The Properties, Structure, Function, Intracellular Localisation and Movement of Hepatic 5′-Nucleotidase

Luzio, J. Paul; Bailyes, E M; Baron, Michael D.; Siddle, Kenneth; Mullock, Barbara M.; Geuze, Hans J.; Stanley, Keith K.

doi:10.1007/978-3-642-70664-6_8

Cited by 15 publications

(12 citation statements)

References 92 publications

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“…We further examined whether the inhibition of synthesis 5 '-nucleotidase are thought to be primarily responsible for the synthesis of adenosine in the heart (1-3), and both enzymes are affected by a number of metabolic factors (20)(21)(22). Ectosolic 5'-nucleotidase is strongly inhibited by ATP and ADP (20,21), whereas cytosolic 5 '-nucleotidase activity is activated by ATP and ADP, and inhibited by inorganic phosphate (22,23).…”

Section: Resultsmentioning

confidence: 99%

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Evidence for deactivation of both ectosolic and cytosolic 5'-nucleotidase by adenosine A1 receptor activation in the rat cardiomyocytes.

Kitakaze¹,

Hori²,

Minamino³

et al. 1994

J. Clin. Invest.

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Adenosine, an important regulator of many cardiac functions, is produced by ectosolic and cytosolic 5 '-nucleotidase. The activity of these enzymes is influenced by several ischemia-sensitive metabolic factors, e.g., ATP, ADP, H+, and inorganic phosphate. However, there is no clear evidence that adenosine itself affects 5'-nucleotidase activity. This study tested whether adenosine decreases the activity of ectosolic and cytosolic 5 '-nucleotidase. Cardiomyocytes were isolated from adult male Wistar rats and suspended in the modified Hepes-Tyrode buffer solution. After stabilization, isolated cardiomyocytes were incubated with and without adenosine (10-9-i0-' M). .05] at 10-6 M adenosine) after 30 min. The decrease in ectosolic and cytosolic 5 '-nucleotidase activity was inhibited by 8-phenyltheophylline and pertussis toxin, and was mimicked by N6-cyclohexyladenosine, an adenosine Al receptor agonist. Neither CGS21680C, and A2 receptor agonist, nor cycloheximide deactivated ectosolic and cytosolic 5 '-nucleotidase. Thus, we conclude that activation of adenosine A1 receptors is coupled to G; proteins and attenuates ectosolic and cytosolic 5 '-nucleotidase activity in rat cardiomyocytes.

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Section: Resultsmentioning

confidence: 99%

“…Ectosolic 5'-nucleotidase is strongly inhibited by ATP and ADP (20,21), whereas cytosolic 5 '-nucleotidase activity is activated by ATP and ADP, and inhibited by inorganic phosphate (22,23). This study shows that adenosine inhibits both ectosolic and cytosolic 5 '-nucleotidase.…”

Section: Resultsmentioning

confidence: 99%

Evidence for deactivation of both ectosolic and cytosolic 5'-nucleotidase by adenosine A1 receptor activation in the rat cardiomyocytes.

Kitakaze¹,

Hori²,

Minamino³

et al. 1994

J. Clin. Invest.

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“…The enzyme is inhibited weakly by anions, whether chloride, sulphate or phosphate, and strongly by both EDTA and concanavalin A. The inhibitory effects of EDTA and concanavalin A have been found with other nucleotidases (Luzio et al, 1986).…”

Section: Measurement Of Nucleotidase Activitymentioning

confidence: 85%

“…Since the tick extracts contain large quantities of both alkaline and acid phosphatase, figlycerophosphate was included in the assay to prevent non-specific hydrolysis of the AMP substrate. It was found that the hydrolysis of the substrate by either crude extracts or purified enzyme was inhibited completely by the inclusion of 20 /M-p[CHJpA, an inhibitor of 5'-nucleotidase (Luzio et al, 1986;Zachowski et al, 1981). This suggests that the assay is accurately measuring 5'-nucleotidase activity and is unaffected by the presence of phosphatases.…”

Section: Measurement Of Nucleotidase Activitymentioning

confidence: 99%

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Purification and properties of a novel nucleotide-hydrolysing enzyme (5′-nucleotidase) from Boophilus microplus

Willadsen

Nielsen

Riding

1989

Biochemical Journal

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The tick Boophilus microplus contains a nucleoside phosphate-hydrolysing enzyme which, in many respects, resembles the well characterized 5'-nucleotidase from mammalian tissue. The tick enzyme has been purified to homogeneity. It is a membrane-bound glycoprotein with an apparent Mr of 67,000 and, although it fails to hydrolyse a range of nucleoside 2'- or 3'-monophosphates, it has broad specificity for the 5' derivatives. Further investigation of the enzyme's substrate specificity, however, shows some important differences from the mammalian nucleotidases. It hydrolyses both bis-p-nitrophenyl phosphate and p-nitrophenyl phenylphosphonate, typical substrates for phosphodiesterases. However, the tick enzyme is most strikingly different from the mammalian enzymes in that it hydrolyses not only AMP but ADP and ATP as well. Further, the products of the hydrolysis of ATP are adenosine and tripolyphosphate, a reaction which has not been reported previously. The products of ADP hydrolysis are adenosine and pyrophosphate.

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5′‐Nucleotidase: A new marker for striosomal organization in the rat caudoputamen

Schoen

Graybiel

1992

J of Comparative Neurology

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The distribution of the adenosine-producing ectoenzyme 5'-nucleotidase was studied by means of a histochemical lead technique in the caudoputamen of normal adult rats and of rats in which injections either of 6-hydroxydopamine in the medial forebrain bundle or of ibotenic acid in the caudoputamen had been made 1-3 weeks previously. The patterns of striatal 5'-nucleotidase activity in these animals were compared in serial sections to the patterns of calbindin-D28k immunoreactivity and of 3H-naloxone ligand binding, which respectively mark the known matrix and striosome (patch) compartments of the caudoputamen. In the normal rats, 5'-nucleotidase activity was differentially concentrated in striosomes, where it produced a dense staining of the neuropil. The enzymatic staining followed a striosomal distribution in all but the caudal caudoputamen. Within the striatal matrix, 5'-nucleotidase staining also observed a lateromedial density gradient. Depletion of the dopamine-containing nigrostriatal innervation of the caudoputamen with 6-hydroxydopamine did not alter the striosomal selectivity of 5'-nucleotidase activity. Destruction of intrastriatal neurons by ibotenic acid led to a strongly 5'-nucleotidase-positive gliosis within the resulting necrotic region. Elsewhere in the caudoputamen, the enzyme's striosomal distribution was not detectably altered. We conclude that 5'-nucleotidase histochemistry provides an advantageous tool for detecting the striosomal architecture of the rat's caudoputamen. Moreover, 5'-nucleotidase is prominently associated with glial membranes in the central nervous system, so that the concentration of this enzyme in striosomes could mark these as sites of selective glial populations within striatum. These properties and actions of 5'-nucleotidase in purinergic neurotransmission and in neuroadhesion may contribute to the specialized functions of striosomes and matrix.

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The Properties, Structure, Function, Intracellular Localisation and Movement of Hepatic 5′-Nucleotidase

Cited by 15 publications

References 92 publications

Evidence for deactivation of both ectosolic and cytosolic 5'-nucleotidase by adenosine A1 receptor activation in the rat cardiomyocytes.

Evidence for deactivation of both ectosolic and cytosolic 5'-nucleotidase by adenosine A1 receptor activation in the rat cardiomyocytes.

Purification and properties of a novel nucleotide-hydrolysing enzyme (5′-nucleotidase) from Boophilus microplus

5′‐Nucleotidase: A new marker for striosomal organization in the rat caudoputamen

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