Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.8 (cholinesterase)
 12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We measured serum sex hormone-binding globulin (SHBG) using a radioimmunoassay developed by us, testosterone (T), estradiol (E2), free T and free E2 in 50 male patients with non-alcoholic liver cirrhosis (compensated: 30, decompensated; 20) and age-matched healthy male subjects, SHBG was significantly increased in patients with liver cirrhosis compared with healthy subjects. The high serum SHBG level in male compensated cirrhotic patients tended to decrease with progression to the decompensated state. Serum cholinesterase showed a positive correlation with SHBG in liver cirrhosis. Serum free T and the T/SHBG ratio decreased, while serum E2, free E2, and the E2/T and the free E2/free T ratios increased in liver cirrhosis, resulting in estrogen predominance and feminization of male patients. These changes were more marked in decompensated than compensated liver cirrhosis. An increased free E2/free T ratio was observed in patients with gynecomastia, palmar erythema or vascular spider. The T/SHBG ratio showed a positive correlation with serum free T, suggesting that it can be used as a free T index in liver cirrhosis. From these observations, it is suggested that serum SHBG plays an important role, by regulating the serum free T level in the occurrence of feminization in male patients with non-alcoholic liver cirrhosis.
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PMID:Mechanism of feminization in male patients with non-alcoholic liver cirrhosis: role of sex hormone-binding globulin. 191 51

The binding capacities of SHBG and CBG were measured by agar gel electrophoresis in 63 men with cirrhosis of the liver and in 42 healthy male subjects. The normal range (X- +/- 2s) for SHBG was 8.3-17.1 microgram/l, for CBG 46.4-82.8 micrograms/l. SHBG binding capacity was significantly higher in men with liver cirrhosis (mean 18;1 microgram/l; p less than 0.001) but CBG binding capacity was significantly lower (mean 49.7 microgram/l; p less than 0.001). Although SHBG was lower in patients with decreased CBG binding capacity, a correlation between both steroid binding proteins did not exist. Moreover, there was no correlation between SHBG or CBG on one hand and other parameters of hepatic protein synthesis such as serum protein concentration, cholinesterase activity and the coagulation factors V and VII on the other hand. In contrast to liver cirrhosis, 12 patients with fatty liver and 11 patients with toxic fibrosis of the liver did not reveal changes in SHBG or CBG. Treatment with spironolactone (200 mg daily for one week in 9 subjects) did not change the steroid binding capacity of human serum.
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PMID:[Binding capacity of sex hormone binding globulin and corticosteroid binding globulin in serum of male patients with liver cirrhosis (author's transl)]. 718 44

The heterophilic synaptic adhesion molecules neuroligins and neurexins are essential for establishing and maintaining neuronal circuits by modulating the formation and maturation of synapses. The neuroligin-neurexin adhesion is Ca2+-dependent and regulated by alternative splicing. We report a structure of the complex at a resolution of 2.4 A between the mouse neuroligin-1 (NL1) cholinesterase-like domain and the mouse neurexin-1beta (NX1beta) LNS (laminin, neurexin and sex hormone-binding globulin-like) domain. The structure revealed a delicate neuroligin-neurexin assembly mediated by a hydrophilic, Ca2+-mediated and solvent-supplemented interface, rendering it capable of being modulated by alternative splicing and other regulatory factors. Thermodynamic data supported a mechanism wherein splicing site B of NL1 acts by modulating a salt bridge at the edge of the NL1-NX1beta interface. Mapping neuroligin mutations implicated in autism indicated that most such mutations are structurally destabilizing, supporting deficient neuroligin biosynthesis and processing as a common cause for this brain disorder.
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PMID:Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions. 1808 3