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  • COS Cells  (2)
  • American Association for the Advancement of Science (AAAS)  (2)
  • American Physical Society
  • International Union of Crystallography (IUC)
  • Springer Nature
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Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (2)
  • American Physical Society
  • International Union of Crystallography (IUC)
  • Springer Nature
Years
  • 1
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    A membrane receptor for retinol binding protein mediates cellular uptake of vitamin A (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-01-27
    Description: Vitamin A has diverse biological functions. It is transported in the blood as a complex with retinol binding protein (RBP), but the molecular mechanism by which vitamin A is absorbed by cells from the vitamin A-RBP complex is not clearly understood. We identified in bovine retinal pigment epithelium cells STRA6, a multitransmembrane domain protein, as a specific membrane receptor for RBP. STRA6 binds to RBP with high affinity and has robust vitamin A uptake activity from the vitamin A-RBP complex. It is widely expressed in embryonic development and in adult organ systems. The RBP receptor represents a major physiological mediator of cellular vitamin A uptake.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawaguchi, Riki -- Yu, Jiamei -- Honda, Jane -- Hu, Jane -- Whitelegge, Julian -- Ping, Peipei -- Wiita, Patrick -- Bok, Dean -- Sun, Hui -- 5T32EY07026/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2007 Feb 9;315(5813):820-5. Epub 2007 Jan 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, David Geffen School of Medicine at UCLA, 650 Charles E. Young Drive South, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17255476" target="_blank"〉PubMed〈/a〉
    Keywords: Acyltransferases/metabolism ; Amino Acid Sequence ; Animals ; Blood-Retinal Barrier ; COS Cells ; Cattle ; Cell Line ; Cell Line, Tumor ; Cell Membrane/metabolism ; Cercopithecus aethiops ; Embryonic Development ; Endocytosis ; Humans ; Molecular Sequence Data ; Mutation, Missense ; Pigment Epithelium of Eye/*metabolism ; Placenta/metabolism ; Receptors, Cell Surface/*metabolism ; Retinal Vessels/metabolism ; Retinol-Binding Proteins/*metabolism ; Spleen/metabolism ; Transfection ; Vitamin A/*metabolism
    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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    KCNQ1 gain-of-function mutation in familial atrial fibrillation (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-11
    Description: Atrial fibrillation (AF) is a common cardiac arrhythmia whose molecular etiology is poorly understood. We studied a family with hereditary persistent AF and identified the causative mutation (S140G) in the KCNQ1 (KvLQT1) gene on chromosome 11p15.5. The KCNQ1 gene encodes the pore-forming alpha subunit of the cardiac I(Ks) channel (KCNQ1/KCNE1), the KCNQ1/KCNE2 and the KCNQ1/KCNE3 potassium channels. Functional analysis of the S140G mutant revealed a gain-of-function effect on the KCNQ1/KCNE1 and the KCNQ1/KCNE2 currents, which contrasts with the dominant negative or loss-of-function effects of the KCNQ1 mutations previously identified in patients with long QT syndrome. Thus, the S140G mutation is likely to initiate and maintain AF by reducing action potential duration and effective refractory period in atrial myocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Yi-Han -- Xu, Shi-Jie -- Bendahhou, Said -- Wang, Xiao-Liang -- Wang, Ying -- Xu, Wen-Yuan -- Jin, Hong-Wei -- Sun, Hao -- Su, Xiao-Yan -- Zhuang, Qi-Nan -- Yang, Yi-Qing -- Li, Yue-Bin -- Liu, Yi -- Xu, Hong-Ju -- Li, Xiao-Fei -- Ma, Ning -- Mou, Chun-Ping -- Chen, Zhu -- Barhanin, Jacques -- Huang, Wei -- New York, N.Y. -- Science. 2003 Jan 10;299(5604):251-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cardiology, Tongji Hospital, and Institute of Medical Genetics, Tongji University, 399 Xin Cun Road, Shanghai 200065, People's Republic of China. drchen@public7.sta.net.cn〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12522251" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Adolescent ; Adult ; Aged ; Animals ; Atrial Fibrillation/*genetics/physiopathology ; COS Cells ; Child ; China ; Chromosomes, Human, Pair 11/genetics ; Electrocardiography ; Female ; Haplotypes ; Heart Atria/physiopathology ; Heart Ventricles/physiopathology ; Humans ; KCNQ Potassium Channels ; KCNQ1 Potassium Channel ; Lod Score ; Long QT Syndrome/genetics/physiopathology ; Male ; Microsatellite Repeats ; Middle Aged ; Mutation ; *Mutation, Missense ; Myocytes, Cardiac/*physiology ; Patch-Clamp Techniques ; Pedigree ; Potassium Channels/*genetics/physiology ; *Potassium Channels, Voltage-Gated
    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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    PAPER CURRENT
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