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Biomedical subjects

U Kvist

Publications and source records attributed to U Kvist.

At least 37 records · Page 2Linked to original sources
PubMed1990

Changes in human sperm chromatin stability during preparation for in-vitro fertilization.

This study was designed to define the effects of sperm preparation on sperm chromatin stability in relation to in-vitro fertilization (IVF). Semen samples used for IVF-embryo transfer (ET) in the treatment of infertility due to tubal factors were studied. Cases with semen variables below reference limits in previous samples were excluded. Sperm were prepared by a swim-up technique employing either of two different tissue culture media, Ham's F-10 or Earle's balanced salt solution. Sperm chromatin stability was tested by exposure both to sodium dodecyl sulphate (SDS) only and SDS together with a zinc-chelating agent, disodium ethylene diamine tetraacetate (SDS-EDTA). Sperm head swell scores were defined under different experimental conditions and the relationship to sperm motility, morphology, fertilization rate and pregnancy occurrence was tested. No differences were seen between the chromatin stability of sperm from the original sample and that after swim-up preparation, neither immediately after completion of the swim-up procedure, nor at the time of insemination of ova. With time, the chromatin became more stable, which occurred to a similar extent both in the original sample and in swim-up preparations using Ham's F-10. Otherwise, sperm chromatin stability was unaffected by either of the two media used for swim-up. At higher incubation temperatures, decondensation in SDS was enhanced. Altogether, no correlation was found between sperm chromatin stability or enhancement of decondensation by temperature and the success of IVF treatment expressed in fertilization rates or pregnancies. The results are reassuring in that only small changes in sperm chromatin stability occurred during the preparation for IVF. As long as semen of presumably good quality is used, these changes in chromatin stability do not seem to be of clinical importance.

Chromatin↗
PubMed1990

Immunocytochemical localization of nuclear protamine in boar spermatozoa during epididymal transit.

Protamine was specifically demonstrated in boar spermatozoa collected from the rete testis, caput, corpus and cauda epididymidis and the ejaculate by immunoelectron microscopy, using anti-boar or anti-ram protamine antisera and an indirect post-embedding immunogold technique. Spermatozoa from all collection sites stained after incubation although with different degrees of labelling. Controls were negative. Labelling increased from the rete testis towards the epididymal corpus, where it was most intense, decreasing sharply thereafter. The weakest binding of the assayed antibodies was obtained in the ejaculated spermatozoa but it could be reversed by in-vitro induction of chromatin decondensation with sodium dodecyl sulphate and the metal-chelating EDTA. The finding of a significant decrease in the immunolabelling detected from the corpus epididymidis onwards indicates a critical point for the interaction between DNA and the protamines in boar spermatozoa during the epididymal maturation.

Animals↗
PubMed1989

Testicular atrophy and loss of nerve growth factor-immunoreactive germ cell line in rats exposed to n-hexane and a protective effect of simultaneous exposure to toluene or xylene.

Testicular and germ cell line morphology in rats were studied 2 weeks, 10 months and 14 months after cessation of a 61-day inhalation exposure to 1000 ppm n-hexane. Androgen biosynthetic capacity of testis, testosterone blood concentration, vas deferens morphology and noradrenaline (NA) concentration, epididymal sperm morphology, and fertility were also studied. Severe testicular atrophy involving the seminiferous tubules with loss of the nerve growth factor (NGF) immunoreactive germ cell line was found. Total loss of the germ cell line was found in a fraction of animals up to 14 months post-exposure, indicating permanent testicular damage. No impairment of androgen synthesis or androgen dependent accessory organs was observed. Simultaneous administration of 1000 ppm n-hexane and 1000 ppm toluene, or 1000 ppm n-hexane and 1000 ppm xylene, did not cause germ cell line alterations or testicular atrophy. Toluene and xylene were thus found to protect from n-hexane induced testicular atrophy.

Animals↗
PubMed1988

Biochemical characterization of prostaglandin 19-hydroxylase of seminal vesicles.

The microsomal fraction of homogenates of seminal vesicles of men and monkeys, Macaca fascicularis, were analyzed for prostaglandin (PG) 19-hydroxylase activity. The microsomes of the monkey seminal vesicles, supplemented with 1 mM NADPH, metabolized 0.2 mM PGE1 to 19-hydroxy-PGE1 at a mean rate of 0.26 nmol/min/mg of protein (with an apparent Km and an apparent Vmax of 40 microM and 0.30 nmol/min/mg of protein, respectively). The enzyme catalyzed the incorporation of atmospheric oxygen into the substrate. Substituting NADH for NADPH reduced the prostaglandin E1 19-hydroxylase activity to 40%. Carbon monoxide and proadifen (SKF 525A) inhibited the enzyme. Prostaglandin E2 (0.2 mM) was metabolized to 19-hydroxyprostaglandin E2 (0.2 nmol/min/mg of protein), but PGE1 was preferred as a substrate. Prostaglandin B1 was metabolized to 18-hydroxy-, 19-hydroxy-, and 20-hydroxyprostaglandin B1 at a combined rate of approximately 25% of prostaglandin E1. 19-Hydroxyprostaglandin B1 was the main product. The microsomes of human seminal vesicles metabolized 0.2 mM PGE2 to 19-hydroxy-PGE2 in the presence of 1 mM NADPH, while carbon monoxide inhibited this reaction. These results suggest that prostaglandin 19-hydroxylase of seminal vesicles might be a cytochrome P-450. The biosynthesis of 19-hydroxyprostaglandin E1 and 19-hydroxyprostaglandin E2 was also studied in vivo in man by analysis of the product/substrate ratios (i.e. 19-hydroxyprostaglandin E1/prostaglandin E1 and 19-hydroxyprostaglandin E2/prostaglandin E2) in a series of consecutive ejaculates, which were obtained during short intervals. There was a 10-fold interindividual difference in these ratios. Although the product/substrate ratios decreased, the 19-hydroxylation of E prostaglandins appeared to be efficient in vivo, which was in contrast to the rather slow biosynthesis in vitro.

Animals↗
PubMed1988

Zinc in sperm chromatin and chromatin stability in fertile men and men in barren unions.

The stability and the content of zinc of the chromatin were studied in spermatozoa from ten men with unexplained infertility, and in spermatozoa from five fertile donors. A positive relation was found between zinc in sperm nuclei (X-ray microanalysis) and the resistance of the chromatin to decondense in sodium dodecylsulfate (SDS). The infertile men had lower degree of sperm chromatin stability and lower sperm zinc content than the fertile donors. A subgroup of the infertile men, which all had minor clinical signs of prostatic inflammatory reaction, had the lowest content of zinc in the chromatin and the lowest degree of chromatin stability. A low content of nuclear zinc would impair the structural stability of the chromatin and thereby increase the vulnerability of the male genome. This mechanism may be one explanation for the reduced fertility of the men with minor inflammation of the prostate.

Chromatin↗
PubMed1988

Anatomy of the prostate. Aspects of the secretory function in relation to lobar structure.

Anatomic studies have shown the prostate to be a heterogeneous organ in which at least three morphologically differing zones or lobes are identifiable. This indicates that the endocrinologic sensitivity of the prostate is not uniform, and that there may also be intraprostatic functional variations. Few studies have so far been done to prove such differences. Although interlobar differences in zinc content have been observed, their significance is not clear. The field is therefore open for further studies concerning both the anatomic and the functional heterogeneity of the human prostate.

Body Fluids↗
PubMed1987

Cadmium interacts with the zinc-dependent stability of the human sperm chromatin.

Zinc normally participates in the stabilization of the chromatin of human spermatozoa, which have a high content of zinc after ejaculation. Sperm chromatin, depleted of zinc with EDTA, regained stability in the detergent SDS after exposure to Cd2+ in vitro. This effect was reversible with EDTA, but albumin could not reverse the stabilization caused by Cd2+ to the same extent as it reversed the stabilization caused by Zn2+.

Cadmium↗
PubMed1987

Sperm nuclear zinc, chromatin stability, and male fertility.

Zinc excreted from the human prostate secures a high content of zinc in the sperm nucleus and contributes to the stability of the quaternary structure of the chromatin. After ejaculation, in vitro, a second type of stability, most probably involving disulfide-bridge crosslinks, supersedes the zinc-dependent stability. Normally, the nucleus of the ejaculated spermatozoon remains stable, i.e., it does not decondense when exposed to a detergent (e.g., sodium dodecyl sulfate - SDS), whereas a spermatozoon which has been exposed to a zinc-chelating medium becomes destabilized and decondenses in SDS. Spontaneous decondensation in SDS, i.e., without prior treatment with zinc-chelators, occurs among many spermatozoa from some infertile men, especially men with impaired secretory function of the prostate. This indicates that spontaneously decondensing spermatozoa have an inadequate content of zinc at ejaculation. Here, zinc in the sperm nucleus and chromatin stability was studied in semen samples from a group of men living in marriages with hitherto unexplained cause for infertility, and a group of fertile donors, who participated in an insemination program. Sperm nuclear zinc was studied with X-ray microanalysis and chromatin stability was assessed as percentage spermatozoa with stable sperm heads after exposure to SDS. Fertile donors had higher content of zinc in the sperm nuclei and had also higher proportions spermatozoa with a stabilized chromatin, than had the men living in infertile marriages.(ABSTRACT TRUNCATED AT 250 WORDS)

Cell Nucleus↗
PubMed1986

The human sperm nucleus takes up zinc at ejaculation.

Ejaculated and vasal sperm were obtained from men referred for vasectomy, and sperm nuclear elements were determined by X-ray microanalysis. Sperm head zinc concentrations, expressed as the ratio Zinc to Sulphur, were significantly higher in ejaculated than in vasal sperm. A physiological sperm nuclear zinc uptake is discussed in relation to sperm chromatin decondensation.

Adult↗
PubMed1985

Loss of an intrinsic capacity for human sperm chromatin decondensation.

Chromatin decondensation of human ejaculated spermatozoa was studied in vitro, at various points of time after ejaculation, by sperm exposure to the detergent sodium dodecyl sulphate (SDS) containing zinc chelating EDTA. Within 5 min after ejaculation EDTA revealed a capacity for decondensation in 90% of the spermatozoa. This sperm capacity decreased rapidly upon storage. The results support the concept that the capacity to decondense is a normal property of freshly ejaculated spermatozoa and that this property may be rapidly lost. The loss is most probably due to an inability of thiol groups to take part in a thiol-disulphide exchange in the sperm chromatin. A loss of functional thiols may hinder a capacity for chromatin decondensation inherent to the spermatozoon. A loss of thiols due to oxidation, that is, surplus S-S bridge formation, may also delay hypothetical extrinsic S-S cleaving factors in the ooplasm. In either case, the complete and non-delayed sperm chromatin decondensation in the ovum may be hindered. This may result in the abnormal embryonic development observed in ova fertilized with aged spermatozoa.

Chromatin↗
PubMed1985

Zinc preserves an inherent capacity for human sperm chromatin decondensation.

The effect of zinc on the nuclear chromatin decondensation ability of human, ejaculated spermatozoa was studied by exposing washed spermatozoa to the detergent sodium dodecyl sulphate (SDS) before and after sperm storage. Treatment with EDTA increased the proportion of decondensing spermatozoa before storage. Zinc supplementation before storage reversibly inhibited spontaneous decondensation as well as EDTA-enhanced decondensation. Treatment with EDTA before storage decreased the proportion of spermatozoa decondensing after storage. Zinc supplementation during storage reduced the decrease in the proportion of spermatozoa decondensing after storage. Two effects of zinc were observed: one immediate effect (reversible inhibition of the decondensation) and one long-term effect (protection of the intrinsic capacity for decondensation during storage). Both effects may be explained by a zinc-thiol interaction in the chromatin. Spermatozoal zinc is suggested to protect an inherent capacity for decondensation, thereby helping to extend the functional life-span of the ejaculated spermatozoon.

Chromatin↗
PubMed1985

Nuclear zinc in human epididymal and ejaculated spermatozoa.

Sperm nuclear zinc content (expressed as zinc/phosphorus and zinc/sulphur ratios) was determined with X-ray microanalysis in individual, air-dried, epididymal spermatozoa from elderly men, and in ejaculated spermatozoa from healthy donors. Ejaculated sperm nuclei contained (also after treatment with sodium dodecyl sulphate) more zinc than epididymal spermatozoa. The results indicate that the human spermatozoon accumulates zinc from the prostatic fluid upon ejaculation.

Adult↗
PubMed1982

Removal of zinc from subcellular regions of human spermatozoa by EDTA treatment studied by X-ray microanalysis.

The distribution of zinc in the head, neck and mid-piece of human ejaculated spermatozoa was investigated with energy-dispersive X-ray microanalysis. EDTA treatment within 1 h after ejaculation caused removal of 80-90% of the zinc in these regions. Storage for 24 h in own seminal plasma did not alter sperm zinc content. However, these aged spermatozoa only lost 35% of their zinc content on EDTA treatment. The stronger binding of zinc, occurring upon storage in seminal plasma, developed in all 3 parts of the cell investigated. These results are discussed in the light of the role of zinc in nuclear chromatin decondensation ability and sperm head-tail connection.

Edetic Acid↗
PubMed1982

Importance of zinc for human sperm head-tail connection.

Head-tail detachment of ejaculated human spermatozoa was studied with phase contrast microscopy. The frequency of head-tail detachment was assessed after sperm exposure to the anionic detergent sodium dodecyl sulfate (SDS) for 60 min at 22 degrees C. Decapitation was enhanced by EDTA. Zinc reversibly inhibited native as well as EDTA induced head-tail disconnection. Still a certain proportion of spermatozoa were resistant to EDTA-treatment and this proportion significantly increased upon 24 h of saline storage. The development of EDTA resistance was enhanced by EDTA treatment before storage. A physiological role for zinc as a preserver of an inherent mechanism for head-tail detachment is suggested.

Chromatin↗
PubMed1980

Influence of seminal plasma on the chromatin stability of ejaculated human spermatozoa.

Nuclear chromatin decondensation (NCD) of human ejaculated spermatozoa exposed to sodium dodecyl sulphate (SDS) has been studied. A high proportion of NCD reacting spermatozoa was only found in semen samples with a relatively low activity of some prostatic factor(s) (i.e. zinc/fructose ratio below 0.18) in the seminal plasma. Exposure to SDS for one h was found sufficient to reveal the main proportion of spermatozoa undergoing NCD in such a solution. Addition of seminal plasma with an apparently normal composition to a sperm population with a high NCD reactivity restored the sperm SDS resistance to normal, i.e. blocked the NCD-response. Other results indicated that NCD reactivity was decreased or abolished upon prolonged storage of the spermatozoa in the seminal plasma. The various results indicated that some factor(s) in the seminal plasma can preserve the nuclear chromatin stability of human spermatozoa and that this factor most likely is of prostatic origin.

Humans↗