Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 20 de 28
Filter
Add more filters










Publication year range
1.
Alcohol Clin Exp Res ; 18(6): 1386-91, 1994 Dec.
Article in English | MEDLINE | ID: mdl-7695034

ABSTRACT

The aim of the study was to ascertain whether the exposure to ethanol of human colon carcinoma CaCo-2 and HT-29 cell lines affects the differentiation process. As an index of enterocytic differentiation, the expression of sucrase, alkaline phosphatase, alpha 2,6-sialyltransferase toward the N-acetyllactosaminic sequence, and beta 1,4-N-acetylgalactosaminyltransferase (beta 1,4GalNAc-transferase) was examined. The latter enzyme is responsible for the biosynthesis of Sda carbohydrate histo-blood antigen, which mainly occurs in human colonic cells; its expression in CaCo-2 cells depends strictly on the enterocytic differentiation. The addition of ethanol in the culture medium resulted in a significant increment of sucrase and alpha 2,6-sialyltransferase activities in both cell lines, as well as the beta 1,4GalNAc-transferase activity in CaCo-2 cells and alkaline phosphatase activity in HT-29 cells. The increment was dose-dependent in the range between 50 and 200 mM ethanol and evident after 2 days of exposure in both cell systems. These results support the notion that, as occurs for cell lines of different origin, the ethanol in vitro positively affects the differentiation of intestinal cells, namely along the enterocytic lineage. The putative mechanism by which ethanol interferes with the maturation process of colonic cells is discussed.


Subject(s)
Cell Differentiation/drug effects , Cell Transformation, Neoplastic/drug effects , Ethanol/pharmacology , Tumor Cells, Cultured/drug effects , Cell Division/drug effects , Cell Line , Cell Survival/drug effects , Colonic Neoplasms , Dose-Response Relationship, Drug , Enzymes/metabolism , Humans , Intestinal Mucosa/drug effects , Intestinal Mucosa/enzymology
2.
Alcohol Clin Exp Res ; 13(6): 841-4, 1989 Dec.
Article in English | MEDLINE | ID: mdl-2690670

ABSTRACT

The status of xanthine oxidase in ethanol-induced liver injury has been investigated in the rat, by acute and chronic ethanol treatments. A 38% increase of the enzyme O-form was observed after repeated ethanol administration. Chronic intoxication caused a significant decrease of total xanthine oxidase activity after both prolonged ethanol feeding and life span ethanol ingestion. The intermediate D/O-form of xanthine oxidase (that can act either as an oxidase or as a dehydrogenase, being able to react with O2 as well as with NAD+ as electron acceptor) increased 5.5-fold after prolonged ethanol feeding.


Subject(s)
Alcoholic Intoxication/enzymology , Alcoholism/enzymology , Liver/enzymology , Xanthine Oxidase/metabolism , Animals , Female , Male , Rats , Rats, Inbred Strains
3.
Alcohol Clin Exp Res ; 13(5): 649-53, 1989 Oct.
Article in English | MEDLINE | ID: mdl-2688463

ABSTRACT

The effect of a single administration and a 6-week treatment with ethanol on rat liver sialyltransferase activity towards asialoglycoproteins and N-acetyllactosamine (Gal beta 1,4GlcNAc) was studied. Since only the alpha 2,6-sialyltransferase is involved in the in vivo sialylation of transferrin, Gal beta 1,4GlcNAc was chosen as an acceptor and alpha 2,6-sialyl-N-acetyllactosamine was separated from the corresponding alpha 2,3-sialyl isomer present in the sialyltransferase reaction mixture by high-performance liquid chromatography. After a single ethanol administration there was a low (about 20%) but significant (p less than 0.005) reduction of sialyltransferase activity towards asialotransferrin as well as a reduced alpha 2,6-sialyltransferase activity towards N-acetyllactosamine. An opposite result was found in the chronically ethanol-treated rats: in these animals either the total or alpha 2,6-sialyltransferase activity was slightly higher than in control animals. Blood ethanol concentration was significantly high (3.3 +/- 1.2 mg/ml) only in the acute-treated animals, suggesting that the accumulation in the body of ethanol and/or its metabolites induces a reduction of liver alpha 2,6-sialyltransferase activity responsible for the transferrin sialylation. Current results are consistent with the finding (Stibler H, Hultcrantz R: Alcohol Clin Exp Res 11:468-473, 1987) that an enhanced level of hyposialylated transferrin isoforms is a marker of present but not previous alcohol abuse.


Subject(s)
Alcoholic Intoxication/enzymology , Alcoholism/enzymology , Sialyltransferases/blood , Transferrin/analogs & derivatives , Transferrin/analysis , Amino Sugars/blood , Animals , Biomarkers/blood , Female , Male , Rats , Rats, Inbred Strains , beta-D-Galactoside alpha 2-6-Sialyltransferase , beta-Galactoside alpha-2,3-Sialyltransferase
4.
Boll Soc Ital Biol Sper ; 54(23): 2444-9, 1978 Dec 15.
Article in Italian | MEDLINE | ID: mdl-756742

ABSTRACT

It was tested on guinea-pig "Taenia-Coli" the interaction between ATN II and Ach in order to elucidate if there is an antagonism or an independence in the action of the two substances. It was concluded that there is no antagonism but a certain degree of interference.


Subject(s)
Acetylcholine/pharmacology , Angiotensin II/pharmacology , Intestine, Large/drug effects , Acetylcholine/antagonists & inhibitors , Action Potentials/drug effects , Angiotensin II/antagonists & inhibitors , Animals , Drug Interactions , Guinea Pigs , Intestine, Large/physiology
5.
Boll Soc Ital Biol Sper ; 54(22): 2305-7, 1978 Nov 30.
Article in Italian | MEDLINE | ID: mdl-754732

ABSTRACT

This research was carried on denervated isolated rat stomach. Mechanical response to Ach treated with three different ATN II concentrations was recorded. No competitive antagonism was observed so that no common receptor can be supposed. The apparent noncompetitive antagonism may be ascribed to the action of ATN II on P and T Ca++ activating systems.


Subject(s)
Acetylcholine/pharmacology , Angiotensin II/pharmacology , Muscle, Smooth/drug effects , Stomach/drug effects , Acetylcholine/antagonists & inhibitors , Angiotensin II/antagonists & inhibitors , Animals , Drug Interactions , Muscle Contraction/drug effects , Rats
6.
Boll Soc Ital Biol Sper ; 54(22): 2319-25, 1978 Nov 30.
Article in Italian | MEDLINE | ID: mdl-224892

ABSTRACT

Male and female rats were treated with estradiol benzoate in the 5 degrees day of life. The avoidance conditioning, tested after 65 days, was significatively impaired in males treated with estradiol, a significative retardation was observed in females treated, but no significant end-difference versus no-treated females. It is supposed that a hormone induced synaptic shaft/spines ratio in preoptic area may be involved in avoidance conditioning.


Subject(s)
Avoidance Learning/drug effects , Estradiol/pharmacology , Amygdala/drug effects , Animals , Female , Gonadotropins/metabolism , Male , Preoptic Area/drug effects , Rats , Receptors, Neurotransmitter/drug effects , Sex Factors
7.
Arch Sci Biol (Bologna) ; 62(1-4): 77-82, 1978.
Article in English | MEDLINE | ID: mdl-122142

ABSTRACT

The concentrations of gamma-amino-n-butyric acid in brains of rats intoxicated with half intraperitoneal LD50 ethanol were determined at various times and found increased at early times (10 min) and decreased later (1 to 3 hours). The concentration tended to be restored to normal values upon administration of n-dipropylacetate (400 mg/kg) or L-glutamine (340 mg/kg). The treatment with both substances showed a positive interaction with an overall positive effect greater than the sum of each.


Subject(s)
Alcoholic Intoxication/drug therapy , Brain Chemistry , Glutamine/therapeutic use , Valproic Acid/therapeutic use , gamma-Aminobutyric Acid/analysis , Alcoholic Intoxication/metabolism , Animals , Drug Synergism , Drug Therapy, Combination , Glutamine/administration & dosage , Humans , Male , Rats , Valproic Acid/administration & dosage
SELECTION OF CITATIONS
SEARCH DETAIL
...