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 activity of cathepsins A, B, C, D, phospholipases A1 and A2, and aryl sulphatases A and B was studied in hepatic lysosomas, adipocytes of epididymal fatty tissue and in platelets of rats aged 2,5 and 24 months differing in the character of milk feeding. It was found that excessive feeding in the neonatal period resulted in a decrease of the lysosomal proteinase activity by 18-33% in 24-month animals, while phospholipase A2 activity rose 1,4-2.2-fold. Phospholipase A2 activity proved to be also increased in adipocytes of obese rats. Obese rats' platelets were characterized by a drastic (2-3.5-fold) activation of cathepsin C, and phospholipase A1 activity rose by 55% at all the stages of the ontogenesis. It is suggested that the changes in the lysosomal hydrolases activity may reflect the platelet function in the disordered lipoprotein metabolism.
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PMID:[Effect of neonatal nutrition on the enzyme activity of liver lysosomes, adipocytes and thrombocytes in young and old rats]. 370 43

Epididymal 5 alpha-reductase converts testosterone to 5 alpha-dihydrotestosterone. The enzyme is localized to the nuclear and microsomal membranes, and using two approaches, we investigated the relationship between 5 alpha-reductase activity and the membrane environment. In the first, nuclear and microsomal membrane fractions were treated with phospholipases to modify specifically the structure of the phospholipid component of the membranes, and the effects of these treatments on the kinetic parameters of 5 alpha-reductase were examined. The second approach was to observe the effects of phospholipids of known structure on solubilized 5 alpha-reductase activity. Treatment of the membrane fractions with phospholipase C increased the Km(app) of both the nuclear and microsomal 5 alpha-reductases for testosterone. Phospholipase A2 treatment also increased the Km(app) of the microsomal enzyme, but in contrast, the Km(app) of the nuclear 5 alpha-reductase for testosterone was unaffected. This demonstrated a fundamental difference in the role of the membrane environment in the expression of 5 alpha-reductase activity in these subcellular compartments. The ability of phospholipids to enhance the activity of solubilized 5 alpha-reductase was highly specific and structure related. Only phosphatidylcholines containing either unsaturated acyl chains or saturated acyl chains of 12 carbon atoms were found to activate 5 alpha-reductase. The most potent activator was dilauroyl phosphatidylcholine, which reduced the Km(app) values of both nuclear and microsomal 5 alpha-reductases for testosterone, without affecting the concentration of active 5 alpha-reductase (Vmax(app) ). This is the first time that an activator of 5 alpha-reductase has been found. These findings suggest that epididymal 5 alpha-reductase activity may be regulated by changes in the phospholipid environment.
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PMID:Modulation of epididymal delta 4-steroid 5 alpha-reductase activity in vitro by the phospholipid environment. 399 84

Phospholipase A2 and lysophospholipids have been implicated in the mammalian sperm acrosome reaction. In this study we further investigated the role of this enzyme and lysophospholipids on the acrosome reaction of hamster spermatozoa. Hamster epididymal spermatozoa were incubated under capacitation and acrosome reaction-inducing conditions. After 3.0 and 3.5 h, the spermatozoa were treated with different doses of lysophosphatidylcholine for 12 min. Then the percentage of motility, hyperactivation, and acrosome reaction was evaluated by light microscopy. Lysophosphatidylcholine, 10 micrograms/ml, was the highest acrosome reaction-inducing dose without an effect on sperm motility. Lysophosphatidylcholine induced the acrosome reaction only when added to spermatozoa capacitated for a minimum of 2 h. This effect was apparent after 1 min of its addition and reached a plateau after 5 min. Lysophosphatidylethanolamine and lysophosphatidylinositol were also effective in inducing the acrosome reaction. Lysophosphatidylserine did not have any effect on the reaction, but caused an increase in sperm hyperactivation. Sperm treated with the phospholipase A2 inhibitors quinacrine dihydrochloride and p-bromophenacyl-bromide showed an inhibition of the spontaneous occurrence of the acrosome reaction. These inhibitors, however, did not block the acrosome reaction induced by lysophosphatidylcholine. The time course of the lysophosphatidylcholine-induced acrosome reaction was the same whether control or inhibitor treated spermatozoa were used. These results suggest that the membrane events of the acrosome reaction initiate with the activation of the phospholipase A2, thus producing the fusogen agents necessary for this exocytotic event.
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PMID:Studies of lysophospholipids related to the hamster sperm acrosome reaction in vitro. 840 1