Biomedical subjects

G Alemán

Publications and source records attributed to G Alemán.

4 recordsLinked to original sources

PubMed1998

Regulation of histidase gene expression by glucagon, hydrocortisone and protein-free/high carbohydrate diet in the rat.

The effect of glucagon and hydrocortisone was investigated to understand the mechanism of induction of hepatic histidase gene. In this study, glucagon (0.6 mg/100 g body wt/d) was injected to rats fed 10% casein diet. After 3 h of the last injection, histidase activity and amount of enzyme were induced by 3 fold and histidase mRNA concentration by 6 fold. Injection of hydrocortisone (2 mg/100 g body wt/d) increased 100% histidase activity and mRNA concentration and by 150% the amount of enzyme after 3 h of the last injection. These results indicate that glucagon is a better inductor of histidase gene expression than hydrocortisone. Another purpose of the study was to evaluate if a protein-free/high carbohydrate diet could reverse the induction of Hal expression produced by a high protein diet. Hal activity, amount of enzyme and mRNA concentration was repressed by 68, 88 and 95% respectively by a protein-free/high carbohydrate diet. Injection of glucagon reversed partially the effect of a high carbohydrate diet, however, injection of hydrocortisone under the concentration used in these experiments did not reverse the effect of a high carbohydrate diet. These results support the evidence that hepatic histidase gene expression is probably regulated transcriptionally by hormones.

Animals↗

PubMed1998

Histidase expression is regulated by dietary protein at the pretranslational level in rat liver.

The effect of dietary protein on the expression of histidase (Hal) was investigated to understand the mechanism of induction of histidase by a high protein diet. In this study, we examined the following: 1) the effect of 0, 6, 18, 35 and 50% casein diets on hepatic and epidermal Hal activity, amount of the enzyme and Hal-mRNA; 2) the effect of a high histidine diet (1.25%) on Hal expression; 3) the response of Hal expression in rats fed a 10% casein diet and injected with glucagon (0.6 mg /(100 g body wt.d); and 4) the half-lives of the enzyme and Hal-mRNA in rats fed an 80% casein diet for 7 d followed by a protein-free diet. Hal activity increased as the protein content in the diet increased (r = 0.986, P < 0.001) and was associated with a significant increase in Vmax without a change in Km. The dietary regulation was liver specific because skin Hal was unresponsive. Increments in hepatic Hal activity were accompanied by concomitant significant increases in the amount of histidase and its mRNA. The response was more pronounced in rats fed diets containing >18% casein. Rats fed a 12% casein diet containing 1.25% histidine did not have different Hal activity and mRNA levels compared with rats fed a 12% casein diet, indicating that Hal expression is not modified by its substrate. Injection of glucagon into rats fed the 10% casein diet increased Hal activity threefold and Hal- mRNA expression fivefold compared with uninjected rats fed the same diet. The apparent half-life of hepatic histidase in protein-depleted rats previously fed an 80% casein diet was 2.8 d, whereas the half-life of Hal-mRNA was 17 h. In summary, these data support the hypothesis that Hal expression is regulated by dietary protein at the pretranslational level in rat liver, and that glucagon is one of the hormones involved in the induction of Hal.

Animals↗

PubMed1996

Alanine aminotransferase activity in mammary tissue, muscle and liver of dam rat during lactation and weaning.

Transamination reaction is the first step in the catabolism of most of the L-amino acids. Alanine is an important molecule in the inter-organ nitrogen transport, conveying them from muscle to the liver. Amino groups from this amino acid are generally first transferred to alpha-ketoglutarate in the cytosol of liver cells to form glutamate and leaving behind the corresponding alpha-keto acid analog. Measurements of the alanine aminotransferase (EC2.6.1.2.) activity were compared in liver, mammary gland and skeletal muscle in virgin, lactating and weaning dam rats. In this study liver was the principal tissue involved in alanine transamination, while muscle showed a reduction in the enzyme activity during lactation. Results indicate an increase in alanine amino-transferase activity in the mammary gland during lactation and weaning when compared with virgin rats. This suggests that mammary gland during lactation is an important extra-hepatic tissue involved in the metabolism of alanine and probably shunted into the pathways for amino group metabolism in terms of nitrogen economy.

Alanine Transaminase↗

PubMed1965

[Cavernostomy].

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Adult↗