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Effects of cryopreservation on sperm parameters and ultrastructural morphology of human spermatozoa.

ABSTRACT: PURPOSE: Cryopreservation of sperm is a widely used technique to maintain and protect the fertility in various occasions such as infertility and malignancy treatments. This study aims to reveal the effects of freezing and thawing on human spermatozoa. MATERIALS AND METHODS: To evaluate the effects of freeze-thawing, semen samples were evaluated by light microscopy by means of morphology, motility and viability, by scanning and transmission electron microscopy for detailed ultrastructural changes. RESULTS: After cryopreservation, a significant decrease in spermatozoa viability was observed (p < 0.01). Group a, b and c motility according to World Health Organization criteria decreased considerably (p < 0.05, p < 0.01, p < 0.05, respectively), whereas there was a substantial increase in group d motility. A strong correlation between rise in number of immotile spermatozoa and decrease in viability was also noted (r = -0.848, p < 0.01). Post-thaw light microscopic studies revealed a considerable decrease in rate of normal spermatozoa (p < 0.05). A considerable decline in the rate of normal sperm was also observed by TEM (p < 0.05). Statistically, acrosomal changes and subacrosomal swelling were found to be significantly increased (both p < 0.05), where the latter appears to be a novel finding in literature. CONCLUSION: Cryopreservation has deleterious effects on spermatozoa, especially on plasmalemma, acrosomes and tails. Electron microscopy is the ultimate modality to investigate spermatogenic cells.

SUBMITTER: Ozkavukcu S

PROVIDER: S-EPMC2582121 | biostudies-other | 2008 Aug

REPOSITORIES: biostudies-other

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Project description:Male infertility is a medical condition that has been on the rise globally. Lysine acetylation of human sperm, an essential posttranslational modification involved in the etiology of sperm abnormality, is not fully understood. Therefore, we first generated a qualified pan-anti-acetyllysine monoclonal antibody to characterize the global lysine acetylation of uncapacitated normal human sperm with a proteomics approach. With high enrichment ratios that were up to 31%, 973 lysine-acetylated sites that matched to 456 human sperm proteins, including 671 novel lysine acetylation sites and 205 novel lysine-acetylated proteins, were identified. These proteins exhibited conserved motifs XXXKYXXX, XXXKFXXX, and XXXKHXXX, were annotated to function in multiple metabolic processes, and were localized predominantly in the mitochondrion and cytoplasmic fractions. Between the uncapacitated and capacitated sperm, different acetylation profiles in regard to functional proteins involved in sperm capacitation, sperm-egg recognition, sperm-egg plasma fusion, and fertilization were observed, indicating that acetylation of functional proteins may be required during sperm capacitation. Bioinformatics analysis revealed association of acetylated proteins with diseases and drugs. Novel acetylation of voltage-dependent anion channel proteins was also found. With clinical sperm samples, we observed differed lysine acetyltransferases and lysine deacetylases expression between normal sperm and abnormal sperm of asthenospermia or necrospermia. Furthermore, with sperm samples impaired by epigallocatechin gallate to mimic asthenospermia, we observed that inhibition of sperm motility was partly through the blockade of voltage-dependent anion channel 2 Lys-74 acetylation combined with reduced ATP levels and mitochondrial membrane potential. Taken together, we obtained a qualified pan-anti-acetyllysine monoclonal antibody, analyzed the acetylproteome of uncapacitated human sperm, and revealed associations between functional protein acetylation and sperm functions.

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Effects of cryopreservation on sperm parameters and ultrastructural morphology of human spermatozoa.

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