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J L Leonard

Publications and source records attributed to J L Leonard.

At least 73 records · Page 4Linked to original sources

Selective modification of the active center of renal iodothyronine 5'-deiodinase by iodoacetate.

Pretreatment of renal iodothyronine 5'-deiodinase with sulfhydryl reagents, iodoacetate, iodoacetamide and N-alkylmaleimides, results in irreversible loss of catalytic activity. Iodoacetate and iodoacetamide were the most potent inhibitors, being 100- to 1000-times more potent than N-alkylmaleimides. Iodoacetate and iodoacetamide inactivation followed pseudo-first-order kinetics with maximum inactivation rate constants of 1.56 min-1 and 0.87 min-1, respectively. Thyroxine and 3,3',5'-triiodothyronine and the competitive inhibitor iopanoate, protected the enzyme against iodoacetate inhibition. Protection by 3,3',5'-triiodothyronine was competitive with iodoacetate with a dissociation constant (Kd) of 113 nM; in close agreement with the Km for rT3 of 190 nM determined under similar reaction conditions. [3H]Carboxymethylation of renal membranes in the absence and presence of 3,3',5'-triiodothyronine showed specific incorporation of iodo[3H]acetate into substrate-protected sites of 35-40% of total when non-essential residues were first blocked with excess unlabeled iodoacetate. ' Protectable ' [3H]acetate incorporation followed pseudo-first-order kinetics and the rate constant for incorporation was identical to the rate constant for inactivation. These results indicate that iodoacetate fulfills the minimum criteria for an active-site-directed reagent for renal 5'-deiodinase and that a sulfhydryl group is in close proximity to the iodothyronine-binding site.

Animals↗

Qualitative and quantitative differences in the pathways of extrathyroidal triiodothyronine generation between euthyroid and hypothyroid rats.

Propylthiouracil (PTU) in maximally inhibitory doses for liver and kidney iodothyronine 5'-deiodinase activity (5'D-I), reduces extrathyroidal T4 to T3 conversion by only 60-70% in euthyroid rats. A second pathway of T4 to T3 conversion (5'D-II) has been found in pituitary, central nervous system, and brown adipose tissue. 5'D-II is insensitive to PTU and increases in hypothyroidism, whereas 5'D-I decreases in hypothyroid rats. Thyroxine (T4) and triiodothyronine (T3) kinetics were assessed in euthyroid and thyroidectomized rats by noncompartmental analysis after injecting [125I]T4 and [131I]T3. Neither the volume of distribution nor the rate of fractional removal of plasma T4 was affected by the thyroid status, but the fractional removal rate of T3 was approximately 50% reduced in hypothyroid rats (P less than 0.001). Fractional T4 to T3 conversion was 22% in euthyroid and 26% in hypothyroid rats. In euthyroid rats, sufficient PTU to inhibit liver and kidney 5'D-I greater than 90% reduced serum [125I]T3 after [125I]T4 (results given as percent dose per milliliter X 10(-3) +/- SEM): 4 h, control 16 +/- 2 vs. PTU 4 +/- 1, P less than 0.005, and 22 h, control 6.4 +/- 0.4 vs. PTU 3.6 +/- 0.7, P less than 0.025. In thyroidectomized rats, the same dose of PTU also inhibited 5'D-I in liver and kidney, but had no effect on the generation of serum [125I]T3 from [125I]T4. Similarly, after 1 microgram T4/100 g bw was given to thyroidectomized rats, serum T3 (radioimmunoassay) increased by 0.30 +/- 0.6 ng/ml in controls and 0.31 +/- 0.09 ng/ml in PTU-treated rats. However, when the dose of T4 was increased to 2-10 micrograms/100 g bw, PTU pretreatment significantly reduced the increment in serum T3. T3 clearance was not affected by PTU in hypothyroid rats. The 5'D-II in brain, pituitary, and brown adipose tissue was reduced to less than or equal to 60% of control by 30 micrograms/100 g bw reverse T3 (rT3), an effect that lasted for at least 3 h after rT3 had been cleared. In rT3-pretreated thyroidectomized rats, the generation of [125I]T3 from tracer [125I]T4 was reduced in the serum: 6 +/- 1 vs. 12 +/- 1 X 10(-3)% dose/ml, P less than 0.01, during this 3-h period. We conclude that virtually all the T3 produced from low doses of exogenous T4 given to hypothyroid rats is generated via a PTU-insensitive pathway, presumably catalyzed by the 5'D-II. This is a consequence of the enhanced activity of this low Km enzyme together with the concomitant decrease in the hepatic and renal 5'D-I characteristic of the hypothyroid state. The results indicate that in some circumstances, 5D-II activity may contribute to the extracellular, as well as intracellular, T3 pool.

Adipose Tissue↗

Acute posttranscriptional regulation of cerebrocortical and pituitary iodothyronine 5'-deiodinases by thyroid hormone.

Cerebrocortical and pituitary iodothyronine 5'-deiodinases produce 50% or more of the T3 found in these tissues and show rapid 3- to 5-fold changes in response to changes in the thyroid status. Since many T3 responses are initiated in the cell nucleus and require protein synthesis, we studied the influence of cycloheximide and actinomycin D on the acute T3 suppression of cerebrocortical and pituitary 5'-deiodinase activities in hypothyroid rats. Cycloheximide inhibited protein synthesis by more than 95%, but did not prevent the rapid (4-h) T3-mediated decreases in 5'-deiodinase activity. In the presence of cycloheximide, T3 decreased enzyme activity by more than 85%, with a t1/2 of approximately 70 min in the cerebral cortex and about 110 min in the pituitary. In vitro, neither T3 nor cycloheximide in large excess had any effect on enzyme activity. In cycloheximide-treated rats, cerebrocortical 5'-deiodinase activity decreased with a fractional turnover rate (k) of 1.2 h-1 in euthyroid and 0.07 h-1 in hypothyroid rats, respectively, with corresponding steady state enzyme levels of 18 +/- 3 and 145 +/- 9 U/mg protein. The resulting production rates of cerebrocortical 5'-deiodinase were 22 and 10 U/mg protein X h. Actinomycin D failed to alter either the cerebrocortical 5'-deiodinase in euthyroid rats in 4 h or the inhibitory effect of T3, but inhibited RNA synthesis by more than 70%. These data indicate that the T3-dependent fall in cerebrocortical 5'-deiodinase is mediated by a posttranscriptional mechanism that ultimately increases the rate of degradation/inactivation of the enzyme.

Animals↗

Regulation of thyroxine 5'-deiodinase activity by 3,5,3'-triiodothyronine in cultured rat anterior pituitary cells.

The influence of the medium T3 concentration on iodothyronine 5'-deiodinase activity was studied in cultured anterior pituitary cells derived from chronically hypothyroid rats. Type II (propylthiouracil-insensitive) enzyme activity, measured with T4 as substrate, was reduced by T3 in a dose-dependent manner, with an ED50 of approximately 1.4 X 10(-10) M free T3. Density gradient centrifugation was used to obtain populations of pituitary cells relatively enriched in thyrotrophs, somatotrophs, mammotrophs, or gonadotrophs, and the effect of T3 on type II 5'-deiodinase activity was evaluated in each of these four populations. In the absence of T3, the enzyme activity was 1.5- to 2-fold greater in the somatotroph- and mammotroph-enriched cell pools than in the thyrotroph- and gonadotroph-enriched pools. In contrast, when the cells were cultured in the presence of T3, enzyme activity was reduced to the same low level in all four enriched pools. The results suggest that the increase in whole pituitary type II 5'-deiodinase activity associated with hypothyroidism is due largely or totally to increases occurring within somatotrophs and mammotrophs. The data also suggest that the intrinsic responsiveness of the deiodinase to hypothyroidism is greater in somatotrophs and mammotrophs than in other anterior pituitary cells.

Adrenocorticotropic Hormone↗

Differential sensitivity of brain iodothyronine 5'-deiodinases to sulfhydryl-blocking reagents.

Propylthiouracil (PTU) and iodoacetate (IAc) partially inhibit the 5'-deiodination of 3,3',5'-triiodothyronine (rT3) in cerebral cortex, but PTU has no effect on the 5'-deiodination of thyroxine (T4). We now report that pretreatment of cerebral cortex microsomes with increasing concentrations of IAc or iodoacetamide inhibits the PTU-sensitive 5'-deiodination of rT3 with half-maximal inhibition at less than 1 microM IAc. PTU-insensitive 5'-deiodination of rT3 and T4 requires 100-1000-fold higher concentrations of IAc to achieve similar inhibition. Trypsinization decreases both 5'-deiodinating activities by greater than 90%. These data suggest that enzyme SH groups do not participate in the 5'-deiodination of T4 or rT3 by the PTU-insensitive pathway.

Animals↗

Evidence for two pathways of iodothyronine 5'-deiodination in rat pituitary that differ in kinetics, propylthiouracil sensitivity, and response to hypothyroidism.

We have studied 5'-deiodination of thyroxine (T(4)) and 3,3',5'-triiodothyronine (rT(3)) in rat pituitary tissue in vitro, with respect to substrate specificity, reaction kinetics, effects of 6-n-propyl-2-thiouracil (PTU), and the time course of effects of thyroid hormone depletion and repletion. Removal of one phenolic iodine or both tyrosyl iodines from the T(4) molecule resulted in compounds that were not deiodinated, but alterations in the alanine side chain had little effect.5'-Deiodination of 2 nM rT(3) by pituitary microsomes from euthyroid rats was inhibited >90% by 1 mM PTU, but was inhibited <10% by 100 nM T(4). The apparent Michaelis constant (K(m)) and maximum velocity (V(max)) for rT(3) at 20 mM dithiothreitol (DTT) were 33 nM and 84 pmol/mg protein per h. This reaction followed ping-pong type reaction kinetics when concentrations of DTT were varied. PTU inhibition was competitive with DTT and uncompetitive with rT(3). In contrast, when pituitary microsomes from hypothyroid rats (21 d postthyroidectomy) were used, deiodination of 2 nM rT(3) was inhibited only 20% by 1 mM PTU and up to 80% by 100 nM T(4). At 20 mM DTT, the apparent K(m) and V(max) in hypothyroid microsomes were 4.7 nM rT(3) and 16 pmol/mg protein per h. T(4) was a competitive inhibitor of PTU-insensitive rT(3) 5'-deiodination (K(i) = 1.3 nM). T(4) 5'-deiodination by hypothyroid microsomes was not affected by PTU, was competitively inhibited by rT(3) (K(i), 1.7 nM), and exhibited sequential type reaction kinetics with DTT as cosubstrate. When T(4) 5'-deiodination was measured in euthyroid and hypothyroid microsomes, respectively, the apparent K(m) and V(max) for T(4) at 20 mM DTT, were 0.9 nM and 0.55 pmol/mg protein per h (euthyroid), and 0.8 nM and 6.9 pmol/mg protein per h (hypothyroid). The T(4) 5'-deiodination rate and the PTU-insensitive, but not total, rT(3) 5'-deiodination rate (i.e. measured in the presence and the absence of 1 mM PTU, respectively) in pituitary homogenates were significantly elevated 24 h after thyroidectomy. PTU-insensitive activity continued to increase until at >/=30 d after thyroidectomy it was 11 times the PTU-insensitive activity in controls. At the latter time, PTU-sensitive rT(3) 5'-deiodinase activity appeared to be decreased. The increase in PTU-insensitive T(4) and rT(3) 5'-deiodination observed 48 h after thyroidectomy was prevented by replacement doses of T(4) or T(3). The PTU-insensitive activity of long term hypothyroid pituitaries was decreased by 71% and >/=84% 4 h after injection of 20 and 200 mug T(3), respectively, with no change in PTU-sensitive rT(3) deiodination. These data show that rat pituitary tissue contains two distinct iodothyronine 5'-deiodinating pathways that differ with respect to substrate specificity, PTU sensitivity, reaction kinetics, and regulation by thyroid hormone. One of these resembles the 5'-deiodinase of liver and kidney, and predominates in euthyroid pituitary tissue in vitro. The other, also found in rat brain, predominates in hypothyroid pituitary tissue, is rapidly responsive to changes in thyroid hormone availability, and, as judged by previous, in vivo studies, appears to account for all the T(3) produced locally in the pituitary and, thereby, 50% of the intracellular T(3) in this tissue.

Animals↗

Thyroxine 5'-deiodinase activity in brown adipose tissue.

Homogenates of rat brown adipose tissue (BAT) and epididymal fat pad (EPI) catalyze the 5'-deiodination of 3,3',5'-triiodothyronine (rT3) in the presence of dithiothreitol. BAT, but not EPI, catalyzes the 5'-deiodination of thyroxinE (T4) generating equal amounts of 3,5,3'-triiodothyronine (T3) and iodide. BAT 5'-deiodinase activity was unaffected by propylthiouracil (PTU) and was elevated in hypothyroid rats, whereas EPI 5'-deiodinase was totally inhibited by PTU and was depressed in hypothyroidism. These results indicate that type II (PTU-insensitive) 5'-iodothyronine deiodinase activity is present in BAT.

Adipose Tissue↗

Subcellular distribution of iodothyronine 5'-deiodinase in cerebral cortex from hypothyroid rats.

We have examined iodothyronine deiodination in subcellular fractions of cerebral cortex obtained from hypothyroid rats. Enzymatic activities were measured at 37 degrees C in the presence of 20 mM dithiothreitol with 125I-labeled T4 and 125I-labeled rT3 as substrates for 5'-deiodination and 131I-labeled T3 as the substrate for the 5-deiodinase. Reaction products were separated by descending paper and/or ion-exchange chromatography. Cerebral cortex subcellular fractions were also characterized by marker enzyme analysis and electron microscopy. Under optimal reaction conditions more than 80% of the 5'-deiodinase was recovered after fractionation. Both 5'-deiodinase and (Na+ + K+)-ATPase showed similar subcellular distributions and were enriched approx. 3-fold in the easily sedimenting membrane fraction and nerve terminal plasma membranes. Crude microsomal membranes (6 X 10(6) g X min pellet) also showed 2-fold enrichment of these enzymes. Nuclei and isolated mitochondria were devoid of deiodinating activity. T4 and T3 5-deiodinating activity was absent in the easily sedimenting membranes and present but not enriched in particulate fractions containing microsomal membranes. These data suggest that iodothyronine 5'-deiodinase is associated with plasma membrane fractions in the cerebral cortex.

Animals↗

Kinetic evidence suggesting two mechanisms for iodothyronine 5'-deiodination in rat cerebral cortex.

Enzymatic 5'-deiodination of 3,3',5'-triiodothyronine (rT3) and 3,3',5,5'-tetraiodothyronine (thyroxine, T4) was studied in microsomal preparations of rat cerebral cortex. Evidence was obtained for the existence of two thiol-dependent 5'-deiodinase entities. One of these predominates in tissue from euthyroid and long-term hypothyroid rats, is specific for rT3, follows "ping-pong" kinetics with dithiothreitol as the cosubstrate, and is inhibited by propylthiouracil (PrSUra) and iodoacetate. Inhibition by PrSUra is uncompetitive with rT3 and competitive with dithiothreitol. These properties are shared with the 5'-deiodinase activity of liver and kidney. The activity of a second type of 5'-deiodinase is highest in cerebral cortex from short-term hypothyroid rats, prefers T4 to rT3 as the substrate, is insensitive to PrSUra and iodoacetate, and follows "sequential" reaction kinetics. A similar PrSUra-insensitive 5'-deiodinase activity is also found in pituitary but is not detectable in liver and kidney; it seems, therefore, characteristic of tissues in which local T4 to 3,3',5-triiodothyronine (T3) conversion supplies a major portion of the total intracellular T3.

Animals↗

Evidence for two tissue-specific pathways for in vivo thyroxine 5'-deiodination in the rat.

Propylthiouracil (PTU) is a well known inhibitor of thyroxine (T(4)) to triiodothyronine (T(3)) conversion as evidenced by its effect in several in vitro systems and by the decrease in serum T(3) caused by this drug in either rats or man receiving T(4) replacement. However, the failure of PTU to decrease the intrapituitary T(3) concentration and to completely blunt the serum T(3) concentration in T(4)-replaced athyreotic rats suggest that there may be a PTU-insensitive pathway of T(4) to T(3) conversion in some tissues. To address this question, we have studied the in vivo effect of PTU treatment on the generation of [(125)I]T(3) from [(125)I]T(4) in the serum and cerebral cortex (Cx), cerebellum (Cm), liver (L), and anterior pituitary (P) of euthyroid rats. Whereas PTU decreased the concentration of [(125)I]T(3) in the serum, L homogenates, and L nuclei after [(125)I]T(4), it did not affect the concentration of [(125)I]T(3) in homogenates or nuclei of Cx, Cm, or P. Iopanoic acid pretreatment significantly reduced the [(125)I]T(3) concentration in serum, homogenates, and cell nuclei of all these organs. Neither agent affected the metabolism or tissue distribution of simultaneously injected [(131)I]T(3). The presence of PTU in these tissues was evaluated by in vitro assessment of iodothyronine 5'-deiodinating activity using both [(125)I]rT(3) and [(125)I]T(4) as substrates. In agreement with the in vivo findings, generation of [(125)I]T(3) from T(4) in vitro was not affected by PTU in Cx, Cm, P but it was inhibited by 76% in L. However, rT(3) 5'-deiodination, known to be sensitive to PTU in these tissues, was inhibited in all four indicating that the PTU given in vivo was present in significant amounts. These results demonstrate that in rat Cx, Cm, and P unlike liver, PTU does not inhibit T(4) to T(3) conversion in vivo despite the presence of the drug in the tissues in amounts that significantly inhibit reverse T(3) 5'-deiodination. These results show that in vivo 5'-deiodination of T(4) proceeds via a PTU-insensitive pathway in the central nervous system and pituitary, while this pathway is not quantitatively important in the L. This mechanism accounts for the "locally generated" T(3) in central nervous system and pituitary and could also provide the approximately one-third of extrathyroidally produced T(3) not blocked by PTU administration in athyreotic T(4)-replaced rat.

Animals↗

Cerebral cortex responds rapidly to thyroid hormones.

In rats subjected to thyroidectomy there was a two- to fourfold increase in cerebral cortex iodothyronine 5'-deiodinase activity within 24 hours. This increase was prevented by thyroxine replacement. The increased cortical 5'-deiodinase in chronically hypothyroid rats was normalized within 4 hours by a single intravenous injection of triiodothyronine. These results indicate that the adult central nervous system can give a very rapid biochemical response to thyroid hormone.

Animals↗

Solubilization of a phospholipid-requiring enzyme, iodothyronine 5'-deiodinase, from rat kidney membranes.

Enzymic activities catalyzing the reductive 5'-deiodination of thyroxine and 3,3',5'-triiodothyronine were solubilized from rat kidney microsomes by treatment with 0.2% deoxycholate. Deoxycholate reversibly inhibited the enzyme(s); removal of detergent restored activity and resulted in the formation of enzymatically active aggregates with a buoyant density of 1.17 g/ml resembling that of membranes. Fractionation of the solubilized membrane components in the presence of 0.2% deoxycholate by either gel filtration or sucrose gradient centrifugation inactivated the enzyme(s) and activity could be restored by the addition of partially purified soybean phospholipids; this allowed some of the physical properties of the enzyme(s) to be determined. 5'-Deiodinating activity of both thyroxine and 3,3',5'-triiodothyronine was associated with protein(s) with S20,W of 3.5 S, Stokes' radius of 32 A, and a calculated molecular weight of 49 900. A partial specific volume of 0.74 cm3/g was calculated from sedimentation in 2H2O and H2O sucrose gradients. Phospholipid reactivation of lipid-depleted enzyme preparations was concentration-dependent, with near maximal restoration when sufficient phospholipid was added to restore the phospholipid:protein ratio to that of thyroxine and 3,3',5'-triiodothyronine could not be resolved by sedimentation or molecular sieving and showed similar behavior toward deoxycholate solubilization and phospholipid reconstitution.

Animals↗

Surgical treatment of acute evolving anterior myocardial infarction.

A series of 101 consecutive patients underwent coronary revascularization within a mean of 5.8 hours after anterior myocardial infarction. Forty-one patients had obstruction of the left anterior descending coronary artery (LAD), 35 had obstruction of the LAD and of the right or circumflex coronary artery and 25 had obstruction of the LAD and both the right and circumflex coronary arteries. Sixty-four patients (63%) had total occlusion of the LAD. In-hospital mortality was 2%. The total mortality during a mean follow-up of 43 months was 5%, and 90% of the patients were free of angina. Thirty-six patients had repeat coronary arteriography a mean of 13.4 months after operation. Fifty-two of 62 grafts (84%) were patent. Cardiac catheterization and immediate coronary artery bypass grafting in the first hours of anterior myocardial infarction can be done safely and may reduce in-hospital and long-term mortality.

Adult↗