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)

Glycerol release from epididymal fat fragments of young adult (3-month old) ob/ob mice was three times lower than normal, on a tissue weight basis. Dose-response curves in response to isoproterenol and ACTH-(1--24) indicated that the capacity of the lipolytic process was reduced. However, the sensitivity to both hormones was normal, i.e. greater for ACTH than for isoproterenol. The burst of cyclic AMP observed at 7 minutes was affected even more than the lipolytic capacity in adipose tissue from obese mice. This was already observed in 1-month old animals, i.e. at a time when total body weight was still normal. It is concluded that the adenylate cyclase system is defective in adipose tissue of ob/ob mice. Besides, glucagon, vasoactive intestinal polypeptide, and secretin failed to stimulate glycerol release and cyclic AMP accumulation in both ob/ob, ob+/ob+, and HA-ICR mice, suggesting that mouse adipose tissue does not possess receptors for this group of hormones.
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PMID:Lipolysis and cyclic AMP levels in epididymal adipose tissue of obese-hyperglycaemic mice. 20 30

Pituitary adenylate cyclase-activating-polypeptide (PACAP) is a new member of the secretin/glucagon/vasoactive intestinal peptide family of peptides; it occurs as two amidated forms with 38 (PACAP38) and 27 (PACAP27) amino acids. Rabbit antisera against synthetic PACAP27 were characterized by enzyme-linked immunosorbent assay. One of the antisera, using a high antibody titer, recognized both PACAP27 and PACAP38 and was found useful for immunohistochemistry. The distribution and ultrastructural localization of PACAP-like immunoreactivity (PACAP-LI) in the rat testes at different stages of spermatogenesis were studied with this antiserum. Four oligonucleotide probes, each complementary to a different region covering a different intron-exon junction, were chosen to maximize hybridization based on the predicted secondary structure of PACAP messenger RNA. PACAP-LI was detected in the developing germ cells but not in either Sertoli or Leydig cells. Intense PACAP-LI was found in spermatids situated near the lumen of the seminiferous tubules. Lower levels of PACAP-LI were detected in spermatogonia and primary spermatocytes, but no PACAP-LI was found in mature spermatids, testicular spermatozoa, or epididymal spermatozoa. In spermatids, PACAP-LI was detected during the cap phase and acrosome phase but not in the maturation phase. At the ultrastructural level, numerous gold particles representing PACAP-LI were found in both acrosomal granules and acrosomal caps of spermatids, while a few particles were found in the Golgi complex. Very few gold particles were seen in the acrosome of mature spermatids and spermatozoa. PACAP-LI decreased and finally disappeared from spermatids during the late developmental stages. In situ hybridization indicated that most of the signal was detected near the perimeter of seminiferous tubules in early developing germ cells, especially in spermatogonia and primary spermatocytes, suggesting that transcription of the PACAP gene occurs in spermatogonia and primary spermatocytes. The processing of the prohormone appears to be slow, and mature PACAP only appears in spermatids. These morphological findings suggest that PACAP-like substances, synthesized by germ cells, participate in spermatogenesis, particularly spermiogenesis, probably by an autocrine and paracrine mechanism. However, the possibility that PACAP acts on the Sertoli and/or Leydig cells cannot be excluded.
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PMID:Localization of pituitary adenylate cyclase-activating polypeptide and its messenger ribonucleic acid in the rat testis by light and electron microscopic immunocytochemistry and in situ hybridization. 807 Mar 75

A novel gene product, HE6, showing homology to the seven transmembrane-domain (Tm7) receptor superfamily, has been cloned by differential screening from a human epididymal cDNA library. The cDNA clone represented an abundant approximately 5-kb mRNA, comprising 0.01% of the cDNA library. Northern blot analysis including various human tissues revealed an epididymis-specific expression. In situ transcript hybridization localized the mRNA within the epithelial cells lining the epididymal duct. Southern blot analysis, employing a fragment encoding part of the amino-terminal extracellular domain as a probe, identified an autosomal single-copy gene in the human genome. Homologous cDNA products showing 90% sequence identity were observed in the epididymides of all mammalian species investigated. A cloning and sequencing strategy, combining approximately 3.7-kb cDNA fragments obtained by conventional cDNA library construction with overlapping 5' rapid amplification of cDNA ends (RACE) fragments, yielded total sequence information of 4.7 kb for the human mRNA. This sequence comprises a long open reading frame of 3.1 kb. A homology search for related sequences revealed highest similarity (25% amino acid identity) with the secretin/vasoactive intestinal peptide (VIP) superfamily of G-protein-coupled receptors. The predicted extracellular amino-terminal extension, however, was much longer than in the other members, and showed similarity to highly glycosylated mucin-like cell-surface molecules.
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PMID:Cloning of a human epididymis-specific mRNA, HE6, encoding a novel member of the seven transmembrane-domain receptor superfamily. 915 Apr 25

There is growing evidence that secretin, the first hormone discovered in our history, has functions in the brain other than in the gastrointestinal tract. This article reports for the first time that secretin and its receptor mRNAs are produced in distinct cell types within the epididymis. To test if secretin affects electrolyte transport in the epididymis, we measured short-circuit current (Isc) in cultured epididymal epithelia and found secretin dose-dependently stimulated Isc. Ion substitution experiments and use of pharmacological agents inferred that the stimulated Isc is a result of concurrent electrogenic chloride and bicarbonate secretion. It is further shown that secretin and pituitary adenylate cyclase-activating polypeptide (PACAP) function via totally different mechanisms: 1) PACAP works only from the apical side of the epithelium to stimulate chloride and not bicarbonate secretion, while secretin acts on the apical and basolateral sides to stimulate chloride and bicarbonate secretion. 2) the stimulation by PACAP but not secretin requires local prostaglandin synthesis. By immunocytochemical staining, secretin is localized in the principal cells of the initial segment and caput epididymidis, whereas secretin receptor is present in the principal cells of the proximal as well as the distal part of the epididymis. This pattern of distribution appears to be consistent with the idea that secretin is secreted by the proximal epididymis and acts on the proximal and distal epididymis in an autocrine and paracrine fashion. Its function is to control secretion of electrolytes and water.
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PMID:Secretin controls anion secretion in the rat epididymis in an autocrine/paracrine fashion. 1474 98