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  • 1
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    Regulation of fasted blood glucose by resistin (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-21
    Description: The association between obesity and diabetes supports an endocrine role for the adipocyte in maintaining glucose homeostasis. Here we report that mice lacking the adipocyte hormone resistin exhibit low blood glucose levels after fasting, due to reduced hepatic glucose production. This is partly mediated by activation of adenosine monophosphate-activated protein kinase and decreased expression of gluconeogenic enzymes in the liver. The data thus support a physiological function for resistin in the maintenance of blood glucose during fasting. Remarkably, lack of resistin diminishes the increase in post-fast blood glucose normally associated with increased weight, suggesting a role for resistin in mediating hyperglycemia associated with obesity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Banerjee, Ronadip R -- Rangwala, Shamina M -- Shapiro, Jennifer S -- Rich, A Sophie -- Rhoades, Ben -- Qi, Yong -- Wang, Juan -- Rajala, Michael W -- Pocai, Alessandro -- Scherer, Phillipp E -- Steppan, Claire M -- Ahima, Rexford S -- Obici, Silvana -- Rossetti, Luciano -- Lazar, Mitchell A -- NIH T32-GM008216/GM/NIGMS NIH HHS/ -- P01 DK49210/DK/NIDDK NIH HHS/ -- P30 DK19525/DK/NIDDK NIH HHS/ -- P60 DK20541/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 20;303(5661):1195-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Endocrinology, Diabetes, and Metabolism, Department of Medicine, and The Penn Diabetes Center, 611 CRB, 415 Curie Boulevard, Universityof Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976316" target="_blank"〉PubMed〈/a〉
    Keywords: AMP-Activated Protein Kinases ; Adipocytes/metabolism ; Animals ; Blood Glucose/*metabolism ; Body Weight ; Diet ; Dietary Fats/administration & dosage ; *Fasting ; Gene Targeting ; Gluconeogenesis ; Glucose Tolerance Test ; Glucose-6-Phosphatase/metabolism ; Homeostasis ; Hormones, Ectopic/administration & dosage/blood/genetics/*physiology ; Insulin/blood ; Liver/metabolism ; Male ; Mice ; Multienzyme Complexes/metabolism ; Obesity/metabolism ; Phosphoenolpyruvate Carboxykinase (GTP)/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Recombinant Proteins/administration & dosage ; Resistin ; Signal Transduction
    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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    Disulfide-dependent multimeric assembly of resistin family hormones (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-25
    Description: Resistin, founding member of the resistin-like molecule (RELM) hormone family, is secreted selectively from adipocytes and induces liver-specific antagonism of insulin action, thus providing a potential molecular link between obesity and diabetes. Crystal structures of resistin and RELMbeta reveal an unusual multimeric structure. Each protomer comprises a carboxy-terminal disulfide-rich beta-sandwich "head" domain and an amino-terminal alpha-helical "tail" segment. The alpha-helical segments associate to form three-stranded coiled coils, and surface-exposed interchain disulfide linkages mediate the formation of tail-to-tail hexamers. Analysis of serum samples shows that resistin circulates in two distinct assembly states, likely corresponding to hexamers and trimers. Infusion of a resistin mutant, lacking the intertrimer disulfide bonds, in pancreatic-insulin clamp studies reveals substantially more potent effects on hepatic insulin sensitivity than those observed with wild-type resistin. This result suggests that processing of the intertrimer disulfide bonds may reflect an obligatory step toward activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patel, Saurabh D -- Rajala, Michael W -- Rossetti, Luciano -- Scherer, Philipp E -- Shapiro, Lawrence -- New York, N.Y. -- Science. 2004 May 21;304(5674):1154-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15155948" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/metabolism ; Adiponectin ; Amino Acid Sequence ; Animals ; Cell Line ; Crystallization ; Crystallography, X-Ray ; Culture Media, Conditioned ; Disulfides/*chemistry ; Glucose/metabolism ; Hormones, Ectopic/*chemistry/genetics/*metabolism/pharmacology ; Humans ; Insulin/administration & dosage/blood ; Insulin Resistance ; *Intercellular Signaling Peptides and Proteins ; Liver/metabolism ; Mice ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/chemistry/metabolism ; Resistin
    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
    BibTip Others were also interested in ...
    PAPER CURRENT
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