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RAPIDLY TRANSPORTED PROTEINS IN SENSORY, MOTOR AND SYMPATHETIC-NERVES OF ISOLATED FROG NERVOUS-SYSTEM

BRAIN RESEARCH 1976年第3期105卷 497-515页

作者： BARKER, JL NEALE, JH GAINER, H NICHHD BEHAV BIOL BRANCH BETHESDA MD 20014 USA

The synthesis and rapid axonal transport of [35S]methionine-labeled proteins was studied using the isolated frog spinal cord and peripheral nervous system. Polyacrylamide gel electrophoresis in sodium dodecylsulfate of synthesized and transported proteins revealed similar labeling patterns of proteins transported in the sensory, motor and sympathetic systems. The relative labeling pattern of transported proteins which accumulated at ligatures in peripheral nerves was different from those obtained from ganglia or nerves and roots when they were incubated in labeled methionine. When compared with methionine-labeled protein profiles of rapid axonal transport in other species and systems, a common set of rapidly transported proteins emerges. The approximate molecular weights of these common proteins include (in 1000 daltons): 18, 24-29, 34-36, 57, 65-68, 100 and 130. These proteins may represent fundamental macromolecules involved in the general maintenance of the function of nerve processes.

关键词：自主神经纤维节后/代谢生物转运神经节脊/代谢甲硫氨酸/代谢运动神经元/代谢神经组织蛋白质类/生物合成神经组织蛋白质类/代谢神经胶质/代谢神经元传入/代谢周围神经/代谢蛙牛感觉脊髓/代谢脊神经根/代谢交感神经系统/代谢动物

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FGF-2 potentiates Ca²⁺-dependent inactivation of NMDA receptor currents in hippocampal neurons

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JOURNAL OF NEUROPHYSIOLOGY 1999年第6期82卷 3367-3377页

作者： Boxer, AL Moreno, H Rudy, B Ziff, EB NYU Med Ctr Dept Biochem Howard Hughes Med Inst New York NY 10016 USA NYU Med Ctr Dept Physiol & Neurosci New York NY 10016 USA

Peptide growth factors such as the neurotrophins and fibroblast growth factors have potent effects on synaptic transmission, development, and cell survival. We report that chronic (hours) treatment with basic fibroblast growth factor (FGF-2) potentiates Ca2+-dependent N-methyl-D-aspartate (NMDA) receptor inactivation in cultured hippocampal neurons. This effect is specific for the NMDA-subtype of ionotropic glutamate receptor and FGF-2. The potentiated inactivation requires ongoing protein synthesis during growth factor treatment and the activity of protein phosphatase 2B (PP2B or calcineurin) during agonist application. These results suggest a mechanism by which FGF-2 receptor signaling may regulate neuronal survival and synaptic plasticity.

关键词：辅肌动蛋白/生理学钙神经素/代谢钙/生理学钙通道/生理学细胞培养的电刺激电生理学成纤维细胞生长因子2/药理学海马/细胞学海马/药物作用免疫组织化学离子通道闸门/药物作用膜电位/生理学神经组织蛋白质类/代谢神经元/药物作用膜片钳术 RNA 信使/生物合成大鼠 Sprague-Dawley 受体 N-甲基-D-天冬氨酸/拮抗剂和抑制剂逆转录聚合酶链反应动物大鼠

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Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation

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NEURON 1999年第2期24卷 481-489页

作者： Hiesberger, T Trommsdorff, M Howell, BW Goffinet, A Mumby, MC Cooper, JA Herz, J Univ Texas SW Med Ctr Dept Mol Genet Dallas TX 75235 USA Univ Texas SW Med Ctr Dept Pharmacol Dallas TX 75235 USA Fred Hutchinson Canc Res Ctr Seattle WA 98109 USA Univ Namur Sch Med Neurobiol Unit B-5000 Namur Belgium

The large extracellular matrix protein Reelin is produced by Cajal-Retzius neurons in specific regions of the developing brain, where it controls neuronal migration and positioning. Genetic evidence suggests that interpretation of the Reelin signal by migrating neurons involves two neuronal cell surface proteins, the very low density lipoprotein receptor (VLDLR) and the apoE receptor 2 (ApoER2) as well as a cytosolic adaptor protein, Disabled-1 (Dab1). We show that Reelin binds directly and specifically to the ectodomains of VLDLR and ApoER2 in vitro and that blockade of VLDLR and ApoER2 correlates with loss of Reelin-induced tyrosine phosphorylation of Disabled-1 in cultured primary embryonic neurons. Furthermore, mice that lack either Reelin or both VLDLR and ApoER2 exhibit hyperphosphorylation of the microtubule-stabilizing protein tau. Taken together, these findings suggest that Reelin acts via VLDLR and ApoER2 to regulate Disabled-1 tyrosine phosphorylation and microtubule function in neurons.

关键词：细胞黏附分子神经元/遗传学细胞黏附分子神经元/代谢细胞外基质蛋白质类/遗传学细胞外基质蛋白质类/代谢低密度脂蛋白受体相关蛋白-1 小鼠基因敲除/遗传学神经组织蛋白质类/代谢磷酰化蛋白质亚型/代谢受体 LDL/遗传学受体 LDL/代谢受体脂蛋白/遗传学受体脂蛋白/代谢丝氨酸内肽酶类酪氨酸/代谢 tau蛋白质类/代谢动物人类小鼠

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The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids

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MOLECULAR AND CELLULAR BIOLOGY 1999年第7期19卷 5179-5188页

作者： Howell, BW Lanier, LM Frank, R Gertler, FB Cooper, JA Fred Hutchinson Canc Res Ctr Seattle WA 98109 USA MIT Cambridge MA 02139 USA GBF AG Mol Recognit D-38124 Braunschweig Germany

Disabled gene products are important for nervous system development in drosophila and mammals. In mice, the Dab1 protein is thought to function downstream of the extracellular protein Reln during neuronal positioning. The structures of Dab proteins suggest that they mediate protein-protein or protein-membrane docking functions. Here we show that the amino-terminal phosphotyrosine-binding (PTB) domain of Dab1 binds to the transmembrane glycoproteins of the amyloid precursor protein (APP) and low-density lipoprotein receptor families and the cytoplasmic signaling protein Ship. Dab1 associates with the APP cytoplasmic domain in transfected cells and is coexpressed with APP in hippocampal neurons. Screening of a set of altered peptide sequences showed that the sequence GYXNPXY present in APP family members is an optimal binding sequence, with approximately 0.5 mu M affinity. Unlike other PTB domains, the Dab1 PTB does not bind to tyrosine-phosphorylated peptide ligands. The PTB domain also binds specifically to phospholipid bilayers containing phosphatidylinositol 4P (PtdIns4P) or PtdIns4,5P(2) in a manner that does not interfere with protein binding. We propose that the PTB domain permits Dab1 to bind specifically to transmembrane proteins containing an NPXY internalization signal.

关键词：氨基酸序列淀粉样β蛋白前体/化学淀粉样β蛋白前体/代谢结合部位克隆分子细胞质/代谢糖蛋白类/代谢 HeLa细胞配体膜糖蛋白类/代谢膜脂质类/代谢分子序列数据神经组织蛋白质类/遗传学神经组织蛋白质类/代谢肽类/代谢磷脂酰肌醇类/代谢磷脂类/代谢磷酸单酯水解酶类/代谢磷酰化磷酸酪氨酸/代谢受体 LDL/代谢重组融合蛋白质类/遗传学重组融合蛋白质类/代谢酿酒酵母菌亚细胞部分肿瘤细胞培养的动物人类小鼠

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Nuclear localization of the spinocerebellar ataxia type 7 protein, ataxin-7

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HUMAN MOLECULAR GENETICS 1999年第9期8卷 1657-1664页

作者： Kaytor, MD Duvick, LA Skinner, PJ Koob, MD Ranum, LPW Orr, HT Univ Minnesota Inst Human Genet Minneapolis MN 55455 USA Univ Minnesota Dept Lab Med & Pathol Minneapolis MN 55455 USA Univ Minnesota Dept Neurol Minneapolis MN 55455 USA Univ Minnesota Dept Biochem Minneapolis MN 55455 USA

Spinocerebellar ataxia type 7 (SCA7) belongs to a group of neurological disorders caused by a CAG repeat expansion in the coding region of the. associated gene. To gain insight into the pathogenesis of SCA7 and possible functions of ataxin-7, we examined the subcellular localization of ataxin-7 in transfected COS-1 cells using SCA7 cDNA clones with different CAG repeat tract lengths, In addition to a diffuse distribution throughout the nucleus, ataxin-7 associated with the nuclear matrix and the nucleolus. The location of the putative SCA7 nuclear localization sequence (NLS) was confirmed by fusing an ataxin-7 fragment with the normally cytoplasmic protein chicken muscle pyruvate kinase, Mutation of this NLS prevented protein from entering the nucleus. Thus, expanded ataxin-7 may carry out its pathogenic effects in the nucleus by altering a matrix-associated nuclear structure and/or by disrupting nucleolar function.

关键词： COS细胞荧光抗体技术肿瘤蛋白质类/代谢神经组织蛋白质类/遗传学神经组织蛋白质类/代谢核定位信号/遗传学核基质/代谢核蛋白质类/代谢丙酮酸激酶/代谢重组融合蛋白质类/代谢脊髓小脑共济失调/遗传学转录因子/代谢转染肿瘤抑制蛋白质类动物人类

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Squeezing axons out of the gray matter: A role for slit and semaphorin proteins from midline and ventral spinal cord

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CELL 2000年第3期102卷 363-375页

作者： Zoo, YM Stoeckli, E Chen, H Tessier-Lavigne, M Univ Calif San Francisco Howard Hughes Med Inst Dept Anat San Francisco CA 94143 USA Univ Calif San Francisco Howard Hughes Med Inst Dept Biochem & Biophys San Francisco CA 94143 USA Univ Basel Dept Integrat Biol CH-4051 Basel Switzerland

Commissural axons cross the nervous system midline and then turn to grow alongside it, neither recrossing nor projecting back into ventral regions. In Drosophila, the midline repellent Slit prevents recrossing: axons cross once because they are initially unresponsive to Slit, becoming responsive only upon crossing. We show that commissural axons in mammals similarly acquire responsiveness to a midline repellent activity upon crossing. Remarkably, they also become responsive to a repellent activity from ventral spinal cord, helping explain why they never reenter that region. Several Slit and Semaphorin proteins, expressed in midline and/or ventral tissues, mimic these repellent activities, and midline guidance defects are observed in mice lacking neuropilin-2, a Semaphorin receptor. Thus, Slit and Semaphorin repellents from midline and nonmidline tissues may help prevent crossing axons from reentering gray matter, squeezing them into surrounding fiber tracts.

关键词：轴突细胞间通讯果蝇蛋白质类胞间信号肽类和蛋白质类分子序列数据形态发生神经组织蛋白质类/代谢神经通路/细胞学神经通路/胚胎学神经纤毛蛋白质1 脊髓/细胞学脊髓/胚胎学动物大鼠

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Selective insolubility of α-Synuclein in human Lewy body diseases is recapitulated in a transgenic mouse model

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AMERICAN JOURNAL OF PATHOLOGY 2001年第6期159卷 2215-2225页

作者： Kahle, PJ Neumann, M Ozmen, L Müller, V Odoy, S Okamoto, N Jacobsen, H Iwatsubo, T Trojanowski, JQ Takahashi, H Wakabayashi, K Bogdanovic, N Riederer, P Kretzschmar, HA Haass, C Univ Munich Dept Biochem Lab Alzheimers & Parkinsons Dis Res D-80336 Munich Germany Univ Munich Dept Neuropathol D-80336 Munich Germany F Hoffmann La Roche & Co Ltd Pharma Res Genomics CH-4002 Basel Switzerland Univ Tokyo Grad Sch Pharmaceut Sci Dept Neuropathol & Neurosci Tokyo Japan Univ Penn Sch Med Dept Pathol & Lab Med Ctr Neurodegenerat Dis Res Philadelphia PA 19104 USA Niigata Univ Dept Pathol Brain Res Inst Niigata Japan Hirosaki Univ Sch Med Inst Brain Sci Dept Neuropathol Hirosaki Aomori 036 Japan Huddinge Brain Bank Geriatr Sect Dept Clin Neurosci Huddinge Sweden Univ Wurzburg Dept Psychiat Wurzburg Germany Univ Wurzburg Natl Parkinson Fdn Ctr Excellence Res Labs Wurzburg Germany

alpha -Synuclein (alpha -SYN) is deposited in intraneuronal cytoplasmic inclusions (Lewy bodies, LBs) characteristic for Parkinson's disease (PD) and LB dementias. alpha -SYN forms LB-like fibrils in vitro, in contrast to its homologue beta -SYN. Here we have investigated the solubility of SYNs in human LB diseases and in transgenic mice expressing human wild-type and PD-associated mutant [A30P]alpha -SYN driven by the brain neuron-specific promoter, Thy1. Distinct alpha -SYN species were detected in the detergent-insoluble fractions from brains of patients with PD, dementia with LBs, and neurodegeneration with brain iron accumulation type 1 (formerly known as Hallervorden-Spatz disease). Using the same extraction method, detergent-insolubility of human alpha -SYN was observed in brains of transgenic mice. In contrast, neither endogenous mouse alpha -SYN nor beta -SYN were detected in detergent-insoluble fractions from transgenic mouse brains. The nonamyloidogenic beta -SYN was incapable of forming insoluble fibrils because amino acids 73 to 83 in the central region of alpha -SYN are absent in beta -SYN. In conclusion, the specific accumulation of detergent-insoluble alpha -SYN in transgenic mice recapitulates a pivotal feature of human LB diseases.

关键词：氨基酸类/遗传学结合部位/遗传学印迹法蛋白质脑/代谢脑/病理学洗涤剂疾病模型动物 Lewy体病/遗传学 Lewy体病/代谢 Lewy体病/病理学小鼠近交C57BL 小鼠转基因神经组织蛋白质类/遗传学神经组织蛋白质类/代谢溶解度亚细胞部分突触体/代谢突触核蛋白类 α突触核蛋白动物人类小鼠

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Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein

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HUMAN MOLECULAR GENETICS 2000年第15期9卷 2305-2312页

作者： Davidson, JD Riley, B Burright, EN Duvick, LA Zoghbi, HY Orr, HT Univ Minnesota Dept Genet Cell Biol & Dev Minneapolis MN 55455 USA Univ Minnesota Dept Lab Med & Pathol Minneapolis MN 55455 USA Univ Minnesota Dept Biochem Mol Biol & Biophys Minneapolis MN 55455 USA Univ Minnesota Inst Human Genet Minneapolis MN 55455 USA Baylor Coll Med Howard Hughes Med Inst Dept Mol & Human Genet Houston TX 77030 USA

Expansion of a polyglutamine tract within ataxin-1 causes spinocerebellar ataxia type 1 (SCA1). In this study, we used the yeast two-hybrid system to identify an ataxin-1-interacting protein, A1Up. A1Up localized to the nucleus and cytoplasm of transfected COS-1 cells. In the nucleus, A1Up co-localized with mutant ataxin-1, further demonstrating that A1Up interacts with ataxin-1. Expression analyses demonstrated that A1U mRNA is widely expressed as an similar to 4.0 kb transcript and is present in Purkinje cells, the primary site of SCA1 cerebellar pathology. Sequence comparisons revealed that A1Up contains;an N-terminal ubiquitin-like (UbL) region, placing it within a large family of similar proteins. In addition, A1Up has substantial homology to human Chap1/Dsk2, a protein that binds the ATPase domain of the HSP70-like Stch protein. These results suggest that A1Up may link ataxin-1 with the chaperone and ubiquitin-proteasome pathways. In addition, these data support the concept that ataxin-1 may function in the formation and regulation of multimeric protein complexes within the nucleus.

关键词：氨基酸序列印迹法 RNA 脑/代谢 COS细胞载体蛋白质类细胞周期蛋白质类/遗传学荧光抗体技术原位杂交分子序列数据神经组织蛋白质类/代谢核蛋白质类/遗传学核蛋白质类/代谢器官特异性蛋白质结合 RNA 信使/分析序列同源性氨基酸双杂交系统技术泛素类/遗传学动物人类小鼠

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A close association of torsinA and α-synuclein in Lewy bodies -: A fluorescence resonance energy transfer study

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AMERICAN JOURNAL OF PATHOLOGY 2001年第1期159卷 339-344页

作者： Sharma, N Hewett, J Ozelius, LJ Ramesh, V McLean, PJ Breakefield, XO Hyman, BT Massachusetts Gen Hosp E Alzheimers Dis Res Unit Dept Neurol Charlestown MA 02129 USA Massachusetts Gen Hosp E Mol Neurogenet Unit Dept Neurol Charlestown MA 02129 USA Albert Einstein Coll Med Dept Mol Genet Bronx NY 10467 USA

TorsinA, a novel protein In which a mutation causes dominant, early onset torsion dystonia, may serve as a chaperone for misfolded proteins that require refolding or degradation. It has been hypothesized that misfolded alpha -synuclein, a protein in which two mutations cause autosomal dominantly inherited Parkinson's disease, serves as a nidus for the development of a Lewy body. We hypothesized that torsinA plays a role in the cellular processing of alpha -synuclein. We demonstrate that anti-torsin antibodies stain Lewy bodies and Lewy neurites in the substantia nigra and cortex. Using sensitive fluorescent resonance energy transfer (FRET) techniques, we find evidence of a close association between torsinA and alpha -synuclein in Lewy bodies.

关键词：载体蛋白质类能量传递海马/代谢免疫组织化学 Lewy体/代谢 Lewy体病/代谢显微镜检查共焦分子伴侣神经组织蛋白质类/代谢参考值光谱法荧光黑质/代谢突触核蛋白类 α突触核蛋白人类

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TUBULIN NUCLEOTIDE REACTIONS AND THEIR ROLE IN MICROTUBULE ASSEMBLY AND DISSOCIATION

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ANNALS OF THE NEW YORK ACADEMY OF SCIENCES 1975年第JUN30期253卷 562-572页

作者： JACOBS, M KINGS COLL MRC MUSCLE BIOPHYS UNIT LONDON WC2 ENGLAND

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