Cytochemical investigations on the localization of 5?-nucleotidase in the rat hippocampus with special reference to synaptic regions

Hg, Bernstein; Weiss, J.; Luppa, H

doi:10.1007/bf00495765

Cited by 46 publications

(18 citation statements)

References 23 publications

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“…5′Nucleotidases in particular were found at the surface membranes of axons and dendrites (Bernstein et al, 1978) and are associated with glial membranes in the central nervous system (Schoen & Graybiel, 1992). Localization of ecto-Ca-ATPase and 5′-ectonucleotidase activities was shown in caveolae of smooth muscle cells of the guinea-pig vas deferens and their role in neurotransmission has been suggested (Kittel & Bacsy, 1994).…”

Section: Termination Of Neurotransmitter Actionmentioning

confidence: 99%

The purinergic neurotransmitter revisited: A single substance or multiple players?

Mutafova‐Yambolieva

Durnin

2014

Pharmacology & Therapeutics

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The past half century has witnessed tremendous advances in our understanding of extracellular purinergic signaling pathways. Purinergic neurotransmission, in particular, has emerged as a key contributor in the efficient control mechanisms in the nervous system. The identity of the purine neurotransmitter, however, remains controversial. Identifying it is difficult because purines are present in all cell types, have a large variety of cell sources, and are released via numerous pathways. Moreover, studies on purinergic neurotransmission have relied heavily on indirect measurements of integrated postjunctional responses that do not provide direct information for neurotransmitter identity. This paper discusses experimental support for adenosine 5′-triphosphate (ATP) as a neurotransmitter and recent evidence for possible contribution of other purines, in addition to or instead of ATP, in chemical neurotransmission in the peripheral, enteric and central nervous systems. Sites of release and action of purines in model systems such as vas deferens, blood vessels, urinary bladder and chromaffin cells are discussed. This is preceded by a brief discussion of studies demonstrating storage of purines in synaptic vesicles. We examine recent evidence for cell type targets (e.g., smooth muscle cells, interstitial cells, neurons and glia) for purine neurotransmitters in different systems. This is followed by brief discussion of mechanisms of terminating the action of purine neurotransmitters, including extracellular nucleotide hydrolysis and possible salvage and reuptake in the cell. The significance of direct neurotransmitter release measurements is highlighted. Possibilities for involvement of multiple purines (e.g., ATP, ADP, NAD+, ADP-ribose, adenosine, and diadenosine polyphosphates) in neurotransmission are considered throughout.

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Section: Termination Of Neurotransmitter Actionmentioning

confidence: 99%

The purinergic neurotransmitter revisited: A single substance or multiple players?

Mutafova‐Yambolieva

Durnin

2014

Pharmacology & Therapeutics

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“…5'-Nucleotidase has been shown by a number of researchers to be an enzyme closely associated with myelin [Naidoo, 1962;Banik and Davison, 1969;Kreutzberg et al, 1978;Bernstein et al, 1978;Cammer et al, 1980;Cammer andZimmerman, 1981a, 1981b;Smith et al, 1980;Shanker et al, 19821. Recent in vivo studies have shown that 5'-nucleotidase is localized in myelin, in the distal process of oligodendroglia, and in the oligodendroglial expansions surrounding the myelin sheath [Vercelli-Retta et al, 1976;Kreutzberg et al, 1978;Cammer et al, 19801.…”

Section: Introductionmentioning

confidence: 99%

Investigations on myelinogenesis in vitro: Regulation of 5′‐nucleotidase activity by thyroid hormone in cultures of dissociated cells from embryonic mouse brain

Shanker

Rao

Pieringer

1984

J of Neuroscience Research

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The developmental pattern of the myelin-associated 5'-nucleotidase and its regulation by L-3,3',5,-triiodothyronine (T3) have been demonstrated in a culture system of cells dissociated from embryonic mouse brain. Hypothyroid calf serum containing low levels of T3 (31 ng/100 ml), and thyroxine, T4 (less than 1 microgram/ml), was used in the culture medium in place of normal calf serum (T3, 103 ng/100ml; T4, 5.7 micrograms/ml) to render the cultures responsive to exogenously added T3. By means of T3 supplementation, the lower levels of enzyme activity observed in the cultures grown in the presence of hypothyroid calf-serum containing medium could be restored to a considerable extent although not completely to normal values. Half-maximal stimulatory effect was obtained at 3.9 X 10(-8)M T3 concentration. Among the various substrates tested, 5'-AMP, 5'-UMP and 5'-CMP were equally good, while 5'-GMP yielded approximately half the activity.

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“…To learn more about a possible connection between neuronal localization of both transporter proteins and this particular type of neuromodulation, we compared the distribution of ABCB1 and ABCC1 with those of 5-N´ ADA and NTPDase2. Since all three enzymes are important regulators of purinergic cell signalling (Burnstock, 2013; Gampe et al, 2012; Kulesskaya et al, 2013; Mutafova-Yambolieva and Durnin, 2014) by degrading ATP (5-N´ degrades 5´-AMP to adenosine, ADA degrades adenosine to inosine and NTPDase2 hydrolyses extracellular nucleoside triphosphates to nucleoside monophosphates) they have repeatedly been used as putative marker enzymes to anatomically localize adenosinergic/purinergic neuromodulation (Bernstein et al, 1978; Kulesskaya et al, 2013; Staines et al, 1988; Yamamoto et al, 1987)). However, due to their wide distribution within the brain ((Burnstock et al, 2011); this study) the immunodetection of 5´-N and/or ADA in a specific brain cell compartment does not unequivocally prove the presence of purinergic/adenosinergic neuromodulation).…”

Section: Discussionmentioning

confidence: 99%

Vascular and extravascular distribution of the ATP-binding cassette transporters ABCB1 and ABCC1 in aged human brain and pituitary

Bernstein

Hölzl

Dobrowolny

et al. 2014

Mechanisms of Ageing and Development

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ATP-binding cassette (ABC) transporters play an increasing role in the understanding of pathologic peptide deposition in neurodegenerative diseases (NDs), such as Alzheimer’s and Parkinson’s. To describe the location of the most important ABC transporters for NDs in human brain tissue, we investigated ABCB1 and ABCC1 immunohistologically in the adult human brain and pituitary. Both transporters have similar but not identical expression patterns. In brain regions with an established blood-brain barrier (BBB), ABCB1 and ABCC1 were ubiquitously expressed in endothelial cells of the microvasculature and in a subset of larger blood vessels (mostly venules). Remarkably, both transporters were also found in fenestrated capillaries in circumventricular organs where the BBB is absent. Moreover, ABCB1 and ABCC1 were also expressed in various non-endothelia cells such as pericytes, astrocytes, choroid plexus epithelia, ventricle ependymal cells, and neurons. With regard to their neuronal expression it was shown that both transporters are located in specific nerve cell populations, which are also immunopositive for three putative cell markers of purinergic cell signalling, namely 5´-nucleotidase, adenosine deaminase and nucleoside triphosphate diphosphohydrolase-2. Therefore, we speculate that neuronal expression of ABCB1 and ABCC1 might be linked to adenosinergic/purinergic neuromodulation. Lastly, both transporters were observed in multiple adenohypophyseal cells.

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Cytochemical investigations on the localization of 5?-nucleotidase in the rat hippocampus with special reference to synaptic regions

Cited by 46 publications

References 23 publications

The purinergic neurotransmitter revisited: A single substance or multiple players?

The purinergic neurotransmitter revisited: A single substance or multiple players?

Investigations on myelinogenesis in vitro: Regulation of 5′‐nucleotidase activity by thyroid hormone in cultures of dissociated cells from embryonic mouse brain

Vascular and extravascular distribution of the ATP-binding cassette transporters ABCB1 and ABCC1 in aged human brain and pituitary

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