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Author (up) Backberg, M.; Meister, B. file  url
openurl 
  Title Abnormal cholinergic and GABAergic vascular innervation in the hypothalamic arcuate nucleus of obese tub/tub mice Type Journal Article
  Year 2004 Publication Synapse (New York, N.Y.) Abbreviated Journal Synapse  
  Volume 52 Issue 4 Pages 245-257  
  Keywords Acetylcholine/*metabolism; Adaptor Proteins, Signal Transducing; Animals; Arcuate Nucleus of Hypothalamus/blood supply/*metabolism; Blood Vessels/innervation; Carrier Proteins/metabolism; Glutamate Decarboxylase/metabolism; Immunohistochemistry; *Membrane Transport Proteins; Mice; Mutation; Obesity/*physiopathology; Polymerase Chain Reaction; Presynaptic Terminals/metabolism; Proteins/*genetics; Synaptophysin/metabolism; Vesicular Acetylcholine Transport Proteins; *Vesicular Transport Proteins; gamma-Aminobutyric Acid/*metabolism  
  Abstract Tubby and tubby-like proteins (TULPs) are encoded by members of a small gene family. An autosomal recessive mutation in the mouse tub gene leads to blindness, deafness, and maturity-onset obesity. The mechanisms by which the mutation causes the obesity syndrome has not been established. We compared obese tub/tub mice and their lean littermates in order to find abnormalities within the mediobasal hypothalamus, a region intimately associated with the regulation of body weight. Using an antiserum to the vesicular acetylcholine transporter (VAChT), a marker for cholinergic neurons, many unusually large VAChT-immunoreactive (-ir) nerve terminals, identified by colocalization with the synaptic vesicle protein synaptophysin, were demonstrated in the hypothalamic arcuate nucleus of obese tub/tub mice. Double-labeling showed that VAChT-ir nerve endings also contained glutamic acid decarboxylase (GAD), a marker for gamma-aminobutyric acid (GABA) neurons. The VAChT- and GAD-ir nerve terminals were in close contact with blood vessels, identified with antisera to platelet endothelial cell adhesion molecule-1 (PECAM; also called CD31), laminin, smooth muscle actin (SMA), and glucose transporter-1 (GLUT1). Such large cholinergic and GABAergic nerve terminals surrounding blood vessels were not seen in the arcuate nucleus of lean tub/+ mice. The presence of abnormal cholinergic/GABAergic vascular innervation in the arcuate nucleus suggests that alterations in this region, which contains neurons that receive information from the periphery and which relays information about the energy status to other parts of the brain, may be central in the development of the obese phenotype in animals with an autosomal recessive mutation in the tub gene.  
  Call Number Serial 1460  
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Author (up) Berger, U.V.; Carter, R.E.; Coyle, J.T. file  url
openurl 
  Title The immunocytochemical localization of N-acetylaspartyl glutamate, its hydrolysing enzyme NAALADase, and the NMDAR-1 receptor at a vertebrate neuromuscular junction Type Journal Article
  Year 1995 Publication Neuroscience Abbreviated Journal Neuroscience  
  Volume 64 Issue 4 Pages 847-850  
  Keywords Animals; Dipeptidases/*immunology/physiology; Dipeptides/*immunology/physiology; Glutamate Carboxypeptidase II; Immunohistochemistry; Neuromuscular Junction/*physiology; Phrenic Nerve; Rats; Receptors, N-Methyl-D-Aspartate/*immunology/physiology; Vertebrates  
  Abstract Although glutamate is thought to be the neurotransmitter at the invertebrate neuromuscular junction, acetylcholine is accepted as the primary neurotransmitter of the vertebrate motoneurons. N-acetylaspartylglutamate, a dipeptide localized in putative glutamatergic neurons in brain, is also found in high concentrations (> mM) in mammalian motoneurons and the ventral roots of spinal cord. N-acetylaspartylglutamate, which is released from neurons by depolarization in a Ca(2+)-dependent fashion, is implicated in glutamatergic transmission in two ways: it is a partial agonist at NMDA receptors, and it is cleaved to yield extracellular glutamate and N-acetylasparate by the specific peptidase N-acetylated alpha-linked acidic dipeptidase. Given the localization of N-acetylaspartylglutamate in motor neuronal perikarya and axons, we wondered whether N-acetylaspartylglutamate or glutamate cleaved from N-acetylaspartylglutamate by N-acetylated alpha-linked acidic dipeptidase may also play a role in neuromuscular transmission. Here we describe the immunocytochemical detection at the rat neuromuscular junction of N-acetylaspartylglutamate in terminals of motoneurons, of N-acetylated alpha-linked acidic dipeptidase in perisynaptic Schwann cells, and of the NMDAR-1 glutamate receptor subunit on postsynaptic muscle membranes. These results point to a potential role for N-acetylaspartylglutamate at the rat neuromuscular junction. Further, this is the first demonstration of a glutamate receptor protein at vertebrate neuromuscular synapses. Together with other recent findings, our results suggest that glutamate-like molecules are involved in neuromuscular transmission not only in invertebrates but also in veretebrates where they may modulate signaling by acetylcholine.  
  Call Number Serial 114  
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Author (up) Brabin, B.J.; Romagosa, C.; Abdelgalil, S.; Menendez, C.; Verhoeff, F.H.; McGready, R.; Fletcher, K.A.; Owens, S.; D'Alessandro, U.; Nosten, F.; Fischer, P.R.; Ordi, J. file  url
openurl 
  Title The sick placenta-the role of malaria Type Journal Article
  Year 2004 Publication Placenta Abbreviated Journal Placenta  
  Volume 25 Issue 5 Pages 359-378  
  Keywords Cytokines/immunology; Female; Fetal Growth Retardation/etiology/parasitology; Fetal Weight; Humans; Immunity, Cellular/immunology; Immunity, Maternally-Acquired/immunology; Immunohistochemistry; Infant, Low Birth Weight; Infant, Newborn; Malaria/immunology/*pathology; Malaria, Falciparum/immunology/*pathology; Malaria, Vivax/immunology/pathology; Placenta/immunology/pathology/physiopathology; Placenta Diseases/immunology/*pathology; Pregnancy; Pregnancy Complications, Parasitic; Premature Birth/epidemiology/etiology/parasitology  
  Abstract The human placenta is an ideal site for the accumulation of Plasmodium falciparum malaria parasites, and as a consequence serious health problems arise for the mother and her baby. The pathogenesis of placental malaria is only partially understood, but it is clear that it leads to a distinct epidemiological pattern of malaria during pregnancy. The objectives of this review are: (1) To review recent data on the epidemiology of malaria in pregnancy, with emphasis on placental malaria; (2) to describe the pathological changes and immunological factors related to placental malaria; and (3) to discuss briefly the functional consequences of this infection for the mother and her baby. The review attempts to bring together local events at the maternal-fetal interface which encompass immunological and pathological processes which relate to the epidemiological pattern of malaria in pregnancy in areas of both high and low malaria transmission. An integrated understanding of the epidemiological, immunological and pathological processes must be achieved in order to understand how to control malaria in pregnancy. The yearly exposure of at least 50 million pregnancies to malaria infection makes it the commonest and most recurrent parasitic infection directly affecting the placenta. These statistics and our limited understanding of its pathogenesis suggest the research priorities on this subject.  
  Call Number Serial 147  
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Author (up) Canteras, N.S.; Simerly, R.B.; Swanson, L.W. file  url
openurl 
  Title Organization of projections from the medial nucleus of the amygdala: a PHAL study in the rat Type Journal Article
  Year 1995 Publication The Journal of Comparative Neurology Abbreviated Journal J Comp Neurol  
  Volume 360 Issue 2 Pages 213-245  
  Keywords Amygdala--physiology; Animals; Axons--physiology; Brain Mapping; Hypothalamus--immunology; Immunohistochemistry; Male; Neural Pathways--physiology; Rats; Rats, Sprague-Dawley  
  Abstract The organization of axonal projections from the four recognized parts of the medial amygdalar nucleus (MEA) were characterized with the Phaesolus vulgaris leucoagglutinin (PHAL) method in male rats. The results indicate that the MEA consists of two major divisions, ventral and dorsal, and that the former may also consist of rostral and caudal regions. As a whole, the MEA generates centrifugal projections to several parts of the accessory and main olfactory sensory pathways, and projections to a) several parts of the intrahippocampal circuit (ventrally); b) the ventral striatum, ventral pallidum, and bed nuclei of the stria terminalis (BST) in the basal telencephaon; c) many parts of the hypothalamus; d) midline and medial parts of the thalamus; and e) the periaqueductal gray, ventral tegmental area, and midbrain raphe. The dorsal division of the MEA (the posterodorsal part) is characterized by projections to the principal nucleus of the BST, and to the anteroventral periventricular, medial, and central parts of the medial preoptic, and ventral premammillary hypothalamic nuclei. These hypothalamic nuclei project heavily to neuroendocrine and autonomic-related parts of the hypothalamic periventricular zone. The ventral division of the MEA (the anterodorsal, anteroventral, and posteroventral parts) is characterized by dense projections to the transverse and interfascicular nuclei of the BST, and to the lateral part of the medial preoptic, anterior hypothalamic, and ventromedial hypothalamic nuclei. However, dorsal regions of the ventral division provide rather dense inputs to the medial preoptic region and capsule of the ventromedial nucleus, whereas ventral regions of the ventral division preferentially innervate the anterior hypothalamic, dorsomedial, and ventral parts of the ventromedial nuclei. Functional evidence suggests that circuits associated with dorsal regions of the ventral division may deal with reproductive behavior, whereas circuits associated with ventral regions of the ventral division may deal preferentially with agonistic behavior.  
  Call Number Serial 45  
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Author (up) Chou, S.M.; Wang, H.S.; Komai, K. file  url
openurl 
  Title Colocalization of NOS and SOD1 in neurofilament accumulation within motor neurons of amyotrophic lateral sclerosis: an immunohistochemical study Type Journal Article
  Year 1996 Publication Journal of Chemical Neuroanatomy Abbreviated Journal J Chem Neuroanat  
  Volume 10 Issue 3-4 Pages 249-258  
  Keywords Amyotrophic Lateral Sclerosis/*enzymology; Citrulline/metabolism; Cyclic GMP/metabolism; Cytoplasm/metabolism; Humans; Immunohistochemistry; Motor Neurons/chemistry/*enzymology; Neurofilament Proteins/*metabolism; Nitrates/metabolism; Nitric Oxide/analysis/*metabolism; Nitrogen/metabolism; Oxidation-Reduction; Superoxide Dismutase/analysis/*metabolism; Tyrosine/metabolism  
  Abstract Peroxynitrite, formed from nitric oxide and superoxide, may affect neurofilament assembly and cause neurofilament accumulation in motoneurons. This hypothesis may reconcile the mutations of two genes: superoxide dismutase-1 in some patients with familial amyotrophic lateral sclerosis, and the gene for the heavy neurofilament in some patients with sporadic amyotrophic lateral sclerosis previously reported. We found colocalization of superoxide dismutase-1 and nitric oxide synthase in the foci of neurofilament accumulation as 'conglomerates' in upper motor neurons and 'axonal spheroids' in lower motor neurons. In addition, all the specific molecules related to the reactions, including calmodulin, 3', 5'-cyclic guanosine-monophosphate, citrulline, and nitrotyrosine were found strongly immunopositive in the site of neurofilament accumulation. Our data support the view that the neurofilament aggregates are tightly linked with superoxide dismutase-1 and nitric oxide synthase activities. Both enzymes may focally contribute to peroxynitrite formation at light neurofilament, which is rich in both tyrosine and arginine residues and hence considered as the vulnerable site for nitrotyrosine formation. Nitrotyrosine is known to inhibit phosphorylation and if it impairs phosphorylation of neurofilament subunits, either light or heavy, may alter the slow axonal transport culminating in proximo-distal accumulation of NF and slowly progressive motoneuron death.  
  Call Number Serial 1254  
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Author (up) Chu, D.T.; Klymkowsky, M.W. file  url
openurl 
  Title The appearance of acetylated alpha-tubulin during early development and cellular differentiation in Xenopus Type Journal Article
  Year 1989 Publication Developmental Biology Abbreviated Journal Dev Biol  
  Volume 136 Issue 1 Pages 104-117  
  Keywords Acetylation; Animals; Antibodies, Monoclonal; Blastocyst/metabolism; Blotting, Western; Cell Differentiation; Epidermis/metabolism; Fluorescent Antibody Technique; Gastrula/metabolism; Immunohistochemistry; Meiosis; Microtubules/metabolism; Nervous System/embryology/metabolism; Spindle Apparatus/metabolism; Tubulin/immunology/*metabolism; Xenopus/*embryology; Zygote/metabolism  
  Abstract Early development in Xenopus is characterized by dramatic changes in the organization of the microtubule cytoskeleton. We have used whole-mount immunocytochemistry to follow the expression of the acetylated form of alpha-tubulin during early Xenopus development. In the egg and early embryo, the monoclonal anti-acetylated tubulin antibody 6-11B-1 stained meiotic and mitotic spindles, midbody microtubules, and what appears to be the central region of the sperm aster; the antibody did not stain the sperm aster itself or the cortical microtubule system associated with the rotation of the fertilized egg. Following gastrulation, acetylated tubulin disappeared from all but mitotic midbody microtubules. During the course of neurulation high levels of acetylated tubulin reappeared in the precursors of the ciliated epidermal cells (stage 15), transiently in neural folds (stage 16/17), in neuronal processes (stage 18/19), and in somas (stage 21). The changing pattern of anti-acetylated tubulin staining during Xenopus development raises intriguing questions as to the physiological significance of tubulin acetylation.  
  Call Number Serial 1041  
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Author (up) Danielsson, K.G.; Marions, L.; Bygdeman, M. file  url
openurl 
  Title Effects of mifepristone on endometrial receptivity Type Journal Article
  Year 2003 Publication Steroids Abbreviated Journal Steroids  
  Volume 68 Issue 10-13 Pages 1069-1075  
  Keywords Contraception; Contraceptives, Oral, Synthetic/pharmacology; Endometrium/*drug effects; Fallopian Tubes/drug effects; Female; Hormone Antagonists/pharmacology; Humans; Immunohistochemistry; Microscopy, Electron; Mifepristone/*pharmacology; Ovulation/drug effects; Progesterone/metabolism; Receptors, Progesterone/metabolism; Reverse Transcriptase Polymerase Chain Reaction  
  Abstract At the development of receptivity the endometrium undergoes specific changes. Several factors have been suggested as markers of endometrial receptivity. A common feature for most of these factors is that they are directly, or indirectly, regulated by progesterone. The effect of various doses and regimens of mifepristone on endometrial development and markers of receptivity has been studied. Timed endometrial biopsies were assessed by immunhistochemistry, reverse transcriptase polymerase chain reaction (RT-PCR) and electron microscopy. In addition the contraceptive efficacy of these regimens was investigated. Administration of 200 mg of mifepristone immediately post ovulation has a pronounced effect on endometrial development and on suggested markers of receptivity. This regimen has been shown to be an effective contraceptive method. When 10 mg is given pre or post ovulation, only minor effects on the endometrium are observed. Our studies show that mifepristone, when administered in low doses that do not affect ovulation, significantly affects some of the studied markers of endometrial receptivity and reduces pregnancy rates; however, these activities are more pronounced with the higher dose, which is more effective. Our findings provide insight into the regulation of progesterone receptors of various suggested markers of endometrial receptivity and the possibility of using mifepristone for endometrial contraception.  
  Call Number Serial 1601  
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Author (up) Migheli, A.; Mocellini, C. file  url
openurl 
  Title Ultrastructural immunocytochemistry in glial tumors Type Journal Article
  Year 1990 Publication Journal of Neurosurgical Sciences Abbreviated Journal J Neurosurg Sci  
  Volume 34 Issue 3-4 Pages 219-222  
  Keywords Collagen/*analysis; Factor VIII/*analysis; Glial Fibrillary Acidic Protein/*analysis; Glioma/chemistry/*ultrastructure; Humans; Immunohistochemistry; Vimentin/*analysis  
  Abstract We have studied the ultrastructural distribution of GFAP, vimentin, FVIII/RAg and collagen IV in biopsies of human gliomas with various degree of anaplasia. Pre-embedding (vibratome and cryoultrathin sections) and post-embedding (LR White sections) techniques were tested. The immune reaction was demonstrated by peroxidase-DAB and gold labeling. In astrocytes, GFAP and VIM were localized in the same filament bundles; GFAP was always more expressed than vimentin, regardless of the malignancy grade. FVIII was localized in endoplasmic reticulum and in Weibel-Palade bodies. The influence of technical procedures on the optimal demonstration of each antigen is stressed.  
  Call Number Serial 1643  
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Author (up) Petrovich, G.D.; Risold, P.Y.; Swanson, L.W. file  url
openurl 
  Title Organization of projections from the basomedial nucleus of the amygdala: a PHAL study in the rat Type Journal Article
  Year 1996 Publication The Journal of Comparative Neurology Abbreviated Journal J Comp Neurol  
  Volume 374 Issue 3 Pages 387-420  
  Keywords Amygdala--cytology; Animals; Axons--physiology; Basal Ganglia--cytology; Immunohistochemistry; Male; Neural Pathways--cytology, physiology; Phytohemagglutinins; Rats; Rats, Sprague-Dawley  
  Abstract The organization of axonal projections from the basomedial nucleus of the amygdala (BMA) was examined with the Phaseolus vulgaris leucoagglutinin (PHAL) method in adult male rats. The anterior and posterior parts of the BMA, recognized on cytoarchitectonic grounds, display very different projection patterns. Within the amygdala, the anterior basomedial nucleus (BMAa) heavily innervates the central, medial, and anterior cortical nuclei. In contrast, the posterior basomedial nucleus (BMAp) sends a dense projection to the lateral nucleus, and to restricted parts of the central and medial nuclei. Extra-amygdalar projections from the BMA are divided into ascending and descending components. The former end in the cerebral cortex, striatum, and septum. The BMAa mainly innervates olfactory (piriform, transitional) and insular areas, whereas the BMAp also innervates inferior temporal (perirhinal, ectorhinal) and medial prefrontal (infralimbic, prelimbic) areas and the hippocampal formation. Within the striatum, the BMAa densely innervates the striatal fundus, whereas the nucleus accumbens receives a heavy input from the BMAp. Both parts of the BMA send massive projections to distinct regions of the bed nuclei of the stria terminalis. Descending projections from the BMA end primarily in the hypothalamus. The BMAa sends a major input to the lateral hypothalamic area, whereas the BMAp innervates the ventromedial nucleus particularly heavily. Injections were also placed in the anterior cortical nucleus (COAa), a cell group superficially adjacent to the BMAa. PHAL-labeled axons from this cell group mainly ascend into the amygdala and olfactory areas, and descend into the thalamus and lateral hypothalamic area. Based on connections, the COAa and BMAa are part of the same functional system. The results suggest that cytoarchitectonically distinct anterior and posterior parts of the BMA are also hodologically distinct and form parts of distinct anatomical circuits probably involved in mediating different behaviors (for example, feeding and social behaviors vs. emotion-related learning, respectively).  
  Call Number Serial 38  
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Author (up) Sacha, P.; Zamecnik, J.; Barinka, C.; Hlouchova, K.; Vicha, A.; Mlcochova, P.; Hilgert, I.; Eckschlager, T.; Konvalinka, J. file  url
doi  openurl
  Title Expression of glutamate carboxypeptidase II in human brain Type Journal Article
  Year 2007 Publication Neuroscience Abbreviated Journal Neuroscience  
  Volume 144 Issue 4 Pages 1361-1372  
  Keywords Aged; Aged, 80 and over; Antibodies/immunology; Antigens, Surface/analysis/immunology/*metabolism; Astrocytes/enzymology; Blotting, Western; Brain/anatomy & histology/*enzymology; Dipeptides/*metabolism; Enzyme Activation/physiology; Epitope Mapping/methods; Female; Glutamate Carboxypeptidase II/analysis/immunology/*metabolism; Glutamic Acid/*biosynthesis; Humans; Immunohistochemistry/methods; Male; Middle Aged; Models, Molecular; Protein Structure, Tertiary/physiology; Radioligand Assay/methods; Recombinant Fusion Proteins/metabolism  
  Abstract Glutamate carboxypeptidase II (GCPII) is a transmembrane glycoprotein expressed in various tissues. When expressed in the brain it cleaves the neurotransmitter N-acetylaspartylglutamate (NAAG), yielding free glutamate. In jejunum it hydrolyzes folylpoly-gamma-glutamate, thus facilitating folate absorption. The prostate form of GCPII, known as prostate specific membrane antigen (PSMA), is an established cancer marker. The NAAG-hydrolyzing activity of GCPII has been implicated in a number of pathological conditions in which glutamate is neurotoxic (e.g. amyotrophic lateral sclerosis, Huntington's disease, Alzheimer's disease, epilepsy, schizophrenia, and stroke). Inhibition of GCPII was shown to be neuroprotective in tissue culture and in animal models. GCPII is therefore an interesting putative therapeutic target. However, only very limited and controversial data on the expression and localization of GCPII in human brain are available. Therefore, we set out to analyze the activity and expression of GCPII in various compartments of the human brain using a radiolabeled substrate of the enzyme and the novel monoclonal antibody GCP-04, which recognizes an epitope on the extracellular portion of the enzyme and is more sensitive to GCPII than to the homologous GCPIII. We show that this antibody is more sensitive in immunoblots than the widely used antibody 7E11. By Western blot, we show that there are approximately 50-300 ng of GCPII/mg of total protein in human brain, depending on the specific area. Immunohistochemical analysis revealed that astrocytes specifically express GCPII in all parts of the brain. GCPII is enzymatically active and the level of activity follows the expression pattern. Using pure recombinant GCPII and homologous GCPIII, we conclude that GCPII is responsible for the majority of overall NAAG-hydrolyzing activity in the human brain.  
  Call Number Serial 115  
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