Chronic ethanol treatment alters the biosynthesis of β -endorphin by the rat neurointermediate lobe

1983 ◽  
Vol 61 (9) ◽  
pp. 967-976 ◽  
Author(s):  
Christina Gianoulakis ◽  
John S. D. Chan ◽  
Harold Kalant ◽  
Michel Chrétien

Tolerance to ethanol was induced in male Sprague–Dawley rats (225 – 250 g) by chronic feeding with a liquid diet containing 6.5% ethanol (v/v). Control rats were pair-fed with a liquid diet in which the ethanol was replaced by an equicaloric concentration of sucrose. Immediately following sacrifice of the animals the neurointermediate lobes (NIL) were removed and incubated with [3H]phenylalanine. The biosynthesized proopiomelanocortin (POMC), β-lipotropin β-LPH), and β-endorphin (β-EP) were purified by immunoprecipitation with an antiserum to β-EP and analyzed by sodium dodecyl sulfate poly-acrylamide disc gel electrophoresis. Alcohol treatment for 3 days had no effect on the degree of incorporation of [3H]phenylalanine into POMC, β-LPH, and β-EP but treatment for either 15 or 21 days increased the incorporation of [3H]phenylalanine into all three peptides. Ethanol treatment also increased the β-endorphinlike immunoreactivity (β-EPLIR) found in the incubation medium, but no significant change was observed in the β-EPLIR extracted from the NIL either immediately after sacrifice or after 3 h of incubation of the NIL. However, a significant decrease of β-EPLIR was found in the anterior lobes of rats treated with ethanol for 21 days. Furthermore, the β-EPLIR in the serum of alcohol-treated rats was significantly higher than in the serum of their corresponding controls. These results indicate an effect of ethanol on the endorphin system and are consistent with the suggestion that endorphins may be mediators of some of the ethanol effects.

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).


1984 ◽  
Vol 247 (3) ◽  
pp. C282-C287 ◽  
Author(s):  
C. S. Lo ◽  
L. E. Klein ◽  
T. N. Lo

The effect of L-3,5,3'-triiodothyronine (T3) (50 micrograms/100 body wt) on the incorporation of labeled glucosamine and fucose into the subunits of Na+-K+-ATPase was examined by gel electrophoresis in sodium dodecyl sulfate. T3 augmented the incorporation of glucosamine into the alpha- and beta-subunits by 51 and 58%, respectively, in the 22-h chase experiments. Similarly T3 augmented the incorporation of fucose into the alpha- and beta-subunits by 58 and 43%, respectively. Reverse T3 did not alter the incorporation of labeled fucose in either subunit. The effect of T3 on the rate constant of degradation of renal cortical Na+-K+-ATPase was assessed. The rate constant of degradation (Kd) of the [3H]fucose labeled alpha- and beta-subunits for the hypothyroid rats were both 0.20, and for T3-treated rats, the Kd of the alpha- and beta-subunits were 0.23 and 0.18, respectively, suggesting that T3 enhanced fucose incorporation into the subunits of Na+-K+-ATPase rather than retarding the degradation of this enzyme.


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