band of approximately 54,000 molecular weight was revealed. The band was also stained by the periodic acid-Schiff (PAS) procedure. This glycoprotein was not detected in extracts of spermatozoa from the proximal caput epididymidis or of spermatozoa from the cauda epididymidis that were preincubated for 4 hours in an in vitro fertilization environment. Blots of sperm-free fluid from the corpus and cauda epididymidis displayed an immunoreactive and PAS-positive band of about 85,000 molecular weight that was not observed in fluid from the caput epididymidis. The difference in the molecular weights of the antigen in the fluid and that in extracts of cauda spermatozoa suggests that SMA-4 may be modified chemically upon association with the sperm surface.

Animals↗
PubMed1984

Ultrastructural sperm tail defects associated with sperm immotility.

Four individuals with a complaint of infertility were evaluated after a semen analysis had demonstrated no motility. The semen analyses were otherwise normal, with the exception of a low count in one subject. All had normal percentages of living sperm. One of the individuals had chronic respiratory disease, and two others had a previous history of genitourinary infection and/or testicular injury. Three subjects possessed antisperm antibodies. Electron microscopy revealed a multiplicity of sperm tail structural defects seen in all specimens. Some of these data support the concept of acquired immotile sperm syndrome(s) with ultrastructural defects, as contrasted with the usual congenital forms of the immotile-cilia syndrome.

Adult↗
PubMedDate not supplied

Evaluation of computerized analysis of sperm movement characteristics and differential sperm tail swelling patterns in predicting human sperm in vitro fertilizing capacity.

Multivariate discriminant analysis was used to evaluate the usefulness of computer image analysis of sperm movement characteristics and differential patterns of sperm tail swelling after hypoosmotic treatment for predicting the human sperm in vitro fertilizing capacity assessed by the zona-free hamster egg penetration assay. Fifty-five semen samples, mostly normospermic, from untreated infertility clinic patients were analyzed. The % normal sperm morphology, linearity of seminal sperm movement, seminal sperm head beat frequency, mean and maximum amplitudes of lateral head displacement, and hypoosmotic sperm tail swelling patterns c, d and f were selected by multivariate discriminant analysis to be capable of discriminating the samples exhibiting the presence or the absence of sperm in vitro fertilizing capacity. The % total sperm tail swelling did not give additional information about in vitro fertilizing capacity. These preliminary data suggest that computer image analysis of sperm movement characteristics and differential evaluation of hypoosmotic sperm tail swelling might be useful for the prediction of human sperm fertility. Further prospective studies are necessary to validate their predictive functions.

Evaluation Studies as Topic↗
PubMed1986

Isolation and characterization of a rabbit sperm tail protein.

Rabbit sperm tails were obtained by a nitrogen cavitation procedure and separated by discontinuous sucrose gradient centrifugation. Proteins were extracted from sperm tails with 3[(3-cholamidopropyl)-dimethylammonio]-1-propane sulfonate (CHAPS) and separative disk electrophoresis and DEAE-trisacryl column chromatography. A protein with an estimated mol wt of 20.1 +/- 1.1 kD was isolated and found to be homogeneous by SDS-PAGE and designated as rSMP-B. The isoelectric point of rSMP-B was in the range of pH 4.4-4.7. The amino acid composition was determined, and glycine was identified as the N-terminal residue. Antisera were raised against purified rSMP-B. Using a peroxidase-antiperoxidase method, the rSMP-B antigen was located on the surface of the midpiece and tail of the sperm. Testis sections showed intense staining of late spermatids located within the seminiferous tubules. Adult male rabbits were inoculated with rSMP-B protein and Freund's adjuvant. The testis and epididymis of the immunized animals showed absence of sperm. The immunolocalization findings and the immunization data suggest that rSMP-B is formed in late spermatid and that it is an essential structural component of sperm.

Amino Acids↗
PubMed1998

An X-linked gene encodes a major human sperm fibrous sheath protein, hAKAP82. Genomic organization, protein kinase A-RII binding, and distribution of the precursor in the sperm tail.

Mammalian sperm motility is regulated by a cascade of cAMP-dependent protein phosphorylation events mediated by protein kinase A. A-kinase anchor proteins (AKAPs) direct protein kinase A activity by tethering the enzyme near its physiological substrates. We have characterized a major human sperm fibrous sheath AKAP, hAKAP82, and its precursor, pro-hAKAP82, the homologues of the mouse fibrous sheath proteins mAKAP82 and pro-mAKAP82. The cDNA sequence of pro-hAKAP82 was highly homologous to the mouse sequence, and the functional domains of the pro-hAKAP82 protein, the protein kinase A binding, and the pro-hAKAP82/hAKAP82 cleavage sites were identical to those of the mouse protein. The genomic organization of mouse pro-AKAP82 was determined. Alternative splicing occurred in both the mouse and human pro-AKAP82 genes that resulted in at least two distinct transcripts and possibly two different proteins. Compared with pro-mAKAP82, considerably less pro-hAKAP82 was processed to hAKAP82 in human sperm. Although pro-mAKAP82 localizes only to the proximal portion of the principal piece of the flagellum, pro-hAKAP82 localized to the entire length of the principal piece. The pro-hAKAP82 gene mapped to human chromosome Xp11.2, indicating that defects in this gene are maternally inherited. These studies suggest several roles for hAKAP82 in sperm motility, including the regulation of signal transduction pathways.

A Kinase Anchor Proteins↗
PubMed1975

Immunological immobilization of detached rabbit sperm tails.

Motile rabbit sperm tails that lack heads are immobilized by antibody plus complement. Accordingly, immunological immobilization may not necessarily require the extensive sperm acrosomal damage previously reported in immobilized normal sperm.

Animals↗
PubMed2002

Mapping of an immotile short tail sperm defect in the Finnish Yorkshire on porcine Chromosome 16.

An immotile short tail sperm defect has recently been identified as a hereditary disorder present within the Finnish Yorkshire pig population. The syndrome is inherited as an autosomal recessive disease exclusively expressed in male individuals as shorter sperm tail length and immotile spermatozoa. Based on the assumption of a recent common origin of the disease-causing mutation, a genome-wide search was performed with 228 evenly spaced microsatellites by homozygosity mapping of affected and unaffected DNA pools. One locus, SW2411 on Chr 16, demonstrated a significantly skewed allele distribution between the two pools. Linkage analysis of five markers in this region mapped the disease-causing gene within a 6-cM confidence interval region with a highest LOD score of 7.7 at marker SW419. It appears that three-marker haplotypes can be used for marker-assisted selection within analyzed pedigrees. Furthermore, future fine mapping may reveal a more precise population-wide associated haplotype and facilitate identification of a new gene affecting sperm tail development.

Animals↗
PubMed1996

Fate of the sperm mitochondria, and the incorporation, conversion, and disassembly of the sperm tail structures during bovine fertilization.

Sperm incorporation and the conversion of the sperm-derived components into zygotic structures during in vitro fertilization of bovine oocytes was explored by combining ultrastructural studies with observations of the fertilizing sperm tagged with a mitochondrion-specific vital dye MitoTracker green FM. The zygotes fertilized by the MitoTracker-labeled sperm were fixed at various times after fertilization and then processed for immunocytochemistry to examine the distribution of DNA, microtubules, and sperm tail components, including the fibrous sheath and axonemal microtubules. We show here that the complete incorporation of the sperm, but not sperm-oocyte binding and oocyte activation, depends upon the integrity of oocyte microfilaments and is inhibited by the microfilament disrupter cytochalasin B. After sperm incorporation, the mitochondria are displaced from the sperm's connecting piece, and the sperm centriole is exposed to the egg cytoplasm. This event is followed by the formation of the microtubule-based sperm aster, which is responsible for the union of male and female pronuclei. Concomitantly, the major structure of the sperm principal piece, the fibrous sheath, disappears. After the first mitosis, the compact mitochondrial sheath can be seen in one of the blastomeres. An aggregate of the sperm mitochondria is observed at the entry of the second mitosis, although they remain in the vicinity of the nucleus and can later be seen at one pole of the metaphase spindle. The mitochondrial cluster is occasionally found in one of the blastomeres in the early-stage four-cell embryos, but it is no longer detected by the beginning of the third mitotic cycle. These data suggest that the disassembly of the sperm tail during bovine fertilization occurs as a series of precisely orchestrated events involving the destruction (fibrous sheath and mitochondrial sheath) and transformation (DNA, sperm centriole) of particular sperm structures into zygotic and embryonic components.

Acrosome↗
PubMed2002

Developmental expression of spermatid-specific thioredoxin-1 protein: transient association to the longitudinal columns of the fibrous sheath during sperm tail formation.

The mammalian sperm tail presents a complex organization in which a number of additional structures, namely outer dense fibers and fibrous sheath, surround the central axoneme and are thought to regulate flagellar motility. We have previously described a novel member of the thioredoxin family of proteins with a spermatid specific expression pattern, spermatid-specific thioredoxin-1 (Sptrx-1). We report here the developmental analysis of Sptrx-1 expression during murine spermiogenesis. Immunocytochemical analysis of Sptrx-1 through the different steps of spermiogenesis in rat seminiferous tubule sections showed that its expression begins at step 9, gets progressively stronger until steps 14-16 (where a peak is reached), and then diminishes in steps 17 and 18 until practically no immunolabeling is detected in step 19 spermatid. During its transient expression in spermiogenesis, Sptrx-1 is most concentrated in the periaxonemal compartment of the tail of the elongating spermatid, except in the very last steps (steps 17-19), when periaxonemal labeling disappears and a residual buildup of Sptrx-1 occurs in the shrinking cytoplasmic lobe. Electron microscopic analysis by immunogold labeling pinpointed the localization of Sptrx-1 to the assembling longitudinal columns of the fibrous sheath, whereas the forming ribs of the fibrous sheath were unlabeled. Immunoblotting of isolated fibrous sheath and tails obtained from epididymal or ejaculated sperm of rat and human confirmed our immunocytochemical observation: Sptrx-1 is no longer a component of the mature fibrous sheath. To our knowledge, this is the first report of a protein that specifically associates to the fibrous sheath during development but does not become a permanent structural component. The expression pattern of Sptrx-1 during rat spermiogenesis suggests that it could be part of a nucleation center for the formation of the longitudinal columns and transverse ribs that bridge the latter.

Animals↗
PubMed2001

Molecular evaluation of two major human sperm fibrous sheath proteins, pro-hAKAP82 and hAKAP82, in stump tail sperm.

OBJECTIVE: To determine whether mutations in the pro-hAKAP82 gene and the resulting pro-hAKAP82 and hAKAP82 proteins were associated with the infertility seen in a patient with stump tail sperm. DESIGN: Case report. SETTING: Academic research and teaching environment, tertiary care hospital. PATIENT(S): A single, infertile Caucasian male diagnosed with essentially 100% stump tail sperm. INTERVENTION(S): None. MAIN OUTCOME MEASURE(S): Electrophoresis, silver staining, and immunoblotting of patient and control sperm proteins; RII (type II regulatory subunit of protein kinase-A) overlay assay of patient and control sperm proteins, partial DNA sequence analysis of patient's pro-hAKAP82 gene; indirect immunofluorescence and immunogold electron microscopy of patient and control sperm. RESULTS(S): No significant abnormalities in the size or amount of pro-hAKAP82 and hAKAP82 or in the ability of these proteins to bind the regulatory subunit of protein kinase-A were identified in the patient's sperm. Partial sequence analysis of the patient's pro-hAKAP82 gene was identical to the published normal sequence. Indirect immunofluorescence and immunoelectron microscopy of sperm localized pro-hAKAP82/hAKAP82 to the sperm flagellum and demonstrated that the proteins were present in a disorganized, amorphous region, which apparently represented the fibrous sheath. CONCLUSION(S): These results suggest that, although pro-hAKAP82 and hAKAP82 localize to the correct structural component of the flagellum and are not directly responsible for the stump tail phenotype, they are unable to assemble normally into the fibrous sheath. Although this study did not identify abnormalities in the pro-hAKAP82 gene or its resulting proteins in a patient with stump tail sperm, several regions of the gene and protein remain to be examined.

A Kinase Anchor Proteins↗
PubMed1983

Pig sperm tail tubulin. Its extraction and characterization.

Axonemal tubulin extracted from pig sperm tails has been characterized by one- and two-dimensional electrophoresis and by one-dimensional peptide mapping. The electrophoretic mobilities of its subunits after reduction and carboxymethylation were similar to those of the major subunits of pig brain tubulin. Sperm tail tubulin subunits also had roughly the same isoelectric points as pig brain tubulin subunits, except that they appeared to have a relatively larger tailing effect. The proteolytic cleavage pattern of the pig sperm tail beta-tubulin closely resembled those of both the tunicate (Ciona intestinalis) sperm beta-tubulin and pig brain beta-tubulin. The peptide pattern of pig sperm tail alpha-tubulin, however, was more similar to that of tunicate sperm tail alpha-tubulin than to that of pig brain alpha-tubulin. This supports the hypothesis put forward in a previous investigation [1] that functionally similar tubulins from taxonomically distant species can be more related than functionally dissimilar tubulins from the same species.

Animals↗
PubMed2006

Tyrosine phosphorylation on capacitated human sperm tail detected by immunofluorescence correlates strongly with sperm-zona pellucida (ZP) binding but not with the ZP-induced acrosome reaction.

BACKGROUND: Protein tyrosine phosphorylation (TP) of human sperm is related to sperm capacitation and zona pellucida (ZP) binding. The aim of this study was to determine whether the TP of capacitated sperm is a useful marker for the ability of sperm to bind to the ZP and undergo the ZP-induced acrosome reaction (AR). METHODS: Semen samples were obtained from 115 subfertile men with sperm count > or =20 x 10(6)/ml, motility > or =25% and variable morphology. Motile sperm (2 x 10(6)/ml) selected by swim-up were incubated with four oocytes for 2 h, and the number of sperm bound to the ZP and the ZP-induced AR was examined. TP of sperm tail was assessed by immunofluorescence (IF) with anti-phosphotyrosine monoclonal antibody. The time course and effects of dibutyryl cyclic adenosine monophosphate (dbcAMP) and phorbol myristate acetate (PMA) on TP were also studied. RESULTS: TP was stimulated more by dbcAMP (P < 0.001) and less by PMA (P < 0.05). TP increased significantly with time of incubation of sperm. TP was not detectable on the surface of unfixed live sperm by either Dynabeads or IF. Sperm TP at 2, 4 and 20 h incubation was all significantly correlated with sperm-ZP binding but not with the ZP-induced AR. CONCLUSION: Sperm TP detected by IF correlates strongly with sperm-ZP binding capacity but not with the ZP-induced AR. This simple IF assay of TP may be a clinically useful test of sperm function that is predictive of normal sperm ZP-binding capacity.

Acrosome Reaction↗
PubMed2003

Incidence of sperm-tail tyrosine phosphorylation and hyperactivated motility in normozoospermic and asthenozoospermic human sperm samples.

Our objective was to study the incidence of sperm-tail phosphotyrosine immunoreactivity in normozoospermic and asthenozoospermic human sperm samples, its association with sperm motion parameters, particularly hyperactivated motility, and its potential involvement in the pathogenesis of asthenozoospermia. The work was conducted as a prospective experimental study in the Sperm Biology and Andrology laboratories of the Jones Institute, a medical school-based fertility center. The study subjects were healthy fertile male donors (normozoospermic samples) and infertile patients (asthenozoospermic samples) attending the center. Recently ejaculated semen samples were washed twice to eliminate seminal plasma and a swim-up was performed to select the motile population which, in turn, was incubated up to 18 h at 37 degrees C in 3.5% human serum albumin-supplemented Ham's F10 to allow for capacitation. For evaluation, sperm aliquots were taken pre-swim-up (T0), immediately post swim-up (T1), at 6 h (T6), and 18 h (T18) of incubation. The main outcome measures were computer-analyzed sperm motion parameters and hyperactivated motility, and immunodetection of phosphotyrosine (PY)-containing proteins. During the capacitating incubation, normozoospermic samples displayed maximum motility, velocity, and hyperactivation at T6, significantly decreasing their values at T18. PY-proteins were located both at the tail and head of spermatozoa. Their expression increased progressively during the incubation, being present in about 70% of the sperm tails at T18. Asthenozoospermic samples showed an inability to respond to capacitation with an increase in motion parameters and PY-phosphorylation. At T6, both hyperactivation and PY-phosphorylation were significantly lower than in normal samples. Our results suggest that PY-phosphorylation of tail proteins is highly conspicuous in human spermatozoa, and increases its incidence in a time-dependent manner, as more sperm become capacitated. Asthenozoospermic samples displaying low percentages of motile sperm and altered motion characteristics showed a decreased incidence of PY-phosphorelated sperm. Tail protein PY-phosphorylation may be related to sperm movement, especially to hyperactivated motility and its deficiency may be associated to asthenozoospermia.

Humans↗
PubMed1998

Mouse Odf2 cDNAs consist of evolutionary conserved as well as highly variable sequences and encode outer dense fiber proteins of the sperm tail.

The outer dense fibers (ODF) of the mammalian sperm tail comprise a unique, specialized, and very prominent structure, consisting of nine fibers surrounding the axoneme. The ODF may play an important but as yet undefined role in sperm morphology, integrity and function. Study of the ODF is hampered by insufficient knowledge of their protein composition and the genetic regulation of their synthesis. We report here on the characterization of cDNAs encoding the Odf2 proteins of outer dense fibers of mouse sperm. We isolated two cDNA clones with variable 5' regions. Variability in sequence is restricted to specific regions in the N-terminal part of the encoded proteins, whereas the C-terminal part is highly conserved in Odf2 proteins both between species and within a species. This variability is confirmed at the protein level. The outer dense fibers could be detected immunologically in total sperm tails allowing a direct comparison of their length in relation to the length of the sperm tail. Odf2 transcripts could be demonstrated in testicular RNA and are restricted to germ cells. The start of transcription is in step 5 spermatids of tubular stage V and the RNA could be detected in the cytoplasm of differentiating spermatids in all subsequent tubular stages.

Amino Acid Sequence↗
PubMed2003

Speract induces calcium oscillations in the sperm tail.

Sea urchin sperm motility is modulated by sperm-activating peptides. One such peptide, speract, induces changes in intracellular free calcium concentration ([Ca2+]i). High resolution imaging of single sperm reveals that speract-induced changes in [Ca2+]i have a complex spatiotemporal structure. [Ca2+]i increases arise in the tail as periodic oscillations; [Ca2+]i increases in the sperm head lag those in the tail and appear to result from the summation of the tail signal transduction events. The period depends on speract concentration. Infrequent spontaneous [Ca2+]i transients were also seen in the tail of unstimulated sperm, again with the head lagging the tail. Speract-induced fluctuations were sensitive to membrane potential and calcium channel blockers, and were potentiated by niflumic acid, an anion channel blocker. 3-isobutyl-1-methylxanthine, which potentiates the cGMP/cAMP-signaling pathways, abolished the [Ca2+]i fluctuations in the tail, leading to a very delayed and sustained [Ca2+]i increase in the head. These data point to a model in which a messenger generated periodically in the tail diffuses to the head. Sperm are highly polarized cells. Our results indicate that a clear understanding of the link between [Ca2+]i and sperm motility will only be gained by analysis of [Ca2+]i signals at the level of the single sperm.

1-Methyl-3-isobutylxanthine↗
PubMed1999

Outer dense fibre proteins from human sperm tail: molecular cloning and expression analyses of two cDNA transcripts encoding proteins of approximately 70 kDa.

The outer dense fibres (ODF) are a main cytoskeletal structure of the sperm tail. Despite their importance in the morphology and function of the sperm tail, their constituents are poorly described. Here we investigate the protein composition of human outer dense fibres. Our results suggest that human ODF consist of about 10 major and of at least 15 minor proteins, where all major proteins are ODF1, ODF2 or ODF2-related proteins. From a human testis cDNA library, we isolated two slightly different cDNAs encoding ODF2 proteins of approximately 70 kDa. Human ODF2 cDNAs and their encoded proteins are very similar to those isolated from rat and mouse pointing to a high evolutionary pressure residing on these proteins. Transcription of ODF2 is restricted to testis tissue and more specifically to round spermatids as was demonstrated by a non-radioactive in-situ hybridization. ODF2 proteins were detected in the sperm tail. Their distribution along the length of the sperm tail shows that the ODF normally extend to about half the principal piece of the sperm tail. The former result opens the possibility for a screening regarding the distribution of sperm tail proteins related to motility disorders.

Amino Acid Sequence↗
PubMed1965

Effect of adenosine triphosphate on Perca fluviatilis sperm tails isolated in buffered sucrose.

1. Sperm tails were isolated from mechanically disrupted spermatozoa of Perca fluviatilis and suspended in buffered sucrose solution. When freshly prepared suspensions were treated with ATP and magnesium chloride and centrifugal pellets obtained these weighed up to about 40% heavier than controls. 2. The effect is closely linked to the enzymic splitting of ATP and under conditions where this was inhibited no increase in weight was observed. Pellets from suspensions aged overnight at 2 degrees and then treated with ATP and magnesium chloride were no heavier than the controls although the suspensions had undiminished enzymic activity. Sperm tails from Salmo trutta did not show the effect. 3. Analyses showed that the weight increases were the result of uptake of sucrose solution and that sucrose completely penetrated the pellet water. Polyethylene glycol (mol.wt. 4000) did not penetrate the water of the pellets completely and an amount approximately equal to 1.9 times the flagellar dry weight was inaccessible. 4. Electron-microscopic studies indicated that the effect is the result of tail disintegration.

Adenosine Triphosphate↗