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    Modulating sphingolipid biosynthetic pathway rescues photoreceptor degeneration (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-15
    Description: Mutations in proteins of the Drosophila phototransduction cascade, a prototypic guanine nucleotide-binding protein-coupled receptor signaling system, lead to retinal degeneration and have been used as models to understand human degenerative disorders. Here, modulating the sphingolipid biosynthetic pathway rescued retinal degeneration in Drosophila mutants. Targeted expression of Drosophila neutral ceramidase rescued retinal degeneration in arrestin and phospholipase C mutants. Decreasing flux through the de novo sphingolipid biosynthetic pathway also suppressed degeneration in these mutants. Both genetic backgrounds modulated the endocytic machinery because they suppressed defects in a dynamin mutant. Suppression of degeneration in arrestin mutant flies expressing ceramidase correlated with a decrease in ceramide levels. Thus, enzymes of sphingolipid metabolism may be suitable targets in the therapeutic management of retinal degeneration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Acharya, Usha -- Patel, Shetal -- Koundakjian, Edmund -- Nagashima, Kunio -- Han, Xianlin -- Acharya, Jairaj K -- New York, N.Y. -- Science. 2003 Mar 14;299(5613):1740-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regulation of Cell Growth Laboratory, National Cancer Institute-Frederick, Frederick, MD 21702, USA. acharyau@mail.ncifcrf.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12637747" target="_blank"〉PubMed〈/a〉
    Keywords: Acyltransferases/genetics/metabolism ; Amidohydrolases/genetics/*metabolism ; Animals ; Animals, Genetically Modified ; Apoptosis ; Arrestins/genetics/metabolism ; Ceramidases ; Ceramides/biosynthesis/*metabolism ; Clathrin/physiology ; Cloning, Molecular ; Crosses, Genetic ; Drosophila/genetics/*physiology ; Dynamins/genetics/physiology ; Electroretinography ; *Endocytosis ; Genes, Insect ; Light ; Mutation ; Necrosis ; Neutral Ceramidase ; Phosphatidylinositol Diacylglycerol-Lyase ; Phosphoproteins/genetics/metabolism ; Photoreceptor Cells, Invertebrate/cytology/*physiology/ultrastructure ; Receptors, Cell Surface/metabolism ; Retinal Degeneration/genetics ; Rhodopsin/metabolism ; Serine C-Palmitoyltransferase ; Spectrometry, Mass, Electrospray Ionization ; Sphingosine/metabolism ; Type C Phospholipases/genetics/metabolism ; *Vision, Ocular
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Transmembrane segments of syntaxin line the fusion pore of Ca2+-triggered exocytosis (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-16
    Description: The fusion pore of regulated exocytosis is a channel that connects and spans the vesicle and plasma membranes. The molecular composition of this important intermediate structure of exocytosis is unknown. Here, we found that mutations of some residues within the transmembrane segment of syntaxin (Syx), a plasma membrane protein essential for exocytosis, altered neurotransmitter flux through fusion pores and altered pore conductance. The residues that influenced fusion-pore flux lay along one face of an alpha-helical model. Thus, the fusion pore is formed at least in part by a circular arrangement of 5 to 8 Syx transmembrane segments in the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, Xue -- Wang, Chih-Tien -- Bai, Jihong -- Chapman, Edwin R -- Jackson, Meyer B -- GM56827/GM/NIGMS NIH HHS/ -- MH61876/MH/NIMH NIH HHS/ -- NS30016/NS/NINDS NIH HHS/ -- NS44057/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Apr 9;304(5668):289-92. Epub 2004 Mar 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Wisconsin, 1300 University Avenue, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15016962" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Cell Membrane Structures/*chemistry/metabolism ; Electric Capacitance ; Electric Conductivity ; Electrophysiology ; *Exocytosis ; Membrane Fusion ; Membrane Proteins/*chemistry/genetics/*metabolism ; Models, Biological ; Mutation ; Neurons/*physiology ; Norepinephrine/metabolism ; PC12 Cells ; Patch-Clamp Techniques ; Protein Structure, Secondary ; Qa-SNARE Proteins ; Rats ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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