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  • 1
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    Germ cell survival through carbohydrate-mediated interaction with Sertoli cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-05
    Description: Spermatogenesis is a precisely regulated process in which the germ cells closely interact with Sertoli cells. The molecular basis of this cell-cell adhesion is unknown. Here, we demonstrate that targeted disruption of Man2a2, a gene encoding alpha-mannosidase IIx (MX), an enzyme that forms intermediate asparagine-linked carbohydrates (N-glycans), results in Man2a2 null males that are largely infertile. The Man2a2 null spermatogenic cells fail to adhere to Sertoli cells and are prematurely released from the testis to epididymis. We identified an N-glycan structure that plays a key role in germ cell-Sertoli cell adhesion and showed that a specific carbohydrate was required for spermatogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akama, Tomoya O -- Nakagawa, Hiroaki -- Sugihara, Kazuhiro -- Narisawa, Sonoko -- Ohyama, Chikara -- Nishimura, Shin-Ichiro -- O'Brien, Deborah A -- Moremen, Kelley W -- Millan, Jose Luis -- Fukuda, Michiko N -- CA 42595/CA/NCI NIH HHS/ -- CA71932/CA/NCI NIH HHS/ -- GM47533/GM/NIGMS NIH HHS/ -- HD05863/HD/NICHD NIH HHS/ -- RR05351/RR/NCRR NIH HHS/ -- U54 HD035041/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):124-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Glycobiology Program and, Stem Cell Program, The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778047" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylglucosamine/metabolism ; Animals ; Cell Adhesion ; Cell Survival ; Crosses, Genetic ; Female ; Gene Targeting ; Glycopeptides/pharmacology ; Infertility, Male/etiology ; Lectins/metabolism ; Male ; Mannosidases/genetics/*metabolism ; Mice ; Mutation ; Oligosaccharides/metabolism ; *Plant Lectins ; Polysaccharides/biosynthesis/chemistry/*metabolism ; Sertoli Cells/*metabolism ; Spermatocytes/metabolism/physiology ; *Spermatogenesis ; Spermatozoa/*metabolism/physiology ; Testis/cytology/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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    Structural basis for regulation of human calcium-sensing receptor by magnesium ions and an unexpected tryptophan derivative co-agonist (2016)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2016-05-28
    Description: Ca 2+ -sensing receptors (CaSRs) modulate calcium and magnesium homeostasis and many (patho)physiological processes by responding to extracellular stimuli, including divalent cations and amino acids. We report the first crystal structure of the extracellular domain (ECD) of human CaSR bound with Mg 2+ and a tryptophan derivative ligand at 2.1 Å. The structure reveals key determinants for cooperative activation by metal ions and aromatic amino acids. The unexpected tryptophan derivative was bound in the hinge region between two globular ECD subdomains, and represents a novel high-affinity co-agonist of CaSR. The dissection of structure-function relations by mutagenesis, biochemical, and functional studies provides insights into the molecular basis of human diseases arising from CaSR mutations. The data also provide a novel paradigm for understanding the mechanism of CaSR-mediated signaling that is likely shared by the other family C GPCR [G protein (heterotrimeric guanine nucleotide–binding protein)–coupled receptor] members and can facilitate the development of novel CaSR-based therapeutics.
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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