Demonstration of nitric oxide synthase (NOS) in marmosets by NADPH diaphorase (NADPH-d) histochemistry and NOS immunoreactivity

Grozdanovic, Zarko; Νάκος, Γεώργιος; Christova, Tatjana; Nikolova, Kamelia; Mayer, Bernd; Gossrau, Reinhart

doi:10.1016/s0065-1281(11)80197-2

Cited by 29 publications

(7 citation statements)

References 27 publications

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“…The NADPH diaphorase activity of NOS I (NOSaD) was demonstrated according to Grozdanovic et al (1995b) with 0.5 mM potassium permanganate in the incubation medium containing 1 mg/ml b-NADPH, 0.25 mg/ml nitro blue tetrazolium (NBT), and 0.3% Triton X-100 (v/v) in 0.1 M phosphate buffer, pH 7.4. In addition, the indirect approach was employed to detect NOSaD in sections of NM-RI and MDX mice muscles using the incubation media (with 0.3% Triton X-100) for NADP + -dependent glucose-6-phosphate dehydrogenase (EC 1.1.1.49), isocitrate dehydrogenase (EC 1.1.1.42), or malate dehydrogenase (malic enzyme, EC 1.1.1.40) as described by Lojda et al (1979).…”

Section: Enzyme Histochemistrymentioning

confidence: 99%

Co-localization of nitric oxide synthase I (NOS I) and NMDA receptor subunit 1 (NMDAR-1) at the neuromuscular junction in rat and mouse skeletal muscle

Grozdanovic

Gossrau

1997

Cell and Tissue Research

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Nitric oxide synthase I (NOS I) has been localized to the skeletal muscle sarcolemma in a variety of vertebrate species including man. It is particularly enriched at neuromuscular junctions. Recently, the N-methyl-D-aspartate (NMDA) receptor subunit 1 (NMDAR-1) has been detected in the postjunctional sarcolemma of rat diaphragm, providing a clue as to the possible source of Ca2+ ions that are necessary for NOS I activation. To address this possibility, we studied the distribution of NMDAR-1 and NOS I in mouse and rat skeletal muscles by immunohistochemistry and enzyme histochemistry. NMDAR-1 and NOS I were closely associated at neuromuscular junctions primarily of type II muscle fibers. NOS I was also present in the extrajunctional sarcolemma of this fiber type. Dystrophin, beta-dystroglycan, alpha-sarcoglycan, and spectrin were found normally expressed in both the junctional and extrajunctional sarcolemma of both fiber types. By contrast, in the muscle sarcolemma of MDX mice, dystrophin and dystrophin-associated proteins were reduced or absent. NOS I immunoreactivity was lost from the extrajunctional sarcolemma and barely detectable in the junctional sarcolemma. NOS I activity was clearly demonstrable in the junctional sarcolemma by NADPH diaphorase histochemistry, especially when the two-step method was used. NMDAR-1 was not altered. These data suggest that different mechanisms act to attach NOS I to the junctional versus extrajunctional sarcolemma. It may further be postulated that NMDA receptors are involved not only in the regulation but also sarcolemmal targeting of NOS I at neuromuscular junctions of type II fibers. The evidence that glutamate may function as a messenger molecule at vertebrate neuromuscular junction is discussed.

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Section: Enzyme Histochemistrymentioning

confidence: 99%

Co-localization of nitric oxide synthase I (NOS I) and NMDA receptor subunit 1 (NMDAR-1) at the neuromuscular junction in rat and mouse skeletal muscle

Grozdanovic

Gossrau

1997

Cell and Tissue Research

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“…Increased amounts of activated forms of nNOS should correspond to changes in nNOS activity. We used nitro blue tetrazolium to histochemically detect nNOS activity in muscle sections (Grozdanovic et al, 1995), and co-localized to NMJs in serial sections using a cholinesterase histochemical stain (Figure 1D, upper). In WT muscle only about 6% of NMJs were labeled for activated nNOS, while in mSCS muscle approximately 39% had histochemically detectable nNOS activity (Figure 1D, lower-left).…”

Section: Resultsmentioning

confidence: 99%

“…Protein samples (10μg) were analyzed by Ultrasensitive Colorimetric NOS Assay Kit following manufacturer’s protocol (Oxford Biomedical Research, Oxford, MI). nNOS activity detected on muscle slides using the NADPH diaphorase (NADPH-d) reaction as previously described (Grozdanovic et al, 1995). Endplates were labeled using acetyl cholinesterase reaction as previously described (Koelle and Friedenwald, 1949).…”

Section: Methodsmentioning

confidence: 99%

Skeletal Muscle Calpain Acts through Nitric Oxide and Neural miRNAs to Regulate Acetylcholine Release in Motor Nerve Terminals

et al. 2013

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Cholinergic overactivity in diseases of neuromuscular transmission elicits a retrograde signal resembling homeostatic synaptic plasticity that down-regulates transmitter release. Understanding this compensatory pathway could provide insights into novel therapeutic avenues and molecular mechanisms underlying learning and memory. We identified nitric oxide as a possible source of this signal in pathological human and mouse muscle samples and linked this signaling pathway to changes in synaptic function in the NMJ. We further showed that neuronal nitric oxide synthase was regulated by cholinergic excess through activation of skeletal muscle calpain and its effect on the Cdk5 and CaMKII, leading to direct modulation of presynaptic function. Finally, we showed that this signaling pathway acted through specific microRNA control of presynaptic vesicle protein expression. The control of presynaptic miRNA levels by postsynaptic activity represents a novel mechanism for modulation of synaptic activity in normal or pathological conditions.

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“…Evidence for a role of neuronal NO synthase in skeletal muscle fibers is well established (Kobzik et al 1994;Brenman et al 1995;Grozdanovic et al 1995aGrozdanovic et al ,b, 1996Chang et al 1996;Frandsen et al 1996;Gossrau et al 1996;Kusner and Kaminski 1996;Oliver et al 1996;Urazaev et al 1996;Stamler and Meissner 2001) and more recently, a role in control of non-quantal release of the mediator from the motor nerve terminals has been described (Mukhtarov et al 2000;Malomouzh et al 2003).…”

Section: Discussionmentioning

confidence: 99%

Effect of N‐acetylaspartylglutamate (NAAG) on non‐quantal and spontaneous quantal release of acetylcholine at the neuromuscular synapse of rat

Malomouzh

Nikolsky

Lieberman

et al. 2005

Journal of Neurochemistry

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N-Acetylaspartylglutamate (NAAG), known to be present in rat motor neurons, may participate in neuronal modulation of nonquantal secretion of acetylcholine (ACh) from motor nerve terminals. Non-quantal release of ACh was estimated by the amplitude of the endplate membrane hyperpolarization (H-effect) caused by inhibition of nicotinic receptors by (+)-tubocurarine and acetylcholinesterase by armin (diethoxyp-nitrophenyl phosphate). Application of exogenous NAAG decreased the H-effect in a dose-dependent manner. The reduction of the H-effect by NAAG was completely removed when N-acetyl-b-aspartylglutamate (bNAAG) or 2-(phosphonomethyl)-pentanedioic acid (2-PMPA) was used to inhibit glutamate carboxypeptidase II (GCP II), a presynaptic Schwann cell membrane-associated ectoenzyme that hydrolyzes NAAG to glutamate and N-acetylaspartate. Bath application of glutamate decreased the H-effect similarly to the action of NAAG but N-acetylaspartate was without effect.Inhibition of NMDA receptors by DL-2-amino-5-phosphopentanoic acid, (+)-5-methyl-10,11-dihydro-5H-dibenzocyclohepten-5,10-imine (MK801), and 7-chlorokynurenic acid or inhibition of muscle nitric oxide synthase (NO synthase) by N G -nitro-L-arginine methyl ester and 3-bromo-7-nitroindazole completely prevented the decrease of the H-effect by NAAG. These results suggest that glutamate, produced by enzymatic hydrolysis of bath-applied NAAG, can modulate non-quantal secretion of ACh from the presynaptic terminal of the neuromuscular synapse via activation of postsynaptic NMDA receptors and synthesis of nitric oxide (NO) in muscle fibers. NAAG also increased the frequency of miniature endplate potentials (mEPPs) generated by spontaneous quantal secretion of ACh, whereas the mean amplitude and time constants for rise time and for decay of mEPPs did not change.

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Demonstration of nitric oxide synthase (NOS) in marmosets by NADPH diaphorase (NADPH-d) histochemistry and NOS immunoreactivity

Cited by 29 publications

References 27 publications

Co-localization of nitric oxide synthase I (NOS I) and NMDA receptor subunit 1 (NMDAR-1) at the neuromuscular junction in rat and mouse skeletal muscle

Co-localization of nitric oxide synthase I (NOS I) and NMDA receptor subunit 1 (NMDAR-1) at the neuromuscular junction in rat and mouse skeletal muscle

Skeletal Muscle Calpain Acts through Nitric Oxide and Neural miRNAs to Regulate Acetylcholine Release in Motor Nerve Terminals

Effect of N‐acetylaspartylglutamate (NAAG) on non‐quantal and spontaneous quantal release of acetylcholine at the neuromuscular synapse of rat

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