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)

The proteins which are secreted from the restricted part of the epididymis are suggested to sustain sperm maturation. In porcine species, as the potential abilities of sperm for movement and fertilization greatly increase in the corpus epididymis, the secretions in both the caput and corpus epididymis seem to be very important for the sperm maturation. In this study, we have directed our attention to the 40 kDa protein which is detected in the fluid of the distal caput epididymis of boar. It was purified from the porcine cauda epididymal fluid and its cDNA was cloned from the cDNA library of the distal caput epididymis. According to the deduced amino acid sequence, the 40 kDa protein has been identified as procathepsin L. Northern blot analysis showed that the procathepsin L mRNA was most abundant in the distal caput epididymis among the tissues as examined. Consistent with the distribution of the procathepsin L mRNA in the epididymis, the activity of procathepsin L was absent in the fluid of the proximal and mid caput epididymis and first appeared in the distal caput epididymal fluid, whose contents gradually decreased with the passage through the epididymis. These results first appeared in the first distal caput epididymis expresses very high levels of procathepsin L and unusually secretes it into the luminal fluid instead of targeting it to lysosomes. It has been also found that the mRNA of PDGF, which is known to enhance cathepsin L expression in the culture cells, is very high in the mid caput epididymis, which just precedes the site of procathepsin L secretion. This result indicates that PDGF directly regulates the locally restricted expression and secretion of procathepsin L in the epididymis, which is one of the possible mechanisms involved in the functional differentiation in the epididymis.
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PMID:Direct evidence for the elevated synthesis and secretion of procathepsin L in the distal caput epididymis of boar. 749 81

The synthesis and secretion of proteins by the boar genital tract were studied in vitro by incubating epididymal tissues with [35S]methionine and cysteine. Characterization of the major neosynthesized proteins was performed electrophoretically by one- and two-dimensional PAGE analysis, and an epididymal protein cartography was established. Some of the proteins secreted were found to be unregionalized. Polarization studies of the secretions in the epididymal tubule were carried out by in vitro incubation of isolated tubules, and most of these unregionalized proteins were found not to be secreted in the epididymal lumen. Inside the epididymal lumen, protein secretion was highly regionalized, and electrophoresis analysis detected few proteins secreted at all points along the organ. A total of 146 epididymal proteins, covering 220 spots, were found to be secreted by the epididymis. The distal caput showed the highest number of spots, the lowest number of proteins secreted being found in the proximal caput and cauda. Most of the epididymal proteins analyzed are highly polymorphic in terms of both isoelectric point and molecular mass. The presence and importance of the different compounds in the various regions of the epididymis were established. Several distinct secretory regions of the epididymis can be determined by the presence of major characteristic proteins. The concentrations of a given protein in the fluids of various regions were not related to the respective secretion intensity of that protein. Identification of some major epididymal proteins was accomplished by N-terminal amino microsequencing and by the use of specific antisera. Of the various major proteins, clusterin, glutathione peroxidase, retinol-binding protein, lactoferrin, EP4, beta-N-acetyl-hexosaminidase, alpha-mannosidase, and procathepsin L were identified and localized along the organ. Several polypeptides found in this study remain unidentified.
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PMID:Characterization and identification of proteins secreted in the various regions of the adult boar epididymis. 890 5

The number of proteins secreted by the boar epididymis increased progressively from 1 mo of age to the adult period. The first specific secretory activity was revealed at 2 mo in the distal caput (hexosaminidase, clusterin, and lactoferrin) and in the corpus (train O/HE1). Train A and glutathione peroxidase specific to the proximal caput, and trains E and M specific to the corpus, appeared at 4 mo. At 5 mo, secretion of procathepsin L occurred in the middle caput and that of mannosidase and E-RABP in the distal caput. Approximately 48% of all the proteins secreted in the adult boar epididymis were dependent on the presence of androgens, either stimulated (33.6%) or repressed (14.4%); 47% were modulated by other factors, and 5% were unregulated. In the proximal caput, 50% of the specific secreted proteins were controlled essentially by factors emanating from the testis. In more distal regions, two proteins secreted in the corpus were regulated by factors from the anterior regions. The regionalization of the secretory activity of the epididymal epithelium resulted in a specific regulation for each protein, which was modulated according to the region of expression and influenced by either testicular or epididymal factors that remain to be identified.
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PMID:Postnatal development and regulation of proteins secreted in the boar epididymis. 1057 12