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)

Gamma-Glutamyl transpeptidase (gamma-GT) was studied histochemically and biochemically in the rat epididymis after castration with or without testosterone treatment, or after hemicastration and ligation of the efferent ducts. There was a strong reaction to gamma-GT in the apical part of the epithelium in the caput epididymis, while in the corpus and cauda the reaction was confined mainly to the luminal contents. Castration caused a marked decline in epithelial gamma-GT activity within 10 days. Subsequent testosterone treatment (1 mg/day for 10 days) restored gamma-GT activity in the apical surface and lumen. After hemicastration of adult rats, and after hemicastration or ligation of the efferent ducts in immature 28-day-old rats, a small but significant (P less than 0.001) decrease was observed in gamma-GT activity in the epididymal caput compared to controls. The quantities of six other enzymes (beta-N-acetylglucosaminidase, beta-galactosidase, angiotensin-converting enzyme, alanyl amino-peptidase, dipeptidyl peptidase IV, acid phosphatase) also displayed significant changes after castration and restoration of activities by testosterone treatment. However, their distribution in the caput and cauda epididymis was more even than that of gamma-GT, and the changes after castration were less drastic. It is concluded that gamma-GT is a highly sensitive androgen-dependent secretory marker in the caput epididymis and may have an important function in sperm maturation.
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PMID:Gamma-glutamyl transpeptidase in rat epididymis: effects of castration, hemicastration and efferent duct ligation. 257 65

Particles found in bovine seminal vesicle secretion were enriched by centrifugation. They varied in size and morphology and contained Mg2+,Ca2+-activated ATPase, aminopeptidase A, alanyl aminopeptidase, gamma-glutamyl transpeptidase and dipeptidyl peptidase IV activities. Hyperactivation of sperm motility and the acrosome reaction were induced by these particles in epididymal spermatozoa suspended in a modified Ringer medium. The hyperactivation, analysed with a microscopic slide test, started within minutes of exposure to membrane particles and continued for 3-4 h, during which time spermatozoa underwent the acrosome reaction. Acrosome staining, phase-contrast microscopy and transmission electron microscopy revealed that the acrosome reaction started within 60 min at 37 degrees C and affected up to 80% of spermatozoa in 4 h. These membrane particles differed from those reported previously in other species in enzyme composition, function and organ of origin.
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PMID:Effect of secretory particles in bovine seminal vesicle secretion on sperm motility and acrosome reaction. 357 75

Small membranous vesicles, between 25- and 75-nm diameter, were collected by high-speed centrifugation from the ram cauda epididymal fluid and were found to be normal constituents of this fluid and of the seminal plasma. The SDS-PAGE protein pattern of these vesicles was specific and very different from that of the caudal fluid, seminal plasma, sperm extract, and cytoplasmic droplets. After two-dimensional electrophoresis separation and mass spectrometry analysis, several proteins were identified and grouped into i) membrane-linked enzymes, such as dipeptidyl peptidase IV (DPP-IV), neprilysin (NEP), phosphodiesterase-I (E-NPP3), and protein G-beta; ii) vesicle-associated proteins, such as lactadherin (MFEG8-PAS6/7) and vacuolar ATPase; iii) several cytoskeleton-associated proteins, such as actin, ezrin and annexin; and iv) metabolic enzymes. The presence of some of these proteins as well as several different hydrophobic proteins secreted by the epididymis was further confirmed by immunoblotting. These markers showed that the majority of the vesicles originated from the cauda epididymal region. The physical and biochemical characteristics of these vesicles suggest they are the equivalent of the exosomes secreted by several cell types and epithelium. The main membrane-linked proteins of the vesicles were not retrieved in the extract from cauda or ejaculated sperm, suggesting that these vesicles did not fuse with sperm in vivo.
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PMID:Identification, proteomic profiling, and origin of ram epididymal fluid exosome-like vesicles. 1563 28

Several studies have investigated whether dipeptidyl peptidase IV (DPP IV) activity is correlated to the severity of diabetes; however, it remains unclear. To investigate the roles of DPP IV activity in metabolic abnormalities, impaired glucose tolerance rats were produced using a high-fat (HF) or high-sucrose (HS) diet. HF diet-fed rats obviously exhibited impaired glucose tolerance, with increases in subcutaneous and epididymal fat mass, insulin resistance and dyslipidaemia. In rats fed a HS diet rather than a normal diet, lower body weight and fasting blood glucose were observed temporarily in the early period after HS diet feeding; however, impaired glucose tolerance was evoked to some extent with an increase in epididymal fat mass. Both HF and HS diet-fed rats showed significantly higher plasma DPP IV activity than normal diet-fed rats, in the order of HF diet>HS diet>normal diet. HF and HS diets did not significantly affect DPP IV activity and mRNA expression in the kidney. On the other hand, HF, but not HS, diet caused a significant decrease in DPP IV activity in the liver as compared to the control. Of note, both HF and HS diets caused a significant decrease in DPP IV activity in epididymal fat, even though they did not change DPP IV activity in subcutaneous fat. In conclusion, HF or HS diet-induced impaired glucose tolerance with visceral fat accumulation may be interrelated with increased plasma DPP IV activity and decreased DPP IV activity of visceral but not subcutaneous adipose tissue.
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PMID:Increased plasma dipeptidyl peptidase IV (DPP IV) activity and decreased DPP IV activity of visceral but not subcutaneous adipose tissue in impaired glucose tolerance rats induced by high-fat or high-sucrose diet. 1925 96