Steroid receptors in human spermatozoa

Revelli, Alberto; Modotti, M.; Piffaretti-Yanez, A.; Massobrio, M; Balerna, M.

doi:10.1093/oxfordjournals.humrep.a138592

Cited by 52 publications

(23 citation statements)

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“…The presence of significant transcript levels of mPR␣ in the human testis, ovary, and placenta suggests it is the major subtype mediating the rapid, nongenomic actions of progesterone in reproductive tissues. There is considerable evidence that progesterone has rapid actions on human sperm to induce hyperactivity and the acrosome reaction by binding to an mPR (27,28). Similarly, an mPR previously characterized biochemically on sperm in spotted seatrout is likely the intermediary in the rapid actions of progestins to increase sperm motility and fertilization success in this species (29).…”

Section: Discussionmentioning

confidence: 96%

Identification, classification, and partial characterization of genes in humans and other vertebrates homologous to a fish membrane progestin receptor

Zhu

Bond

Thomas

2003

Proc. Natl. Acad. Sci. U.S.A.

645

470

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Recently we discovered a previously uncharacterized gene with the characteristics of a membrane progestin receptor (mPR) in a fish model, spotted seatrout. Here, we report the identification, cloning, and characteristics of other members of this hitherto unknown family of putative mPRs from several vertebrate species, including human, mouse, pig, Xenopus, zebrafish, and Fugu, with highly conserved nucleotide and deduced amino acid sequences and similar structures to the spotted seatrout mPR. The 13 vertebrate genes identified seem to belong to an unknown gene family. Phylogenetic analysis indicates these cDNAs comprise three distinct groups (named ␣, ␤, and ␥) within this gene family. Structural analyses of the translated cDNAs suggest they encode membrane proteins with seven transmembrane domains. The transcript sizes of the human ␣, ␤, and ␥ putative mPR mRNAs varied from 2.8 to 5.8 kb and showed distinct distributions in reproductive, neural, kidney and intestinal tissues, respectively. Recombinant human ␣, ␥, and mouse ␤ proteins produced in an Escherichia coli expression system demonstrated high affinity (Kd ‫؍‬ 20 -30 nM) saturable binding for progesterone. Further analysis of binding to the ␥-subtype revealed binding was specific for progestins and was displaceable, with rapid rates of association and dissociation (t1/2 ‫؍‬ 2-8 min). These results suggest this is a new family of steroid receptors unrelated to nuclear steroid receptors, but instead having characteristics of G protein-coupled receptors.A lthough the existence of specific receptors on the surface of target cells mediating rapid nongenomic actions of steroids was recognized 20 years ago (1, 2), efforts to determine the structures of steroid membrane receptors have been unsuccessful until now (3-5). In the accompanying paper in this issue of PNAS (6), we described a gene discovered in a teleost species, spotted seatrout, whose protein fulfils the criteria for its designation as a steroid membrane receptor, including structural plausibility, specific tissue and plasma membrane localization, steroid binding characteristic of steroid and progestin receptors, coupling to second messenger pathways, regulation by steroid hormones, and biological relevance. Evidence was obtained that this progestin membrane receptor (mPR) is the intermediary in progestin induction of oocyte meiotic maturation in teleost fishes and activates an inhibitory G protein (G i/o ), which suggests it may be a G protein-coupled receptor (GPCR).The aims of this study were to search for related cDNA fragments of other vertebrates in the genomic databases, clone and sequence their full-length cDNAs, and partially characterize these genes and their recombinant proteins. This paper reports the identification of 13 additional vertebrate genes closely related to the spotted seatrout mPR. Structural and phylogenetic evidence is presented that these vertebrate genes encode for membrane proteins with seven or occasionally six transmembrane domains that can be classified into three subty...

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Section: Discussionmentioning

confidence: 96%

Identification, classification, and partial characterization of genes in humans and other vertebrates homologous to a fish membrane progestin receptor

Zhu

Bond

Thomas

2003

Proc. Natl. Acad. Sci. U.S.A.

645

470

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“…These effects of progesterone are preceded by an immediate transient calcium influx into spermatozoa (Blackmore et al, 1990). These rapid biological effects of progesterone to stimulate calcium influx, and the fact that transcription is inactive in the nucleus of mature spermatozoa, indicate a non-genomic response and suggest that a cell surface receptor exists for progesterone Revelli et al, 1994). This receptor has been located in the plasma membrane of the sperm head, not in the midpiece or tail .…”

Section: Introductionmentioning

confidence: 99%

Andrology: Undetectable expression of genomic progesterone receptor in human spermatozoa

et al. 1995

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The expression of genomic progesterone receptor in human ejaculated spermatozoa was investigated. Spermatozoa from 10 fertile donors who exhibited normal semen parameters were analysed. Indirect immunofluorescence and an enzyme immunoassay using monoclonal antibodies against genomic progesterone receptor were used. Different types of spermatozoa were studied: fresh, post-swim-up (migrated), capacitated and post-artificial induction of the acrosome reaction by calcium ionophore A23187. Progestin receptor-rich T47D human breast cancer cells were used as a positive control, and progestin receptor-poor MDA-MB-231 human breast carcinoma cells were used as a negative control. Genomic progesterone receptor was not detected in fresh, migrated, capacitated and post-acrosome reaction induction human spermatozoa and MDA-MB-231 cells by either indirect immunofluorescence or enzyme immunoassay. However, in T47D cells a mean concentration of 1043.2 +/- 125.2 fmol genomic progesterone receptor/mg protein was observed by enzyme immunoassay, and indirect immunofluorescence results were positive using both flow cytometry and fluorescence microscopy. These findings suggest that the effect of progesterone on human spermatozoa is not mediated by genomic progesterone receptor.

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“…In our case, it had no effect. It has been suggested that the membrane-bound progesterone receptor may itself be a Ca 2+ channel or a binding site of the Ca 2+ channel [33]. Such a situation was found on neurons, where the progesterone receptor was shown to be the Cl − ion channel itself and to contribute to its activation in response to some stimuli [30].…”

Section: Discussionmentioning

confidence: 99%

Characterization of specific corticosterone binding sites in adrenal cortex plasma membrane and their localization by autoradiographic studies

Andrés

Marino

et al. 1997

Cellular and Molecular Life Sciences (CMLS)

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Specific corticosterone binding to calf adrenal cortex plasma membrane was measured using the biologically active radioligand [3H]corticosterone. Corticosterone binding was found to be time-dependent, saturable and reversible, and was reduced by more than 70% when membranes were pretreated with proteases. The population of corticosterone binding sites in calf adrenal cortex plasma membrane was homogeneous and displayed the following characteristics: equilibrium dissociation constant Kd = 77 +/- 8 nM and maximum specific binding capacity Bmax = 70,378 +/- 6,385 fmol/mg protein. The relative affinities of several structural analogues of steroids were deduced from competition assays. From these experiments we can conclude that the plasma membrane binding site characterized is selective for corticosterone and progesterone derivatives, and different from nuclear glucocorticoid, mineralocorticoid, estrogen and progestin receptors. Likewise, this corticosterone binding site is independent of mineralocorticoid and Na+, K(+)-ATPase digitalis receptors. From autoradiographic studies we suggest these corticosterone binding sites are located in the whole adrenal cortex.

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Steroid receptors in human spermatozoa

Cited by 52 publications

References 0 publications

Identification, classification, and partial characterization of genes in humans and other vertebrates homologous to a fish membrane progestin receptor

Identification, classification, and partial characterization of genes in humans and other vertebrates homologous to a fish membrane progestin receptor

Andrology: Undetectable expression of genomic progesterone receptor in human spermatozoa

Characterization of specific corticosterone binding sites in adrenal cortex plasma membrane and their localization by autoradiographic studies

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