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)

Thirty-one (31) subfertile men with idiopathic iligozoospermia were treated by a daily oral medication of 600 units of pancreatic kallikrein (Padutin(R) 100) over a period of 3 months. Total sperm output increased significantly with a maximum 3 months after initiation of therapy. In addition, quantitative and qualitative sperm motility improved during treatment and was still improved 2 months after withdrawal of therapy. Compared to other regimens, oral administration of 600 units kallikrein for a period of 3 months yielded better results than shorter medication periods or lower dosage. Quantitative determination of several serum proteins occurring in seminal plasma before, during and after kallikrein therapy showed a significant increase of alpha 1, x-antichymotrypsin. Thus, kallikrein treatment seems to affect, to a certain degree, the secretory activity of the accessory glands or the blood-seminal plasma barrier. Determination of serum gonadotropins and serum testosterone levels showed a significant increase of LH and testosterone during kallikrein treatment, whereas FSH was unaffected. Thus, systemic kallikrein administration induces significant changes of the pituitary-gonadal axis influencing spermatogenesis and epididymal sperm maturation. However, the local action of kinins as pharmacological active tissue hormones has to be considered too.
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PMID:Determination of various semen parameters and sex hormone levels in subfertile men during kallikrein therapy. 49 34

Human chorionic gonadotropin, kallikrein, indomethacin, and hydralazine were administered to different groups of varicocelized rats, while surgical repair of the varicocele was performed in another group of rats. The effects of conservative and surgical treatment on epididymal sperm content and motility, the weights of the testes, epididymis, and male accessory genital glands, and fertility were compared between each group and a sham-treated group of rats. Surgical repair significantly improved all the evaluated parameters and all the conservative regimens, except hydralazine, resulted in a significant improvement in most parameters. Our results indicate that stimulation of the Leydig or/and Sertoli cells of a varicocelized testicle can counteract some of the detrimental consequences of the varicocele itself.
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PMID:Surgical repair versus medical treatment of varicocele in the rat: pharmacological manipulation of the varicocelized testicle. 142 45

The predominant protein in human semen, semenogelin, was characterized by lambda gt11 clones isolated from a seminal vesicular cDNA library. One clone, carrying a cDNA insert of 1606 nucleotides and a polyadenylated tail, coded for the entire semenogelin precursor. An open reading frame of 1386 nucleotides encodes a signal peptide and the mature protein of 439 amino acid residues, in which residues 85-136 are identical with a previously characterized semenogelin fragment. The polypeptide chain displays a most conspicuous region of internal sequence homology where 46 of the 58 amino acid residues at positions 259-316 are repeated at positions 319-376. An abundant seminal vesicular transcript of 1.8 kilobases (kb) codes for semenogelin. Two additional transcripts, one seminal vesicular 2.2-kb species and one epididymal 2.0-kb species, code for related proteins that have a close structural relationship as well as antigenic epitopes in common with semenogelin. Semenogelin and the semenogelin-related proteins are the major proteins involved in the gelatinous entrapment of ejaculated spermatozoa. Antigenic epitopes common to these proteins are localized to the parts of the spermatozoa involved in locomotion. The spermatozoa become progressively motile as the gel-forming proteins are fragmented by the kallikrein-like protease, prostate-specific antigen, and the gel dissolves.
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PMID:Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa. 291 89

Sequential treatment of the chicken liver fatty acid synthetase by trypsin and subtilisin cleaved the Mr 267,000 subunit to 6-8 polypeptides, ranging in molecular weights from 15,000 to 94,000. Fractionation of the digest by ammonium sulfate and chromatography on a Procion Red HE3B affinity column permitted the isolation of a polypeptide (Mr = 94,000) containing the beta-ketoacyl reductase activity but no other partial activities normally associated with the synthetase. The specific activity of the beta-ketoacyl reductase increased 2 to 3 times in this fraction, an increase that is within the expected range based on relative molecular weight. The kinetic parameters of this fraction towards NADPH and N-acetyl-S-acetoacetyl cysteamine were essentially the same as the beta-ketoacyl reductase component of the intact synthetase. However, the purified fragment did not catalyze the reduction of acetoacetyl-S-CoA derivative, a substrate that is readily reduced by the intact synthetase. Fluorescence measurements with etheno-NADP+ indicate the binding of about 1 mol of NADP+/94,000 daltons, a value which is in agreement with the results obtained from fluorescence measurements with NADPH and the binding of a radiolabeled photoaffinity analog of NADP+. Phenylglyoxal inhibits the beta-ketoacyl reductase activity of either the intact synthetase or the isolated fragment, suggesting the involvement of an essential arginine at or near the active site. Another fragment (Mr 36,000) containing beta-ketoacyl reductase activity was isolated from the synthetase after kallikrein/subtilisin double digestion. Previous mapping studies had shown that this fragment lies adjacent to the COOH-terminal thioesterase domain and overlaps the tryptic Mr 94,000 peptide by approximately 21 daltons. This fragment, but not the Mr 94,000 fragment, was found to contain the phosphopantetheine prosthetic group, indicating that the acyl carrier protein moiety is located in the 15,000-dalton segment that separates the beta-ketoacyl reductase from the thioesterase domain.
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PMID:The architecture of the animal fatty acid synthetase. III. Isolation and characterization of beta-ketoacyl reductase. 636 Oct 31

The motility of spermatozoa from the head and tail of the epididymis in bulls was studied. Qualitatively and quantitatively, the motility of spermatozoa from the cauda was distinctly better than that from the caput. It was possible to achieve a highly significant increase in the motility of epididymal spermatozoa from the caput as well as the cauda area using caffeine or a caffeine-kallikrein mixture. Above all, motility stimulants improved the local motility of the epididymal spermatozoa as compared to twitching and progressive motility. The motility of caudal spermatozoa was increased by 100%, corresponding to local movement of 59% of the total number of sperm cells. It was possible to demonstrate an increase in the almost totally absent motility of the caput spermatozoa to 27% local motility. Application of kallikrein without addition of kininogens led to no significant change in spermatozoa motility. By the addition of caffeine, it was possible to increase the motility of minipig epididymal spermatozoa taken by puncture from alloplastic spermatoceles significantly. In 23 aspirates, a prompt increase in the percentage of locally motile "spermatocele spermatozoa" from 12% to 23.5% was observed.
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PMID:How to increase the motility of spermatozoa from the epididymis of bulls and alloplastic spermatoceles in minipigs. 656 56

Kallikrein has been reported to act positively on sperm motility. Because sperm motility must be analyzed with regard to sperm tail morphology, this study examined whether changes of sperm motility after kallikrein treatment were accompanied by structural alterations of the midpieces and tails of spermatozoa. In 60 andrologic outpatients in whom a significant improvement of sperm motility was noted after treatment with kallikrein (600 U daily for 3 mo), sperm tail morphology was analyzed according to a recently proposed classification. The effect of kallikrein could be clearly attributed to a decrease of tail disturbances characteristic of epididymal dysfunction. Besides possible effects on spermatogenesis, kallikrein may influence the epididymal maturation of spermatozoa, leading to increased progressive motility.
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PMID:Changes of sperm tail morphology after kallikrein treatment. 837 80

Despite considerable basic research effort, the therapeutic possibilities to improve impaired male fertility are still limited. This is partly because the cause of reduced fertility is unknown in many cases and, consequently, no specific therapy is available. Approaches to andrological therapy at different levels include stimulation of spermatogenesis, improvement of epididymal function or sperm transport within the male genital tract, and stimulation of sperm metabolism. Medical therapy of male fertility disturbances has to distinguish between specific and empirical treatment procedures. Specific treatment is based on a pathophysiological concept and implies accurate patient selection; the therapeutic success is predictable. In contrast, empirical treatment involves no patient selection according to specific criteria; thus, the therapeutic success is unpredictable. Hormonal treatment is the main choice in andrological therapy, including pulsatile administration of gonadotrophin-releasing hormone (GnRH), human gonadotrophins, anti-oestrogens and testosterone. Non-hormonal treatment is carried out using different pharmaceutical compounds such as alpha-sympathomimetics, antibiotics, antiphlogistics, corticosteroids, mast cell blockers, pentoxifylline, kallikrein, captopril, vitamins and zinc. In patients with severe male factor who are resistant to therapy, procreation problems may be solved by the method of intracytoplasmic sperm injection (ICSI).
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PMID:Survey of medical therapy in andrology. 871 60

We investigated the role of the kallikrein-kinin system in cardiac function and glucose utilization in the streptozotocin (STZ)-induced diabetic rat model using a gene transfer approach. Adenovirus harboring the human tissue kallikrein gene was administered to rats by intravenous injection at 1 week after STZ treatment. Human kallikrein transgene expression was detected in the serum and urine of STZ-induced diabetic rats after gene transfer. Kallikrein gene delivery significantly reduced blood glucose levels and cardiac glycogen accumulation in STZ-induced diabetic rats. Kallikrein gene transfer also significantly attenuated elevated plasma triglyceride and cholesterol levels, food and water intake, and loss of body weight gain, epididymal fat pad, and gastrocnemius muscle weight in STZ-induced diabetic rats. However, these effects were blocked by icatibant, a kinin B2 receptor antagonist. Cardiac function was significantly improved after kallikrein gene transfer as evidenced by increased cardiac output and +/-delta P/delta t (maximum speed of contraction/relaxation), along with elevated cardiac sarco(endo)plasmic reticulum (Ca2+ + Mg2+)-ATPase (SERCA)-2a, phosphorylated phospholamban, NOx and cAMP levels, and GLUT4 translocation into plasma membranes of cardiac and skeletal muscle. Kallikrein gene delivery also increased Akt and glycogen synthase kinase (GSK)-3beta phosphorylation, resulting in decreased GSK-3beta activity in the heart. These results indicate that kallikrein through kinin formation protects against diabetic cardiomyopathy by improving cardiac function and promoting glucose utilization and lipid metabolism.
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PMID:Kallikrein gene delivery improves serum glucose and lipid profiles and cardiac function in streptozotocin-induced diabetic rats. 1585 48

Water and solute transport in the efferent ducts and epididymis are important for the establishment of the appropriate luminal environment for sperm maturation and storage. Aquaporin 9 (AQP9) is the main water channel in the epididymis, but its regulation is still poorly understood. Components of the kinin-kallikrein system (KKS), leading to the production of bradykinin (BK), are highly expressed in the lumen of the male reproductive tract. We report here that the epididymal luminal fluid contains a significant amount of BK (2 nM). RT-PCR performed on epididymal epithelial cells isolated by laser capture microdissection (LCM) showed abundant BK type 2 receptor (Bdkrb2) mRNA expression but no type 1 receptor (Bdkrb1). Double-immunofluorescence staining for BDKRB2 and the anion exchanger AE2 (a marker of efferent duct ciliated cells) or the V-ATPase E subunit, official symbol ATP6V1E1 (a marker of epididymal clear cells), showed that BDKRB2 is expressed in the apical pole of nonciliated cells (efferent ducts) and principal cells (epididymis). Triple labeling for BDKRB2, AQP9, and ATP6V1E1 showed that BDKRB2 and AQP9 colocalize in the apical stereocilia of principal cells in the cauda epididymidis. While uniform Bdkrb2 mRNA expression was detected in the efferent ducts and along the epididymal tubule, marked variations were detected at the protein level. BDKRB2 was highest in the efferent ducts and cauda epididymidis, intermediate in the distal initial segment, moderate in the corpus, and undetectable in the proximal initial segment and the caput. Functional assays on tubules isolated from the distal initial segments showed that BK significantly increased AQP9-dependent glycerol apical membrane permeability. This effect was inhibited by BAPTA-AM, demonstrating the participation of calcium in this process. This study, therefore, identifies BK as an important regulator of AQP9.
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PMID:Segmental expression of the bradykinin type 2 receptor in rat efferent ducts and epididymis and its role in the regulation of aquaporin 9. 1882 5

Rats have been used to study the function and development of the mammalian prostate. Identification of prostatic secreted proteins is important in order to better understand their physiological function. Previous investigations have showed that prostatein, cysteine-related protein 1, and kallikrein S3 are in the ventral prostate (VP), whereas the proteins probasin, prostate secretory peptide 94, transglutaminase 4, and carbonic anhydrase II are produced in the lateral prostate, dorsal prostate (DP), and anterior prostate. They are also useful markers when looking at androgen dependency as well as prostate-specific expression. Although some of the rat prostatic proteins have been investigated well, the overall protein expression profile of the prostate has not been examined. In the present study, the secretions from the rat prostate were subjected to 2-dimensional gel electrophoresis followed by mass spectrometric analysis. In addition to the previously known proteins, proteome analysis revealed several new secreted proteins, including spermine-binding protein and a protein similar to immunoglobulin-binding protein. In addition, epididymal secreted protein 1 and peroxiredoxin 6 were found in the DP, while glucose-regulated protein 78 was identified in all lobes of the prostate. Castration of the animals led to a decrease in the mRNAs of all of these secreted proteins. While the mRNAs of prostatic proteins became almost completely absent in the VP, the reductions in the other lobes were limited. A novel view of rat prostate secretion from our results should contribute to an understanding of the biological functions of the prostate gland.
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PMID:Identification of rat prostatic secreted proteins using mass spectrometric analysis and androgen-dependent mRNA expression. 1957 34


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