Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.3.5 (
5'-nucleotidase
)
3,167
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The regulation of adrenergic receptors in rat heart was measured in rats made hyperthyroid by injection with thyroxine and made hypothyroid by addition of propylthiouracil to the drinking water. Hyperthyroid rats display cardiac hypertrophy and a decrease in epididymal fat pad weight. The maximal beta-receptor level of ventricular membranes, as determined by (-)-[3H]dihydroalprenolol binding, was increased 60% by thyroxine treatment and decreased about 30% by propylthiouracil treatment. The affinity of the beta receptor was unchanged after thyroxine or propylthiouracil treatment. The maximal activity of the isoproterenol-stimulated adenylate cyclase (EC 4.6.1.1) varied with thyroid state in a manner parallel to the increase in beta-adrenergic binding sites. Thyroxine treatment also increases by 2-fold the beta receptors in isolated rat fat cells.
Propylthiouracil
treatment lowered the level of alpha receptors in heart by 30% as measured by [3H]dihydroergocryptine binding, but increased the affinity about 2.5-fold. The highest level of alpha receptors was seen in control hearts. These studies indicate that thyroxine may control the turnover of beta-adrenergic receptors in heart and fat cells and regulate physiological responses in these tissues via a hormone-hormone interplay system. Thyroxine treatment reduced the activity of the membrane-bound Mg2+-ATPase (EC 3.6.1.3) and
5'-mononucleotidase
(
EC 3.1.3.5
) but appears to increase the activity of the (Na+ + K+)ATPase (EC 3.6.1.4).
...
PMID:Hormone action at the membrane level. VIII. Adrenergic receptors in rat heart and adipocytes and their modulation by thyroxine. 14 63
Bovine anterior pituitary glands were fractionated by differential centrifugation. T4 5'-monodeiodination to T3 was found predominantly in microsomal fractions (M2; 105,000 . g pellet) enriched in glucose-6-phosphatase and
5'-nucleotidase
activities. T4 5'-deiodinase activity in M2 fraction was 85.2 fmol T3/min X mg protein and represented an 8.5-fold enrichment over homogenate specific activity (10.6 fmol T3/min . mg protein). Further subcellular localization of the T4 5'-deiodinase was effected by discontinuous sucrose density gradient centrifugation. Maximum T4 5'-deiodinase activity was found in fraction P5 at the interface of densities 1.18/1.20 (200 fmol T3/min . mg protein) and correlated with the profile of glucose-6-phosphatase and not with that of
5'-nucleotidase
, the maximum activity of which was recovered in fraction P1 at the interface of densities 1.03/1.12. Electron microscopic examination of the fractions confirmed that P5 contained in excess of 90% rough membranes in contrast to 10% or less in P1. Characterization of T4 5'-deiodinase activity was carried out in M2 preparations. The reaction was thiol dependent, requiring the presence of 50 mM dithiothreitol or more (Km, 38 mM), with a maximum velocity of 55-150 fmol T3/min . mg protein (n = 8). Enzyme activity was substrate dependent, with a Km for T4 between 35-70 nM. 5'-Monodeiodination of T4 was abolished by heating to 70 C for 30 min and was unaffected by EDTA.
Propylthiouracil
and methimazole did not inhibit T3 generation. Iopanoic acid, on the other hand, was a competitive inhibitor of the 5'-monodeiodination reaction, abolishing T3 production in a dose-dependent manner with a Ki of 3 microM. These data indicate that the bovine anterior pituitary contains significant T4 5'-deiodinase activity, which shares many properties of the type II 5'-deiodinase of the rat. Bovine anterior pituitary T4 5'-deiodinase appears to be predominantly localized in the rough endoplasmic reticulum.
...
PMID:Subcellular localization of thyroxine 5'-deiodinase activity in bovine anterior pituitary. 406 44
Postnatal ontogeny of rat liver alpha 1-adrenergic receptor was examined using alpha 1-specific radioligand [3H]prazosin in control and propylthiouracil-treated congenital hypothyroid rats at various ages. Partially purified rat liver membranes prepared by the Neville method had 8-fold purification of
5'-nucleotidase
from the crude homogenates from postnatal day 5 to adulthood. [3H]Prazosin binding was typical of an alpha 1-adrenergic receptor, and (-)epinephrine affinity for the [3H]prazosin-binding sites was not altered in the presence of 10(-5) M guanylyl-imidodiphosphate. The receptor density was lower in 5- and 15-day-old rats than in 28-day-old or older rats in both control and hypothyroid groups. (P less than 0.01). At 28-34 days of age, hypothyroid pups had significantly lower alpha 1-receptor density than controls (399 +/- 10 vs. 869 +/- 40 fmol mg protein-1; P less than 0.01). Replacement therapy with daily T4 injection from postnatal days 16-27 restored 54% of the deficit in
PTU
-treated hypothyroid pups at 28 days. The dissociation constant of [3H] prazosin did not change with advancing age or with different treatment and was consistent at 0.1 nM. These findings indicate that the normal ontogeny of plasma membrane alpha 1-adrenergic receptors is dependent upon thyroid hormone and matures postnatally in rat liver.
...
PMID:Normal ontogeny of alpha 1-adrenergic receptor in rat liver is thyroid hormone dependent. 630 46