Binding of 125I-prolactin to spermatozoa from normospermic and asthenospermic men
Scatchard analysis of prolactin binding sites (PRL-BS) from ejaculated spermatozoa showed a single population of binding sites (apparent association constant: 2.51 ± 0.186 nmol/l-1) with 0.317 ± 0.0743 fmol/106 sperm binding sites. Different pools of spermatozoa were incubated with increasing concen...
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todo:paper_03914097_v20_n11_p635_Luthy2023-10-03T15:33:48Z Binding of 125I-prolactin to spermatozoa from normospermic and asthenospermic men Luthy, I.A. Mormandi, E. Aszpis, S. Vázquez, S.M. Maccallini, G. Levalle, O. Calandra, R.S. Asthenospermic Normospermic Prolactin receptor Reproduction Spermatozoa human growth hormone iodine 125 prolactin recombinant follitropin tetracosactide corticotropin diagnostic agent follitropin human growth hormone prolactin radioactive iodine article asthenospermia binding site clinical article controlled study hormone binding human human cell male Scatchard plot seminal plasma spermatozoon animal binding competition chemistry cohort analysis comparative study male infertility metabolism pathology sheep sperm spermatozoon Adrenocorticotropic Hormone Animals Binding Sites Binding, Competitive Cohort Studies Follicle Stimulating Hormone Human Growth Hormone Humans Infertility, Male Iodine Radioisotopes Male Prolactin Semen Sheep Spermatozoa Scatchard analysis of prolactin binding sites (PRL-BS) from ejaculated spermatozoa showed a single population of binding sites (apparent association constant: 2.51 ± 0.186 nmol/l-1) with 0.317 ± 0.0743 fmol/106 sperm binding sites. Different pools of spermatozoa were incubated with increasing concentrations of several hormones. There was a decrease in [125I]-oPRL binding with purified ovine prolactin (oPRL) and human growth hormone (hGH) which was not observed in the presence of synthetic ACTH and recombinant FSH, suggesting that binding was hormone specific. When the patient's samples were analyzed using the single point assay at saturation concentration, asthenospermic patients showed significantly higher concentration of binding sites compared to normospermic ones. Both groups of patients displayed similar PRL levels in seminal plasma measured by DELFIA. Moreover, individual values of PRL levels in seminal plasma did not correlate with PRL-BS concentrations. We thus conclude that [125I]-oPRL binding to ejaculated spermatozoa was hormone specific and with similar parameters as seen in other target tissues. PRL-BS concentration in asthenospermic patients was significantly higher than in normospermic but this was not due to different levels of PRL in seminal plasma. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03914097_v20_n11_p635_Luthy |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Asthenospermic Normospermic Prolactin receptor Reproduction Spermatozoa human growth hormone iodine 125 prolactin recombinant follitropin tetracosactide corticotropin diagnostic agent follitropin human growth hormone prolactin radioactive iodine article asthenospermia binding site clinical article controlled study hormone binding human human cell male Scatchard plot seminal plasma spermatozoon animal binding competition chemistry cohort analysis comparative study male infertility metabolism pathology sheep sperm spermatozoon Adrenocorticotropic Hormone Animals Binding Sites Binding, Competitive Cohort Studies Follicle Stimulating Hormone Human Growth Hormone Humans Infertility, Male Iodine Radioisotopes Male Prolactin Semen Sheep Spermatozoa |
spellingShingle |
Asthenospermic Normospermic Prolactin receptor Reproduction Spermatozoa human growth hormone iodine 125 prolactin recombinant follitropin tetracosactide corticotropin diagnostic agent follitropin human growth hormone prolactin radioactive iodine article asthenospermia binding site clinical article controlled study hormone binding human human cell male Scatchard plot seminal plasma spermatozoon animal binding competition chemistry cohort analysis comparative study male infertility metabolism pathology sheep sperm spermatozoon Adrenocorticotropic Hormone Animals Binding Sites Binding, Competitive Cohort Studies Follicle Stimulating Hormone Human Growth Hormone Humans Infertility, Male Iodine Radioisotopes Male Prolactin Semen Sheep Spermatozoa Luthy, I.A. Mormandi, E. Aszpis, S. Vázquez, S.M. Maccallini, G. Levalle, O. Calandra, R.S. Binding of 125I-prolactin to spermatozoa from normospermic and asthenospermic men |
topic_facet |
Asthenospermic Normospermic Prolactin receptor Reproduction Spermatozoa human growth hormone iodine 125 prolactin recombinant follitropin tetracosactide corticotropin diagnostic agent follitropin human growth hormone prolactin radioactive iodine article asthenospermia binding site clinical article controlled study hormone binding human human cell male Scatchard plot seminal plasma spermatozoon animal binding competition chemistry cohort analysis comparative study male infertility metabolism pathology sheep sperm spermatozoon Adrenocorticotropic Hormone Animals Binding Sites Binding, Competitive Cohort Studies Follicle Stimulating Hormone Human Growth Hormone Humans Infertility, Male Iodine Radioisotopes Male Prolactin Semen Sheep Spermatozoa |
description |
Scatchard analysis of prolactin binding sites (PRL-BS) from ejaculated spermatozoa showed a single population of binding sites (apparent association constant: 2.51 ± 0.186 nmol/l-1) with 0.317 ± 0.0743 fmol/106 sperm binding sites. Different pools of spermatozoa were incubated with increasing concentrations of several hormones. There was a decrease in [125I]-oPRL binding with purified ovine prolactin (oPRL) and human growth hormone (hGH) which was not observed in the presence of synthetic ACTH and recombinant FSH, suggesting that binding was hormone specific. When the patient's samples were analyzed using the single point assay at saturation concentration, asthenospermic patients showed significantly higher concentration of binding sites compared to normospermic ones. Both groups of patients displayed similar PRL levels in seminal plasma measured by DELFIA. Moreover, individual values of PRL levels in seminal plasma did not correlate with PRL-BS concentrations. We thus conclude that [125I]-oPRL binding to ejaculated spermatozoa was hormone specific and with similar parameters as seen in other target tissues. PRL-BS concentration in asthenospermic patients was significantly higher than in normospermic but this was not due to different levels of PRL in seminal plasma. |
format |
JOUR |
author |
Luthy, I.A. Mormandi, E. Aszpis, S. Vázquez, S.M. Maccallini, G. Levalle, O. Calandra, R.S. |
author_facet |
Luthy, I.A. Mormandi, E. Aszpis, S. Vázquez, S.M. Maccallini, G. Levalle, O. Calandra, R.S. |
author_sort |
Luthy, I.A. |
title |
Binding of 125I-prolactin to spermatozoa from normospermic and asthenospermic men |
title_short |
Binding of 125I-prolactin to spermatozoa from normospermic and asthenospermic men |
title_full |
Binding of 125I-prolactin to spermatozoa from normospermic and asthenospermic men |
title_fullStr |
Binding of 125I-prolactin to spermatozoa from normospermic and asthenospermic men |
title_full_unstemmed |
Binding of 125I-prolactin to spermatozoa from normospermic and asthenospermic men |
title_sort |
binding of 125i-prolactin to spermatozoa from normospermic and asthenospermic men |
url |
http://hdl.handle.net/20.500.12110/paper_03914097_v20_n11_p635_Luthy |
work_keys_str_mv |
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