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Biomedical subjects

M Sapag-Hagar

Publications and source records attributed to M Sapag-Hagar.

At least 37 records · Page 2Linked to original sources

Effects of enkephalin on lactating rat mammary gland: in vitro studies.

We studied the in vitro effects of methionine-enkephalin and D-ala-methionine-enkephalin upon lactating rat mammary gland milk product's secretion and intracellular cyclic AMP levels. Our results show that the lactating gland does not respond to the action of these peptides and suggest that during this period this tissue lacks enkephalin receptors.

Animals↗

[Heterologous hormonal regulation in the mammary gland].

Mammary gland growth and differentiation are largely dependent on a complex and interrelated action of many different hormones which makes the mammary tissue a very suitable one for the study of heterologous hormonal regulation. This type of control is analyzed by two different approaches: 1. The participation of estradiol in prolactin action during lactation, and 2. The role of glucocorticoids and thyroid hormones in the control of functional activity of rat mammary gland beta-adrenergic receptors.

Animals↗

The action of hormones on the rat uterus and mammary gland gamma-glutamyltranspeptidase activity.

The gamma-glutamyltranspeptidase activity of rat uterus and mammary gland was studied in ovariectomized, hypophysectomized and ovariectomized-hypophysectomized rats under different hormonal and drug treatments. The uterine enzyme appears to be mainly dependent on a direct action of estradiol and the mammary gland enzymatic activity is dependent on prolactin. Our result, however, do not exclude a possible role of estradiol in the regulation of prolactin effects on mammary gland enzymatic activity.

Animals↗

Modulation of gamma-glutamyl cycle and glutathione levels in rat mammary gland explants.

The reduced glutathione levels and the enzymes gamma-glutamyl-transpeptidase, 5-oxoprolinase and gamma-glutamylcysteine synthetase, which participate in the metabolism of glutathione through the gamma-glutamyl cycle, were determined in explants from the lactating mammary gland of the rat. Significant activities of the enzyme were found. Two modulators of this cycle were used. L-2-Oxothiazolidine-4-carboxylate, an alternative substrate of 5-oxoprolinase and an intracellular cysteine delivery system, increased the reduced glutathione levels under the experimental conditions used. The other compound utilized, DL-buthionine-SR-sulphoximine, an inhibitor of gamma-glutamylcysteine synthetase, significantly decreased the glutathione levels. This effect is slowly reversible.

Amidohydrolases↗

A role for adrenaline and calmodulin in modulating cyclic AMP levels during the lactogenic cycle.

The effect on lactose production of several external modulators of intracellular cyclic AMP was studied in rat mammary gland tissue slices and explants. Adrenaline, a beta-adrenergic receptor effector, forskolin, a direct adenylate cyclase activator and fluphenazine, a calmodulin inhibitor, all produced an increase in the intracellular level of cyclic AMP and a concomitant inhibition of lactose production. These results suggest a role for adrenaline and calmodulin in modulating cyclic AMP levels in mammary tissue during the lactogenic cycle.

Animals↗

Effect of hormones and cyclic AMP on gamma-glutamyltranspeptidase activity of rat mammary gland explants.

gamma-Glutamyl transpeptidase activity was assayed in midpregnant rat mammary gland explants at 14, 22 and 38 h, in the presence and absence of insulin, prolactin and corticosterone. With these 3 hormones the explants attained the characteristics of a secretory gland after 22 h of tissue culture, at which time the enzyme exhibited its maximal activity. The addition of dibutyryl cyclic AMP in the presence of the 3 hormones produced a significant increase in enzyme activity, which was maximal with a 1 mM concentration of the cyclic nucleotide. A similar effect was observed when theophylline or theophylline plus dibutyryl cyclic AMP were added to the culture medium.

Animals↗

Enzymes of mercapturic acid production in rat mammary gland.

1. The enzymes glutathione S-transferase, gamma-glutamyl peptidyltransferase and dipeptidase, which participate in the detoxification pathway through mercapturic acid production, were measured in rat mammary gland during pregnancy and lactation. 2. Mammary-gland concentration of reduced glutathione showed, concomitantly with the enzyme activities, a significant increase during lactation. 3. The mammary-gland glutathione S-transferase exhibits characteristics quite similar to those described for the liver and kidney enzymes with respect to substrates, isoenzymes, molecular weight and probenecid and bilirubin inhibition. 4. In view of these similarities, mammary-gland glutathione S-transferase may play the same role as a cytoplasmic organic-anion receptor proposed for the hepatic enzyme. It may also represent a detoxification pathway for protecting the mammary tissue during the lactogenic cycle.

Acetylcysteine↗

Glutathione and gamma-glutamyl cycle enzymes in rat mammary gland.

The main enzymes of the gamma-glutamyl cycle during the lactogenic cycle in rat mammary gland were studied. A significant increase was found in all of them with the onset of lactogenesis. The effect of methionine sulfoximine on reduced glutathione concentration was studied in tissue slices of lactating mammary gland. The findings suggest that this compound effects glutathione synthesis by inhibiting gamma-glutamylcysteine synthetase.

Animals↗

Properties of gamma-glutamyltranspeptidase, and glutathione levels in rat mammary gland.

gamma-Glutamyltranspeptidase activity and glutathione levels were studied in rat mammary gland during the lactogenic cycle; both increased during mid-lactation. The enzyme's specific activity with several amino acids showed that glutamine and methionine were the best substrates. Maleate decreased the transpeptidation reaction and increased the hydrolytic activity. These results suggest that gamma-glutamyltranspeptidase from the mammary gland is similar to the enzyme described in other tissues in relation to these properties and the physiological role proposed in amino acids transport.

Amino Acids↗

Inorganic pyrophosphatase activity of the synovial fluid. Kinetic and clinical study.

Inorganic pyrophosphatase activity has been partially characterized in joint fluid and determined in patients with sporadic and familial chondrocalcinosis and their controls. Optimal pH was established at 3.5 and Km values were estimated. Ca-2 and Mg-2 did not affect this activity whereas orthophosphate (Pi) strongly inhibited it. In the clinical study no significant differences were found among groups. This suggests that if a pyrophosphatase defect is present it might be localized in joint tissue and not be reflected in synovial fluid.

Adolescent↗