Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adrenomedullin (AM) has been found in the brain as well as in various peripheral tissues, including reproductive organs such as the testis and the prostate. Here, we report the expression of AM in the rat epididymis and its role in anion secretion. Whole-epididymal extracts had 35.3 +/- 1.4 fmol of immunoreactive AM per mg of protein, and immunocytochemical studies showed positive AM immunostaining in the epithelial cells. By solution-hybridization-RNase protection assay, preproAM mRNA was detected at high levels in the epididymis. Gel filtration chromatography of AM showed two peaks, with the predominant one eluting at the position of authentic rat AM (1-50). Specific binding of AM to the epididymis, which could be displaced by calcitonin gene-related peptide, was observed. The epididymis also bound to calcitonin gene-related peptide, and this was displaceable by AM. Furthermore, the epididymis was shown to co-express mRNA encoding the calcitonin receptor-like receptor and receptor activity-modifying proteins, RAMP1/RAMP2. The corpus region had the highest AM level and gene expression and the lowest active peptide:precursor ratio. However, mRNA levels of the receptor and the receptor activity-modifying proteins were similar in all regions. In monolayer cultures derived from the rat epididymal cells, AM stimulated short-circuit current on the luminal side in a dose-dependent manner. Our results demonstrate the presence of AM, preproAM mRNA, AM receptors, and specific-binding sites in the rat epididymis as well as the possible role of AM in the regulation of electrolyte and fluid secretion in the epididymis.
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PMID:Co-expression of adrenomedullin and adrenomedullin receptors in rat epididymis: distinct physiological actions on anion transport. 1260 69

Most of the proteins secreted in the epididymis are produced by the proximal region, and several of them are secreted in abundance. Many of these major proteins have now been identified, including a new epididymis-specific RNase A-like Train A protein, which has been recently described in several mammals. This protein is expressed and secreted exclusively in the initial part of the epididymis. RNase A activity was analyzed in the fluids from the testis and from different epididymal regions, but in no case was the Train A protein found to have RNase A activity. The protein was present only in the luminal fluid of the epididymal region that secreted it. Using an in vitro/in vivo microperfusion technique and immunogold electron microscopy labeling, we demonstrated that the epithelium that secreted it specifically reabsorbed the protein that was present in the lumen of the tubule. Thus, the presence of Train A protein in epididymal fluid was the result of a steady state between secretion and absorption. The transcription and translation of Train A mRNA were simultaneous and actively regulated by testicular factors. The function of this protein is unknown, but it does not seem to interact directly with sperm. As for other members of the RNase family (e.g., angiogenin), its biological activity might be expressed after its cellular reabsorption. This new compound might therefore participate in an unknown function in the epithelial cells of this first part of the epididymis by an autocrine pathway.
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PMID:Train A, an RNase A-like protein without RNase activity, is secreted and reabsorbed by the same epididymal cells under testicular control. 1525 24

Members of the RNase superfamily participate in a diverse array of biological processes, including RNA degradation, antipathogen activities, angiogenesis, and digestion. In the present study, we cloned the rat RNase9 gene by in silico methods and genome walking based on homology to the Macaca mulatta (rhesus monkey) epididymal RNase9. The gene is located on chromosome 15p14, spanning two exons, and is clustered with other members of the RNase A superfamily. It contains 1279 bp and encodes 182 amino acids, including a 24-amino acid signal peptide, and it has unique features known from other RNases. Unlike those other members, the rat RNase9 mRNA was specifically expressed in the epididymis, especially in the caput and corpus, and exhibited an androgen-dependent expression pattern but was downregulated in an epididymitis animal model. The RNASE9 was expressed in a principal cell-specific pattern. Interestingly, most of the principal cells in the caput expressed the RNASE9; however, in the distal caput, the principal cells showed a checkerboard-like pattern of immunoreactivity. We also observed that the RNASE9 was bound on the acrosomal domain of sperm. Its potential roles in sperm maturation are discussed.
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PMID:RNase9, an androgen-dependent member of the RNase A family, is specifically expressed in the rat epididymis. 1700 42

This study aimed to determine the effect of bull seminal plasma (SP) and sperm on endometrial function. Bovine endometrial explants were incubated with: ejaculated sperm with or without SP, epididymal sperm, or SP alone. Neither ejaculated nor epididymal sperm induced differential expression of IL1A, IL1B, IL6, IL8, PTGES2, TNFA, and LIF. Interestingly, SP had a detrimental effect on endometrial RNA integrity. Addition of an RNase inactivation reagent to SP blocked this effect, evidencing a role for a SP-RNase. Because bulls deposit the ejaculate in the vagina, we hypothesized that the bovine endometrium is more sensitive to SP-RNase than vaginal and cervical tissues (which come into contact with SP during mating), or to endometrium from intrauterine ejaculators (such as the horse). In addition, due to differences in SP-RNase abundance depending on SP collection method (i.e., with an artificial vagina, AV, or by electroejaculation, EE), this effect was also tested. Bull SP, collected by AV, degrades RNA of mare endometrium, and bovine vagina, cervix and endometrium. However, stallion SP or bull SP collected by EE did not elicit this effect. Thus, results do not support a role for SP in modulating endometrial function to establish pregnancy in cattle.
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PMID:Species-specific and collection method-dependent differences in endometrial susceptibility to seminal plasma-induced RNA degradation. 3163 62


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