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G Lück

Publications and source records attributed to G Lück.

12 recordsLinked to original sources
PubMed2001

Just in time and place: NOS/NO system assembly in neuromuscular junction formation.

Recent advances in the molecular, biochemical, and anatomical aspects of postsynaptic membrane components at the neuromuscular junction (NMJ) are briefly reviewed focussing on assembly, architecture, and function of the multi-subunit dystrophin-protein complex (DPC) and its associated nitric oxide (NO)-signaling complex. Elucidation of unique structural binding motifs of NO-synthases (NOS), and microscopical codistribution of neuronal NOS (nNOS), the major isoform of NOS expressed at the NMJ, with known synaptic proteins, i.e., family members of the DPC, nicotinic acetylcholine receptor (AChR), NMDA-receptor, type-1 sodium and Shaker K(+)-channel proteins, and linker proteins (e.g., PSD-95, 43K-rapsyn), suggests targeting and assembly of the NO-signaling pathway at postsynaptic membrane components. NO mediates agrin-induced AChR-aggregation and downstream signal transduction in C2 skeletal myotubes while administration of L-arginine, the limiting substrate for NO-biosynthesis, enhances aggregation of synapse-specific components such as utrophin. At the NMJ, NO appears to be a mediator of (1) early synaptic protein clustering, (2) synaptic receptor activity and transmitter release, or (3) downstream signaling for transcriptional control. Multidisciplinary data obtained from cellular and molecular studies and from immunolocalization investigations have led us to propose a working model for step-by-step binding of nNOS, e.g., to subunit domains of targeted and/or preexisting membrane components. Formation of NOS-membrane complexes appears to be governed by agrin-signaling as well as by NO-signaling, supporting the idea that parallel signaling pathways may account for the spatiotemporally defined postsynaptic assembly thereby linking the NOS/NO-signaling cascade to early membrane aggregations and at the right places nearby preexisting targets (e.g., juxtaposition of NO source and target) in synapse formation.

Animals↗
PubMed2000

Nitric oxide synthase (NOS-1) coclustered with agrin-induced AChR-specializations on cultured skeletal myotubes.

Previously we reported that neuronal nitric oxide synthase type-1 (NOS-1) is expressed in skeletal myotubes in vitro. In the present paper we sought to determine whether agrin-induced membrane specializations known to include the nicotinic acetylcholine receptor (AChR) on cultured myotubes may also contain NOS-1 and related molecules. After treatment with various agrin constructs containing the full C-terminally AChR-clustering domain (fragments N2, N4), but not with fragment C2 (truncated), NOS-1 expressed in the cytosol of mouse C2C12 skeletal myotubes coclustered with AChR, 43K rapsyn, MuSK, and the dystrophin/utrophin glycoprotein-complex (DUGC). Agrin-induced specializations also included coaggregates of N-methyl-d-aspartic acid (NMDA)-receptor, alpha-sodium (NaCh), or Shaker-type K+ channel (KCh)/PSD-95 complexes, and NOS-1. We conclude that agrin is crucial for recruitment of preassembled multimolecular membrane clusters, including AChR, NMDAR, and ion channels linked to NOS-1. Coassembly of NOS-1 to postsynaptic molecules may reflect site-specific NO-signaling pathways in neuromuscular junction formation and functions.

Agrin↗
PubMed2000

[Effect of the long-acting beta-2 agonist inhalant formoterol on the quality of sleep of patients with bronchial asthma].

BACKGROUND: Patients with asthma bronchiale often complain of exacerbations during the night. Some anti-asthmatic drugs are known to impair the quality of sleep. HYPOTHESIS: The study was undertaken to prove the effect of the long-acting, inhaled beta-2-agonist formoterol on the quality of sleep in patients with mild or moderate asthma bronchiale. METHODS: 20 patients with asthma bronchiale (15 female, 21-75 years, O 33.3 years) without sleep disorder were evaluated by polysomnography during 3 nights. After one adaptation night, the patients were randomly assigned 24 micrograms of formoterol during one and placebo during the other night. The frequency of respiratory disturbances, arousals, sleep latency, sleep stages, sleep efficiency, motoric activity, and subjective impression of sleep quality were compared in both groups. RESULTS: Respiratory disturbances were less, and the subjective impression of sleep quality was better with formoterol in 50% of the patients. The objective quality of sleep was slightly better with formoterol, but not significant (Tab. 1). CONCLUSIONS: In patients with mild or moderate asthma bronchiale, formoterol does not impair, probably slightly improves the quality of sleep.

Administration, Inhalation↗
PubMed1998

In situ identification of neuronal nitric oxide synthase (NOS-I) mRNA in mouse and rat skeletal muscle.

Skeletal muscle provides a major source of the signaling molecule nitric oxide (NO) however in situ identification of NO-synthase (NOS) mRNA has not been verified. We have used NOS-I (neuronal NOS) probes prepared from plasmid DNA by reverse transcription-polymerase chain reaction (RT-PCR) to detect mRNA transcripts in skeletal muscle cells and myofibers of rat and mouse. Mouse C2C12 myoblasts and myotubes reveal strong cytosolic in situ hybridization (ISH) signals in vitro. In adult animals, ISH signals are detectable in striated myofibers at subsarcolemmal and perinuclear regions whilst the myofibrillar compartment is devoid of signals. Expression of NOS-I mRNA in fusion-competent myoblasts suggests that the NOS/NO system is of relevance to myogenic differentiation. Compartmentalization of NOS-I mRNA may reflect spatiofunctional actions between NOS message and protein and the putative subcellular NO targets.

Animals↗
PubMed1998

Nitric oxide synthase (NOS) in mouse skeletal muscle development and differentiated myoblasts.

The neuronal isoform of nitric oxide synthase (nNOS, termed also NOS-I) is expressed in normal adult skeletal muscle, suggesting important functions for NO in muscle biology. However, the expression and subcellular localization of NOS in muscle development and myoblast differentiation are largely unknown. In the present study, NOS was immunolocalized with isoform-specific antibodies in developing muscle and in differentiated myoblast cultures (mouse C2C12) together with histochemical NADPH-dependent diaphorase activity that is blocked by specific NOS inhibitors and therefore designated as NOS-associated diaphorase activity (NOSaD). Western blot analysis revealed immunoreactive bands for NOS-I-III in lysates from perinatal and adult muscle tissue and C2C12-myotubes that comigrated with prototypical proteins. In embryonic skeletal muscle, but not in adult myofibers, diffuse cytosolic staining and lack of sarcolemmal NOSaD activity and NOS-I immunoreaction were evident. In both myoblasts and fusioned myotubes, NOSaD and NOS isoforms I-III colocalize in the cytosol. Additionally, members of the sarcolemmal dystrophin-glycoprotein complex (i.e., dystrophin, adhalin, beta1-dystroglycan) immunolocalize in the cytosol of differentiating myoblasts, whereas anti-dystrophin and anti-beta1-dystroglycan clearly delineate the sarcolemma in myotubes. Thus, expression of NOS isoforms I-III and NOSaD is cytosolic in fusion-competent myoblasts during myotube formation in vitro. Interaction of NOSaD/NOS-I with the sarcolemmal dystrophin-complex known from mature myofibers is apparently lacking in prenatal muscle development and differentiating myoblasts. Localization of NOS isoforms thus characterized in myogenic cultures may help further to investigate regulated NO formation in muscle cells in vitro.

Animals↗
PubMed1997

NOS type-1 mRNA expression and protein localization in spinal autonomic neurons.

Autonomic neurons of the rat spinal cord show strong NADPH diaphorase activity and immunoreactivity for nitric oxide synthase (NOS). Here we show mRNA expression of NOS type-1 (neuronal or brain NOS) transcripts in cell bodies of sympathetic preganglionic neurons (SPNs) of the intermediolateral (IML) cell column by non-radioactive in situ hybridization using NOS-I riboprobes. Hybridization signals occurred only in neuronal cell bodies and not outside, in what appeared to be fibers and/or terminals. In preganglionic fibers of SPNs, however, dense axoplasmic immunogold labeling was detected with a monoclonal anti-NOS-I antibody. Expression of NOS-I mRNA in SPN cell bodies and axoplasmic immunolocalization of NOS-I protein suggest that protein translocation is involved in NO-mediated preganglionic control of peripheral targets.

Animals↗
PubMed1997

Partial loss of NADPH-diaphorase/nitric oxide synthase-complex in amyotrophic lateral sclerosis and human type-II myofiber atrophy.

To substantiate the role of nitric oxide synthase type-I (NOS-I) in neurogenic muscular disorders we investigated human biopsy samples of type-II fiber atrophy and amyotrophic lateral sclerosis (ALS) by NOS-I immunoreactivity (-IR), NOS-associated NADPH-dependent diaphorase activity (NOSaD) and Western blot analysis. In type-II atrophy, loss of NOSaD and reduced NOS-I-IR was apparent in atrophic myofibers. In atrophic fiber groups lacking NOSaD, both NOS-I and dystrophin-IR was decreased while sarcolemmal beta-dystroglycan- and adhalin-IR (markers of the sarcolemmal dystrophin-glycoprotein complex) was normal. In ALS, groups of scattered angulated atrophic fibers revealed partial loss of NOS-I-IR/NOSaD. Atrophied fibers of either type-I or type-II thus revealed differential sarcolemmal NOS/NOSaD pattern thereby reflecting myopathological alterations of the NO-system in human type-II atrophy and ALS.

Adult↗
PubMed1997

Fibroblast growth factor-2 (FGF-2) and FGF-receptor (FGFR-1) immunoreactivity in embryonic spinal autonomic neurons.

The development of the nervous system appears to be under the control of multiple growth factors, neurotrophins and cytokines, which may be expressed either continuously or transiently throughout defined stages of cellular generation, proliferation or differentiation. Fibroblast growth factor (FGF) cytokines and their receptors are abundantly expressed in the embryonic nervous system but their localization at autonomic levels in the fetal spinal cord has not yet been detailed. Immunoreactivity to FGF-2, probably the best characterized member of the FGF family (FGF-1 to FGF-10) and of one of its high affinity receptors, FGFR-1, was found in autonomic neurons at embryonic day E14, the peak day of generation and proliferation in the common ventral motoneuron pool. It was also continuously present throughout the investigated subsequent stages (E15 to postnatal day P30). Immunogold electron microscopy revealed the cytoplasmic localization of FGF-2 and FGFR-1 in intermediolateral neurons, the major group of sympathetic preganglionic neurons in the spinal cord. In these neurons, immunocytochemistry from E14 onwards showed the co-distribution of both markers at the period of axonal outgrowth to peripheral targets, e.g. the adrenal medulla. Our findings suggest autocrine and/or paracrine actions of FGF-2 for sympathetic preganglionic development but do not support its role as a target-derived neurotrophic factor for autonomic neuron development.

Animals↗
PubMed1979

[An information system for a department of nuclear medicine (author's transl)].

A computer system is connected on-line to each working place of a department for nuclear medicine. It is assisting the daily work such as the measuring and processing of the measured data, the medical interpretation of the results and the finding of the diagnosis, and finally the composing and writing of medical reports. Additionally this system supports the organization of the department in many ways. The organisation and functions of the system are described.

Berlin↗
PubMed1977

[Improvement of the endogenous creatinine clearance by blocking the tubules].

In the endogenic creatinine clearance at present a blocking of the tubuli with phenol red cannot be achieved. The elimination follows in the 20th and 40th minute after the injection of a simple exponential function and thus allows the determination of the half-life period. The phenol red 60/60 value lies in the phase of the backflow of phenol red from the space of distribution.

Creatinine↗