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)

We investigate in this study the hypothesis of human sex steroid-binding protein hSBP internalization into germ cells in a primate model. Human SBP was purified from late-pregnancy serum and labeled either with colloidal gold particles (18 nm) or with [3H]delta 6-testosterone by photoaffinity treatment. The germ cells were isolated from sexually mature monkey testis or caput epididymis (Macaca fascicularis) by mechanical means and cell suspensions (4 x 10(6) per 100 microliters culture medium) were incubated in presence of hSBP-gold complex (60 ng/100 microliters) or hSBP-[3H]delta 6-testosterone complex (66 ng/100 microliters, 20,000 cpm) for 2, 5, 15, 45, and 60 min. The samples were processed for electron microscopy followed by autoradiographic treatment for the radiolabeled samples. Localization of the label occurred over the whole germ cell lineage whichever tracer was used. Spermatogonia, spermatocytes, spermatids, testicular and epididymal spermatozoa exhibited specific binding sites over the plasma membrane associated with clathrin-like coated pits and vesicles. At 34 degrees C, intracellular localization of the labeled ligand was found within coated vesicles, in early and late endosomes. In addition, in early spermatogenic cells, labeled ligand was detected in the nuclei and/or associated with the nuclear envelope whereas in late spermatids and residual bodies, the labeling was accumulated in multivesicular, prelysosomal structures. Quantitative analysis of the "labeled cells/total cells" ratio exhibited a negative correlation to the maturation steps, epididymal spermatozoa being the least labeled. The cellular distribution is similar with one or the other protein in the same spermatogenic cells. Unlabeled hSBP treatment prior to labeled hSBP reduced significantly the internalization. Lowering the temperature to 4 degrees C prevented endocytosis and enhanced membrane binding. EDTA pretreatment strongly decreased hSBP internalization and modified the early endocytic steps, namely, the pinching off of the coated vesicles. It is concluded that monkey germ cells are able to internalize the human sex steroid-binding protein through specific endocytic organelles. This endocytosis leads to the labeling of the nuclei in the early spermatogenic cells and of the multivesicular bodies in the late germ cells. This strongly suggests that steroid-binding proteins may be required for spermatogenesis in acting at the germ cell lineage level either by themselves or by serving as steroid transmembrane carriers.
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PMID:Endocytosis of human sex steroid-binding protein in monkey germ cells. 178 75

Immature male little brown bats were aroused prematurely from their first hibernation and fed ad libitum (Group AL) or given a restricted diet (Group FR). All animals were weighed daily and the food intake of Group FR males was restricted to maintain their body weights at or near initial post-arousal values (5.3-6.8 g). The average body weights of Group AL males increased during the first week after arousal and then stabilized at a level which was 20% higher than those of Group FR males. The post-arousal induction of plasma SBP was similar in Groups FR and AL: plasma SBP activity was significantly increased 1 week after arousal and by 3 weeks had reached levels which were more than 10-fold higher than those of immature hibernating males which served as controls. Although food restriction had no effect on plasma SBP levels, it did inhibit reproductive development. Arousal-induced increases in testicular and epididymal (head/body) weights in Group FR males were less than 50% of those in Group AL males. However, histological examination of the testes revealed similar degrees of spermatogenic activation in both groups. Plasma testosterone concentrations were increased markedly in Groups FR and AL; values were generally lower in Group FR but wide individual variations were observed. Despite these elevated peripheral testosterone values, the accessory sex glands in both groups remained unstimulated.
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PMID:Relationship of food intake to the induction of plasma sex steroid-binding protein and testicular activity in immature male little brown bats (Myotis lucifugus lucifugus). 393 Jul 16

In this study the effect of diet supplementation with grape pomace (GP) and grape pomace extract (GPE) on insulin sensitive tissues (adipose, liver and muscle) was evaluated in an experimental model of metabolic syndrome (MetS). MetS was developed by giving a high-fat-fructose (HFF) diet to Wistar rats. Six weeks of HFF diet induced weight gain, which was partially attenuated by GP (1 g per kg per day) and GPE (300 mg per kg per day) supplementation. HFF diet increased systolic blood pressure, triglycerides, insulin resistance (HOMA:IR) and inflammation (c-reactive protein (CRP)). Supplementation with GP prevented SBP, triglycerides and CRP increased and partially attenuated insulin resistance. On the other hand, GPE partially reduced SBP and triglycerides and significantly prevented insulin resistance and inflammation. Also, HFF diet induced higher triglycerides content and enhanced NADPH oxidase activity in the liver. Also, HFF diet increased the epididymal adipose tissue weight, enlarged adipocyte size, and c-jun N-terminal kinase (JNK) activation, probably contributing to a pro-inflammatory cytokine pattern (higher resistin) and lower adiponectin protein expression. These alterations may result in an impairment of insulin signaling cascade observed in adipose, liver and muscle tissue (IRS1, Akt, and extracellular signal-regulated kinases (ERK1/2)) from HFF rats. Supplementation with GP and to a greater extent GPE attenuated liver triglyceride content and adiposity and restored adipose, liver and muscle response to insulin. These findings show that supplementation with GP and GPE to a greater extent can counteract adiposity, inflammation, liver damage and impaired insulin signaling associated to MetS, supporting the utilization of winemaking residues in food industry/human health due to their high amount of bioactive compounds.
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PMID:Grape pomace and grape pomace extract improve insulin signaling in high-fat-fructose fed rat-induced metabolic syndrome. 2690 21