Impaired ability of human spermatozoa to penetrate zona‐free hamster oocytes: Is a postacrosomal sheath anomaly involved?

Courtot, Anne-Marie; Escalier, Denise; Jouannet, Pierre; David, G

doi:10.1002/mrd.1120170206

Cited by 13 publications

(9 citation statements)

References 22 publications

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“…In fact, several investigations examining the pathology of infertile acrosomeless sperm have noted the conspicuous absence of the perinuclear theca and/or perinuclear theca proteins (i.e., calicin) during development [27][28][29]. Since we have shown that a 60-kDa polypeptide (presumably calicin) underlies the acrosome, the finding that calicin is absent during "acrosomeless development" [28,29] strengthens the idea that its presence is necessary for acrosome attachment.…”

Section: Protein Composition Of the Bull Perinuclear Thecasupporting

confidence: 73%

Protein Composition of the Perinuclear Theca of Bull Spermatozoa1

Oko

Maravei

1994

Biology of Reproduction

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The perinuclear theca is a cytoskeletal structure that covers the nucleus of mammalian spermatozoa except for a narrow zone around the insertion of the tail. It shows two distinct regions, a subacrosomal layer or perforatorium and, continuing caudally beyond the acrosomic system, the postacrosomal sheath. The main objective of this study was to analyze the protein composition of the bull perinuclear theca and the distribution of some of its proteins. The perinuclear theca was extracted from demembranated and acrosome-depleted sperm heads by alkaline treatment. Gel electrophoresis revealed that the extract was composed of over 20 polypeptide bands, of which the 15.5-, 25-, 28-, 32-, 36-, and 60-kDa bands were most prominent. Polyclonal antibodies prepared against these major polypeptides were screened on Western blots of the theca extracts and were immunolocalized on sections of spermatozoa prepared for electron microscopy. Antibodies against the 15.5- and 60-kDa polypeptides reacted monospecifically with their respective bands on Western blots, and immunogold labeled the perforatorium and the entire perinuclear theca, respectively. Antibodies against the 25-, 28-, 32-, and 36-kDa polypeptides showed distinctive patterns of cross-reactivity with other polypeptides on Western blots, but immunogold labeled exclusively the entire perinuclear theca. In conclusion, this study provides evidence that the protein composition of the bull perinuclear theca is complex: at least six major polypeptides make up this cytoskeletal element. As to their distribution, the 15.5-kDa polypeptide is localized exclusively to the subacrosomal layer, and the other five major polypeptides analyzed in this study appear to be shared between the subacrosomal and post-acrosomal regions of the perinuclear theca.

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Section: Protein Composition Of the Bull Perinuclear Thecasupporting

confidence: 73%

Protein Composition of the Perinuclear Theca of Bull Spermatozoa1

Oko

Maravei

1994

Biology of Reproduction

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“…This suggested that sperm with high concentrations of retained CK and cytoplasmic proteins have failed to complete cellular maturation, with a consequential impairment of various functions, including fertilization potential. Considering that elevated CK activity, higher intensity of CK staining, and increased size and roundness and abnormal morphology of the sperm head are all related to the incomplete extrusion of the cytoplasm, one can now understand the relationship between abnormal sperm morphology and diminished fertility in man (Courtot et al, 1987;Freund, 1966;Zamboni, 1987). The two major morphologic features that classically signify diminished fertility, round sperm heads and amorph sperm heads, showed the most intense CK staining (Fig.…”

Section: Discussionmentioning

confidence: 98%

Incomplete development of human spermatozoa is associated with increased creatine phosphokinase concentration and abnormal head morphology

Huszár

Vigue

1993

Molecular Reproduction Devel

129

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Our previous creatine phosphokinase (CK) activity studies in human sperm revealed differences among men and among sperm populations within the same specimen. Samples with low sperm concentrations, high incidence of abnormal sperm morphology, and diminished fertility had higher per sperm CK activity. In the present work, we demonstrated, with 14C-FDNB covalent CK active site modification and with direct CK immunocytochemistry, that the higher CK activity is related to an increased content of CK and of other proteins in sperm. Also, sperm heads with higher CK content were significantly larger and rounder and showed a higher incidence of amorph configuration. We suggest that these biochemical and morphological irregularities are related and are due to a failure of spermatogenesis, more specifically, to a higher retention of cytoplasm, which in normal sperm development is lost to the Sertoli cells as residual bodies. Thus higher CK activity and larger or irregular head size in human sperm signify cellular immaturity and a failure to complete spermatogenesis.

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“…Considering the testicular specificity of PERF 15, it is probable that genetic assays designed to "knock out" this protein in the mouse will provide useful information on the function of PT proteins during acrosome formation and fertilization. Development of such a mouse model could aid in the explanation for the failure of acrosome-nuclear attachment, a documented cause in some cases of human infertility [20][21][22].…”

Section: Discussionmentioning

confidence: 99%

Analysis of the Protein Composition of the Mouse Sperm Perinuclear Theca and Characterization of its Major Protein Constituent1

Korley

Pouresmaeili

Oko

1997

Biology of Reproduction

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The perinuclear theca (PT) is a cytoskeletal structure that covers the nucleus of mammalian spermatozoa and is believed to have a membrane-binding role. The objectives of this study were to analyze the protein composition of the mouse PT, to identify and sequence its major protein component, and to characterize this protein's transcriptional and translational origins during spermatogenesis. The PT was extracted from demembranated and acrosome-depleted mouse sperm heads by alkaline treatment. The protein profile of the PT extract was composed of several polypeptides, of which a 15-kDa subacrosomal protein predominated and was found to be immunocross-reactive with a previously cloned 15-kDa PT protein of the rat (PERF 15) that belongs to a family of lipid-binding proteins. A primer pair designed from rat PERF 15 cDNA was then used to screen a mouse testicular cDNA library by polymerase chain reaction (PCR). The deduced amino acid sequence obtained from the PCR product was almost identical to the testicular-specific rat PERF 15. Developmental Northern blots and in situ hybridization studies performed with riboprobes encoding the mouse PERF 15 cDNA revealed that mRNA levels were highest in round and early elongating mouse spermatids. Immunohistochemistry indicated that PERF 15 began to be expressed in the cytoplasm of mid-pachytene spermatocytes and appeared to reach maximum expression in the distal cytoplasm of late elongating mouse spermatids, long after transcriptional arrest. During the development of round and early elongated spermatids, the immunolabel became progressively concentrated over the anterior half of the spermatid nucleus, suggesting a subacrosomal deposition of PERF 15 during this phase of mouse spermiogenesis.

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Impaired ability of human spermatozoa to penetrate zona‐free hamster oocytes: Is a postacrosomal sheath anomaly involved?

Cited by 13 publications

References 22 publications

Protein Composition of the Perinuclear Theca of Bull Spermatozoa1

Protein Composition of the Perinuclear Theca of Bull Spermatozoa1

Incomplete development of human spermatozoa is associated with increased creatine phosphokinase concentration and abnormal head morphology

Analysis of the Protein Composition of the Mouse Sperm Perinuclear Theca and Characterization of its Major Protein Constituent1

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