The isolation of nerve endings from brain: An electron microscopic study of cell fragments derived by homogenization and centrifugation

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The isolation of nerve endings from brain: An electron microscopic study of cell fragments derived by homogenization and centrifugation

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The isolation of nerve endings from brain: An electron microscopic study of cell fragments derived by homogenization and centrifugation

01 Jan 1962-Journal of Anatomy (Wiley-Blackwell)-Vol. 96, pp 79-88

About: This article is published in Journal of Anatomy.The article was published on 1962-01-01 and is currently open access. It has received 2490 citations till now. The article focuses on the topics: Homogenization (biology).

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Microglia Promote Learning-Dependent Synapse Formation through Brain-Derived Neurotrophic Factor

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Christopher N. Parkhurst¹, Guang Yang¹, Ipe Ninan¹, Jeffrey N. Savas², John R. Yates², Juan J. Lafaille¹, Barbara L. Hempstead³, Dan R. Littman¹, Wen-Biao Gan¹ - Show less +5 more•Institutions (3)

New York University¹, Scripps Research Institute², Cornell University³

19 Dec 2013-Cell

TL;DR: It is found that microglia could be specifically depleted from the brain upon diphtheria toxin administration and removal of brain-derived neurotrophic factor (BDNF) frommicroglia largely recapitulated the effects of microglian depletion.

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1,890 citations

Cites methods from "The isolation of nerve endings from..."

...Isolation of Synaptosome Fractions and Western Blot Mice were deeply anesthetized and perfused with 40 ml of Ca2+/Mg2+-free Dulbecco’s PBS. Brain tissue was removed and synaptosomes were isolated as previously described (Gray and Whittaker, 1962)....
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...Brain tissue was removed and synaptosomes were isolated as previously described (Gray and Whittaker, 1962)....
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Journal Article•DOI•

Two genes encode distinct glutamate decarboxylases.

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Mark G. Erlander¹, Niranjala J.K. Tillakaratne¹, Sophie Feldblum¹, Neela Patel¹, Allan J. Tobin¹ - Show less +1 more•Institutions (1)

University of California, Los Angeles¹

01 Jul 1991-Neuron

TL;DR: The brain contains two forms of the GABA synthetic enzyme glutamate decarboxylase (GAD), which differ in molecular size, amino acid sequence, antigenicity, cellular and subcellular location, and interaction with the GAD cofactor pyridoxal phosphate.

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1,198 citations

Cites background from "The isolation of nerve endings from..."

...…have different subcellular distributions, we examined the relative levels of each GAD in two subcellular fractions-&, a high speed supernatant consisting of the cytosol of all cells in the brain, and the synaptosomal fraction, which consists primarily of nerve endings (Gray and Whittaker, 1962)....
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Journal Article•DOI•

Calcium-dependent activation of a multifunctional protein kinase by membrane phospholipids.

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Yoshimi Takai, Akira Kishimoto, Y Iwasa, Y Kawahara, Taisuke Mori, Yasutomi Nishizuka - Show less +2 more

25 May 1979-Journal of Biological Chemistry

TL;DR: The proenzyme of a Ca2+-dependent protease-activated protein kinase previously obtained from mammalian tissues showed an ability to phosphorylate five histone fractions and muscle phosphorylase kinase, and appeared to possess multifunctional catalytic activities.

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1,068 citations

Journal Article•DOI•

Calcium-activated, phospholipid-dependent protein kinase from rat brain. Subcellular distribution, purification, and properties.

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Ushio Kikkawa, Y Takai, Ryoji Minakuchi, S Inohara, Yasutomi Nishizuka - Show less +1 more

25 Nov 1982-Journal of Biological Chemistry

TL;DR: The subcellular distribution of Ca2+-activated, phospholipid-dependent protein kinase in rat brain was investigated and most of the enzyme was found to be associated with synaptosomal membranes, indistinguishable from the cytosol protein Kinase in physical, kinetic, and catalytic properties.

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936 citations

Journal Article•DOI•

Identification of a transmembrane glycoprotein specific for secretory vesicles of neural and endocrine cells.

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K Buckley, R B Kelly

01 Apr 1985-Journal of Cell Biology

TL;DR: A transmembrane glycoprotein (Mr approximately 100,000) is described that is present in secretory vesicles in all neurons and endocrine cells studied, in species from elasmobranch fish to mammals, and in neural andendocrine cell lines.

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Abstract: Several types of cells store proteins in secretory vesicles from which they are released by an appropriate stimulus. It might be expected that the secretory vesicles in different cell types use similar molecular machinery. Here we describe a transmembrane glycoprotein (Mr approximately 100,000) that is present in secretory vesicles in all neurons and endocrine cells studied, in species from elasmobranch fish to mammals, and in neural and endocrine cell lines. It was detected by cross-reactivity with monoclonal antibodies raised to highly purified cholinergic synaptic vesicles from the electric organ of fish. By immunoprecipitation of intact synaptic vesicles and electron microscopic immunoperoxidase labeling, we have shown that the antigenic determinant is on the cytoplasmic face of the synaptic vesicles. However, the electrophoretic mobility of the antigen synthesized in the presence of tunicamycin is reduced to Mr approximately 62,000, which suggests that the antigen is glycosylated and must therefore span the vesicle membrane.

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701 citations