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E A Ryan

Publications and source records attributed to E A Ryan.

94 records · Page 6Linked to original sources
PubMedDate not supplied

Triiodothyronine (T3) nuclear binding sites in human placenta and decidua.

We studied the binding of triiodothyronine (T3) to human placenta and decidua. Although the placenta effectively blocks transfer of thyroxine (T4) and T3 it may itself be a thyroid hormone-dependent tissue and may specifically bind T3. A single class of high-affinity binding sites was found (Ka 3.8 +/- 0.31 s.e.m., and 3.3 +/- 10(9) M-1) for both placenta and decidua. Limited capacity was also observed, viz., 0.117 +/- 0.01 and 0.102 +/- 0.018 fmoles/microgram deoxyribonucleic acid (DNA), respectively. Endogenous T3 nuclear saturation was 34 per cent. Our results are consistent with the proposal that placenta and decidua have similar T3 specific nuclear binding sites and that T3 may have a direct action in the placenta.

Cell Nucleus↗
PubMedDate not supplied

Identification of multi-S-substituted conjugates of hydroquinone by HPLC-coulometric electrode array analysis and mass spectroscopy.

Chemical reaction of 1,4-benzoquinone with GSH gives rise to several multisubstituted hydroquinone (HQ)-GSH conjugates, each of which causes renal proximal tubular necrosis when administered to male Sprague-Dawley rats. In addition, HQ has recently been reported to be nephrocarcinogenic following long-term exposure in male rats. Since neither the mechanism nor the extent of HQ oxidation and thioether formation in vivo is known, we have assessed both the qualitative and quantitative significance of HQ-thioether formation in vivo and in vitro. HQ (1.8 mmol/kg, ip) was administered to AT-125-pretreated male Sprague-Dawley rats, and bile and urine samples were analyzed with a HPLC-coulometric electrode array system (CEAS) and by liquid chromatography (LC)/continuous-flow fast atom bombardment (CF-FAB) mass spectroscopy. Five S-conjugates of hydroquinone were identified in bile, and one S-conjugate was identified in urine. The major biliary S-conjugate identified was 2-glutathion-S-ylhydroquinone [2-(GSyl)HQ] (18.9 +/- 2.7 mumol). Additional biliary metabolites were 2,5-diglutathion-S-ylhydroquinone [2,5-(diGSyl)HQ] (2.2 +/- 0.6 mumol), 2,6-diglutathion-S-ylhydroquinone [2,6-(diGSyl)HQ] (0.7 +/- 0.3 mumol),2,3,5-triglutathion-S-ylhydroquinone [2,3,5-(triGSyl)HQ] (1.2 +/- 0.1 mumol), and 2-(cystein-S-ylglycyl)hydroquinone. 2-(N-Acetylcystein-S-yl)HQ was the only urinary thioether metabolite (11.4 +/- 3.6 mumol) identified. The quantity of S-conjugates excreted in urine and bile within 4 h of HQ administration [34.3 +/- 4.5 mumol (4.3 +/- 1.1% of dose)] appears sufficient to propose a role for such metabolites in HQ-mediated nephrotoxicity and nephrocarcinogenicity. Rat liver microsomes catalyzed the NADPH-dependent oxidation of HQ (300 microM), in the presence of GSH, to form 2-(GSyl)HQ,2,5-(diGSyl)-HQ, and 2,6-(diGSyl)HQ. A fraction of the microsomal oxidation of HQ appears to be catalyzed by cytochrome(s) P450, although the exact amount remains unclear. 2-(GSyl)HQ,2,5-(diGSyl)-HQ, and 2,6-(diGSyl)HQ (300 microM) also underwent NADPH-dependent oxidation and GSH conjugation in liver microsomes. The extent of the nonenzymatic oxidation of HQ and its GSH conjugates correlated, approximately, with their half-wave oxidation potentials.

Animals↗
PubMedDate not supplied

Assessment of value of glycosylated albumin and protein in detection of gestational diabetes.

There is a recognized need for the early detection of gestational diabetes, and a single blood test, if reliable, would be advantageous. Because serum albumin and total protein are glycosylated and have short life spans, we investigated the usefulness of glycosylated albumin and glycosylated protein in the detection of gestational diabetes. We studied five groups, each with 20 subjects: nonpregnant and pregnant controls, nonpregnant and pregnant insulin-dependent diabetic (IDDM) patients, and gestational diabetic patients. All patients with no history of diabetes had an oral glucose tolerance test to define their carbohydrate status. Our results showed that percent glycosylated albumin and percent glycosylated protein were significantly elevated in both groups of IDDM patients compared with the other groups. However, gestational diabetic patients had glycosylated albumin and glycosylated protein values similar to those of both control groups. Both glycosylated albumin and glycosylated protein correlated well with HbA1c determinations. Thus, glycosylated albumin and glycosylated protein may be a good index of glycemic control, but they are of little value in the diagnosis of gestational diabetes because of a lack of sensitivity: 8 and 3% for glycosylated albumin and glycosylated protein, respectively.

Adult↗