The nerve growth factor receptor gene is expressed in both neuronal and non-neuronal tissues in the human fetus.
ABSTRACT In situ hybridization was used to study expression of beta-nerve growth factor receptor (NGF-R) mRNA in the early human fetus. In 8- to 12-week old fetuses, high labelling was found over motoneurons along the entire length of the lateral motor column. High levels of NGF-R mRNA were also seen over most developing nerve cell bodies in both the dorsomedial and ventrolateral part of the dorsal root ganglia. Lower, but clearly specific labelling was detected over a subpopulation of cells in Auerbach's plexus in the intestines. Evidence for a non-neuronal expression of NGF-R mRNA came from labelling over a subpopulation of cells in glomeruli of the kidney in a 12-week old human embryo. Myoblasts in skeletal muscle anlagen were labelled as well as cells along peripheral nerve. The widespread expression of NGF-R mRNA in the human fetus suggests that the NGF-R is important for development of a variety of different tissues of both neuronal and non-neuronal origin.
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ABSTRACT: Several projects that would be used for nuclear physics research are at various stages of development or construction. The fixed target projects include a hadron facility now under construction at JAERI and an upgrade of the CEBAF 6 GeV electron facility at Jefferson Lab to 12 GeV. eRHIC is the proposed electron-ion collider at Brookhaven National Laboratory. Jefferson Lab also proposed a project that combines a 25 GeV fixed target capability with an electron-ion collider, eLIC. The conceptual layouts for all the projects are presented as is the utilization of srf technology. The R&D opportunities are discussed.
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ABSTRACT: Nerve growth factor (NGF), brain derived neurotrophic factor (BDNF) and neurotrophin-3 (NT-3) are members of the neurotrophin family, which is involved in the differentiation, growth, repair, plasticity and maintenance of many neuronal populations. They act through three tyrosin-kinase (Trk) specific receptors: NGF bind to TrkA, BDNF to TrkB and NT3 to TrkC. Despite increasing evidence regarding the presence of neurotrophin and their receptors in many vertebrate species, in amphibians there are very few data concerning them. Thus, the aim of this study was to extend the investigation to the presence of both neurotrophins and their Trk receptors in the gut of an anuran amphibian, Rana temporaria. In the frog gut NT-3- like immunoreactivity (IR) was observed in both the nervous system and endocrine cells of the stomach and intestine, while NGF-like IR was observed only in the enteric nervous system, and BDNF-like IR in the intestinal endocrine cells. TrkA- and TrkB-like IR was detected in both neurons and endocrine cells of the intestine, while TrkC-like IR was observed only in intestinal neurons. No Trk IR was detected in the stomach. The occurrence of the IR to neurotrophins and their receptors in the gut of the frog further confirms the well-conserved presence of this family of growth factors and Trk receptors during the evolution of vertebrates and suggests their complex involvement in the biology of the gastrointestinal neuro-endocrine system.Histology and histopathology 05/2004; 19(2):349-56. · 2.28 Impact Factor
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ABSTRACT: We describe the cloning and characterization of a rat single transmembrane protein that is homologous to the common neurotrophin receptor p75NTR in its death domain and the transmembrane region but dissimilar outside these regions. We have dubbed this protein PLAIDD, for p75-like apoptosis-inducing death domain protein. PLAIDD messenger RNA, which is ubiquitously distributed, is highly expressed in the embryo, but downregulated in adult tissues. Alternative splicing within the extracellular region of PLAIDD generates four RNA species, but only two of them are translated, PLAIDD_L and PLAIDD_S (long and short isoforms, respectively). While the amino acid sequence of the intracellular region of PLAIDD displays 41% identity with the intracellular region of p75NTR, the extracellular region of PLAIDD does not reveal any homology with p75NTR. Overexpression of each isoform of PLAIDD led to cytotoxicity in superior cervical ganglion neurons and in human embryonic kidney 293T cells. Both isoforms of PLAIDD could be co-immunoprecipitated with p75NTR, suggesting an interaction between these molecules.NeuroMolecular Medicine 02/2002; 1(3):153-70. · 4.49 Impact Factor