Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.5 (5'-nucleotidase)
 3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ecto-enzyme 5'-nucleotidase isolated from chicken gizzard has previously been shown to be a potent ligand of two glycoproteins of the extracellular matrix, namely fibronectin and laminin. Using immunofluorescent labeling techniques we observed that 5'-nucleotidase codistributed with laminin during the development of chicken striated muscle. In contrast, ecto-5'-nucleotidase was only faintly detectable on cells surrounded by a matrix expressing high levels of fibronectin. This distribution pattern distinguished 5'-nucleotidase from the pluripotent extracellular matrix receptors, chicken beta 1-integrins, which are expressed equally well in muscle and connective tissue. In addition, the specific activity of striated muscle ecto-5'-nucleotidase was stable during development and increased markedly posthatching. At each age considered, this specific activity corresponded to an 80-kDa enzyme which was inhibited by alpha,beta-methyleneadenosine diphosphate or by a monoclonal antibody directed against the smooth muscle isoform of the enzyme. Previous in vitro studies have revealed that 5'-nucleotidase is involved in the spreading of various mesenchyme-derived cells, such as chicken embryonic fibroblasts and myoblasts, on a laminin substrate. A prerequisite to examining a potential in vivo role for 5'-nucleotidase as an extracellular matrix ligand was to study its distribution. In adult muscle, 5'-nucleotidase displayed a more restricted distribution than in embryo. Results show that, in vivo, 5'-nucleotidase is revealed by immunofluorescent labeling using poly- and monoclonal antibodies to chicken gizzard 5'-nucleotidase in two structures, the costameres and myotendinous junctions, which are closely related to the focal adhesion sites observed in cell culture.
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PMID:Enzymatic activity and in vivo distribution of 5'-nucleotidase, an extracellular matrix binding glycoprotein, during the development of chicken striated muscle. 133 Jun 59

The fetal sheep heart responds to beta-adrenergic stimuli; however, in vivo studies show the response of the fetal heart is less than that of the adult heart. We used [3H]dihydroalprenolol (DHA) to study directly beta-adrenergic receptors in heart particulates of fetal sheep at term and adult sheep. [3H]DHA binding to fetal heart particulates was rapid, reversible (t 1/2 = 2.9 +/- 0.3 min), stereoselective, saturable (101.2 +/- 7.4 fmoles/mg protein), and of high affinity (4.8 +/- 0.4 nM). The rank order of agonists competing for [3H]DHA binding was isoproterenol (0.32 +/- 0.10 microM) greater than epinephrine (1.19 +/- 0.23 muM) approximately equal to norepinephrine (2.67 +/- 0.69 muM), which is compatible with beta 1-adrenergic potencies. [3H]DHA also bound to the adult sheep heart in a manner expected for beta 1-receptors. No difference in the binding affinity of [3H]DHA or agonists' competition was demonstrated between the fetal and adult sheep heart. Comparison of the concentration of beta-adrenergic receptors in fetal and adult hearts was confounded by the choice of the denominator for unit expression. The concentration was higher in the adult when expressed as a function of protein content or 5'-nucleotidase activity (0.52 +/- 0.07 versus 1.12 +/- 0.06). However, there was no difference when tissue weight, Na+ - K+-ATPase, or NaF-stimulated adenylate cyclase was used. Furthermore, isoproterenol-stimulated adenylate cyclase and cardiac contractile response to a threshold dose of isoproterenol were identical in the fetal and adult sheep heart. We conclude that beta-receptors can be studied with [3H]DHA in the fetal sheep heart, this receptor is qualitatively similar to the beta-receptor in the adult sheep heart, and it is unlikely that there is a difference in the concentration of beta-adrenergic receptors in fetal and adult sheep heart.
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PMID:Identification of beta-adrenergic receptors using [3H]dihydroalprenolol in fetal sheep heart: direct evidence of qualitative similarity to the receptors in adult sheep heart. 611 56

In fully developed androgen-induced hypertrophy of female mouse kidney, beta-adrenergic receptors per unit membrane protein were increased approx. 2.5-fold, as measured by the binding of [125I]iodocyanopindolol, with no change in apparent dissociation constants (Kd range 20-25 pM). Membrane protein relative to total kidney protein, Na+/K+-dependent ATPase (EC 3.6.1.3) and 5'-nucleotidase (EC 3.1.3.5) activities and cholesterol content per unit membrane protein did not differ significantly in preparations from control and treated animals. The binding of iodocyanopindolol to kidney membranes was characterized with respect to association and dissociation kinetics, and also in regard to the less-specific contributions of other major catecholamine or indolamine receptors, using mixtures of the corresponding specific competitors. beta 1-selective drugs, practolol and metoprolol, and beta 2-selective agents, IPS-339 and zinterol, were competed with iodocyanopindolol to assess the receptor type specificity, and the ensuing binding profiles were dissected by a nonlinear regression analysis as described by Munson, P.J. and Rodbard, D. (Anal. Biochem. (1982) 107, 220-239). Most of the androgen-induced beta-adrenergic receptors had the binding properties corresponding to beta 2-subtype. No consistent increase in the density of beta 1-adrenergic receptors could be shown.
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PMID:Characterization of beta-adrenergic receptor subtypes in androgen-induced mouse kidney hypertrophy using a new high-affinity ligand, [125I]iodocyanopindolol. 629 77