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

A 30-year-old Standardbred stallion was examined for unilateral scrotal swelling. Physical and ultrasound examinations revealed a painless enlarged left testis with a non-homogeneous echogenicity, when compared with the controlateral testis. The stallion underwent left unilateral orchiectomy. Grossly, the excised testis was irregularly enlarged (12 x 9 x 9 cm; weight: 530 g) and firm. The sections showed that testicular parenchyma was replaced by a lobulated, greyish-white mass, which involved the epididymal head. At microscopy, a dual Leydig and Sertoli cell tumour component could be seen. Neoplastic Sertoli cells were prevalent and presented pleomorphic cells, mitotic figures and occasional vascular invasion. Tumour patterns showed tubular and solid areas, cord-like or diffuse in appearance, among which newly formed Leydig cell nests and low-density fibrillar bundles were interposed. Immunohistochemically, a weak to moderate immunostaining for vimentin, AE(1)/AE(3) cytokeratin, alpha-1-antitrypsin and CD99 antigens was found in the growing Sertoli cells, whose nuclear MIB-1 labelling index scored 13 +/- 2%. The Leydig tumour cells, on the other hand, displayed a moderate to strong positivity for alpha-inhibin, vimentin, AE(1)/AE(3) cytokeratin, neurone-specific enolase and CD99. On the basis of these findings, a diagnosis of malignant mixed sex cord-stromal tumour was made.
 ...
PMID:Malignant mixed sex cord-stromal tumour in a stallion. 1536 73

The proteins that are neosynthesized and secreted in the different regions of the human epididymis were determined by in vitro biosynthesis of epididymal tubules, and the luminal proteins were collected by microperfusion of each tubule. The preparations were analyzed by two-dimensional gel electrophoresis and the proteins were identified by mass spectrometry. Some of the major proteins identified corresponded to serum compounds such as albumin, transferrin and alpha-1-antitrypsin. The other proteins identified included lactotransferrin, clusterin, PEBP, NCP2/CTP/HE1, HE3, Crisp, actin, calmodulin, E12, PGDS, l-lactate dehydrogenase, malate dehydrogenase, carbonic anhydrase, triose phosphate isomerase, glutamyltransferase, glutathione S-transferase P, thioredoxin peroxidase, superoxide dismutase, cathepsin D and cystatin. Epididymal activity is highly regionalized in most species. However, in this study in humans, there were only minor changes in the major proteins secreted. It is suggested that this specificity might be related to the difference between species in the location of the epididymis where sperm become fertile.
 ...
PMID:Human epididymal secretome and proteome. 1643 Oct 15

Seminal plasma, an amorphous material that exists in semen, contains proteins related to sperm forward motility. Employing affinity chromatography with ConA beads and protein ultrafiltration, we isolated and concentrated proteins from heated human seminal plasma. Results of computer-assisted semen analyses (CASA) demonstrated that the forward motility index of bovine spermatozoa from the epididymal caput, incubated with proteins and theophylline, was significantly different from that of spermatozoa incubated with theophylline alone (P < 0.01). The electrophoreses revealed that the protein bands with high molecular weights in the gel of PAGE changed into low molecular weights in the gel of SDS-PAGE. Furthermore, proteins from a separated portion of the PAGE gel were still able to stimulate spermatozoa from the epididymal caput to gain forward motility. Two-dimensional (2D)-gel electrophoresis and mass spectrometry indicated that spots focused on the portion seemed, according to their amino acid sequences, to be like human alpha-1-antitrypsin and zinc-alpha-2-glycoprotein (ZAG) precursors. Western blot analysis showed the presence of these two proteins in seminal plasma. These proteins, related to the forward motility of spermatozoa in human seminal plasma, may play important roles during maturation of spermatozoa, from the epididymis through fertilization in the female reproductive tract.
 ...
PMID:Identification of sperm forward motility-related proteins in human seminal plasma. 1739 27